Ignet

Gene Information

Gene symbol: NCK1

Gene name: NCK adaptor protein 1

HGNC ID: 7664

Synonyms: NCKalpha

Related Genes

#	Gene Symbol	Number of hits
1	ACTN4	1 hits
2	AGT	1 hits
3	BCAR1	1 hits
4	CBL	1 hits
5	CD2	1 hits
6	CD2AP	1 hits
7	IQGAP1	1 hits
8	JUP	1 hits
9	LATS1	1 hits
10	MAGI1	1 hits
11	NCK2	1 hits
12	NPHS1	1 hits
13	NPHS2	1 hits
14	PAK1	1 hits
15	RHOA	1 hits
16	RPS27A	1 hits
17	SH3YL1	1 hits
18	SYNPO	1 hits
19	TICAM2	1 hits
20	WAS	1 hits
21	WASL	1 hits
22	WTIP	1 hits

Related Sentences

#	PMID	Sentence
1	16525419	Nck adaptor proteins link nephrin to the actin cytoskeleton of kidney podocytes.
2	16525419	Here we show that nephrin selectively binds the Src homology 2 (SH2)/SH3 domain-containing Nck adaptor proteins, which in turn control the podocyte cytoskeleton in vivo.
3	16525419	The cytoplasmic tail of nephrin has multiple YDxV sites that form preferred binding motifs for the Nck SH2 domain once phosphorylated by Src-family kinases.
4	16525419	We show that this Nck-nephrin interaction is required for nephrin-dependent actin reorganization.
5	16525419	Together, these findings identify a physiological signalling pathway in which nephrin is linked through phosphotyrosine-based interactions to Nck adaptors, and thus to the underlying actin cytoskeleton in podocytes.
6	16525419	Nck adaptor proteins link nephrin to the actin cytoskeleton of kidney podocytes.
7	16525419	Here we show that nephrin selectively binds the Src homology 2 (SH2)/SH3 domain-containing Nck adaptor proteins, which in turn control the podocyte cytoskeleton in vivo.
8	16525419	The cytoplasmic tail of nephrin has multiple YDxV sites that form preferred binding motifs for the Nck SH2 domain once phosphorylated by Src-family kinases.
9	16525419	We show that this Nck-nephrin interaction is required for nephrin-dependent actin reorganization.
10	16525419	Together, these findings identify a physiological signalling pathway in which nephrin is linked through phosphotyrosine-based interactions to Nck adaptors, and thus to the underlying actin cytoskeleton in podocytes.
11	16525419	Nck adaptor proteins link nephrin to the actin cytoskeleton of kidney podocytes.
12	16525419	Here we show that nephrin selectively binds the Src homology 2 (SH2)/SH3 domain-containing Nck adaptor proteins, which in turn control the podocyte cytoskeleton in vivo.
13	16525419	The cytoplasmic tail of nephrin has multiple YDxV sites that form preferred binding motifs for the Nck SH2 domain once phosphorylated by Src-family kinases.
14	16525419	We show that this Nck-nephrin interaction is required for nephrin-dependent actin reorganization.
15	16525419	Together, these findings identify a physiological signalling pathway in which nephrin is linked through phosphotyrosine-based interactions to Nck adaptors, and thus to the underlying actin cytoskeleton in podocytes.
16	16525419	Nck adaptor proteins link nephrin to the actin cytoskeleton of kidney podocytes.
17	16525419	Here we show that nephrin selectively binds the Src homology 2 (SH2)/SH3 domain-containing Nck adaptor proteins, which in turn control the podocyte cytoskeleton in vivo.
18	16525419	The cytoplasmic tail of nephrin has multiple YDxV sites that form preferred binding motifs for the Nck SH2 domain once phosphorylated by Src-family kinases.
19	16525419	We show that this Nck-nephrin interaction is required for nephrin-dependent actin reorganization.
20	16525419	Together, these findings identify a physiological signalling pathway in which nephrin is linked through phosphotyrosine-based interactions to Nck adaptors, and thus to the underlying actin cytoskeleton in podocytes.
21	16525419	Nck adaptor proteins link nephrin to the actin cytoskeleton of kidney podocytes.
22	16525419	Here we show that nephrin selectively binds the Src homology 2 (SH2)/SH3 domain-containing Nck adaptor proteins, which in turn control the podocyte cytoskeleton in vivo.
23	16525419	The cytoplasmic tail of nephrin has multiple YDxV sites that form preferred binding motifs for the Nck SH2 domain once phosphorylated by Src-family kinases.
24	16525419	We show that this Nck-nephrin interaction is required for nephrin-dependent actin reorganization.
25	16525419	Together, these findings identify a physiological signalling pathway in which nephrin is linked through phosphotyrosine-based interactions to Nck adaptors, and thus to the underlying actin cytoskeleton in podocytes.
26	16543952	Nephrin ectodomain engagement results in Src kinase activation, nephrin phosphorylation, Nck recruitment, and actin polymerization.
27	16543952	We found that this nephrin phosphorylation event resulted in recruitment of the SH2-SH3 domain-containing adapter protein Nck and assembly of actin filaments in an Nck-dependent fashion.
28	16543952	Nephrin ectodomain engagement results in Src kinase activation, nephrin phosphorylation, Nck recruitment, and actin polymerization.
29	16543952	We found that this nephrin phosphorylation event resulted in recruitment of the SH2-SH3 domain-containing adapter protein Nck and assembly of actin filaments in an Nck-dependent fashion.
30	16630808	Nck links nephrin to actin in kidney podocytes.
31	16630808	Two papers, one in Nature (Jones et al., 2006) and the other in the Journal of Clinical Investigation (Verma et al., 2006) show that Nck adaptor proteins connect phosphorylated nephrin with actin polymerization in podocyte foot processes, structures important for slit-diaphragm formation in the kidney.
32	16630808	Nck links nephrin to actin in kidney podocytes.
33	16630808	Two papers, one in Nature (Jones et al., 2006) and the other in the Journal of Clinical Investigation (Verma et al., 2006) show that Nck adaptor proteins connect phosphorylated nephrin with actin polymerization in podocyte foot processes, structures important for slit-diaphragm formation in the kidney.
34	16934223	Rat nephrin modulates cell morphology via the adaptor protein Nck.
35	16934223	We and others reported previously that the cytoplasmic domain of human and mouse nephrin interacts with the adaptor protein, Nck, in a tyrosine phosphorylation-dependent manner.
36	16934223	In the current study, we characterized the interaction of rat nephrin with Nck and further addressed its impact on cell morphology.
37	16934223	Rat nephrin expressed in Cos-1 cells co-immunoprecipitated with Nck in a manner dependent on the phosphorylation of Y1204 and Y1228.
38	16934223	Nephrin from normal rat glomeruli was also tyrosine phosphorylated and associated with Nck.
39	16934223	Taken together, we propose that Nck couples nephrin to the actin cytoskeleton in glomerular podocytes and contributes to the maintenance of normal morphology and function of podocytes.
40	16934223	Rat nephrin modulates cell morphology via the adaptor protein Nck.
41	16934223	We and others reported previously that the cytoplasmic domain of human and mouse nephrin interacts with the adaptor protein, Nck, in a tyrosine phosphorylation-dependent manner.
42	16934223	In the current study, we characterized the interaction of rat nephrin with Nck and further addressed its impact on cell morphology.
43	16934223	Rat nephrin expressed in Cos-1 cells co-immunoprecipitated with Nck in a manner dependent on the phosphorylation of Y1204 and Y1228.
44	16934223	Nephrin from normal rat glomeruli was also tyrosine phosphorylated and associated with Nck.
45	16934223	Taken together, we propose that Nck couples nephrin to the actin cytoskeleton in glomerular podocytes and contributes to the maintenance of normal morphology and function of podocytes.
46	16934223	Rat nephrin modulates cell morphology via the adaptor protein Nck.
47	16934223	We and others reported previously that the cytoplasmic domain of human and mouse nephrin interacts with the adaptor protein, Nck, in a tyrosine phosphorylation-dependent manner.
48	16934223	In the current study, we characterized the interaction of rat nephrin with Nck and further addressed its impact on cell morphology.
49	16934223	Rat nephrin expressed in Cos-1 cells co-immunoprecipitated with Nck in a manner dependent on the phosphorylation of Y1204 and Y1228.
50	16934223	Nephrin from normal rat glomeruli was also tyrosine phosphorylated and associated with Nck.
51	16934223	Taken together, we propose that Nck couples nephrin to the actin cytoskeleton in glomerular podocytes and contributes to the maintenance of normal morphology and function of podocytes.
52	16934223	Rat nephrin modulates cell morphology via the adaptor protein Nck.
53	16934223	We and others reported previously that the cytoplasmic domain of human and mouse nephrin interacts with the adaptor protein, Nck, in a tyrosine phosphorylation-dependent manner.
54	16934223	In the current study, we characterized the interaction of rat nephrin with Nck and further addressed its impact on cell morphology.
55	16934223	Rat nephrin expressed in Cos-1 cells co-immunoprecipitated with Nck in a manner dependent on the phosphorylation of Y1204 and Y1228.
56	16934223	Nephrin from normal rat glomeruli was also tyrosine phosphorylated and associated with Nck.
57	16934223	Taken together, we propose that Nck couples nephrin to the actin cytoskeleton in glomerular podocytes and contributes to the maintenance of normal morphology and function of podocytes.
58	16934223	Rat nephrin modulates cell morphology via the adaptor protein Nck.
59	16934223	We and others reported previously that the cytoplasmic domain of human and mouse nephrin interacts with the adaptor protein, Nck, in a tyrosine phosphorylation-dependent manner.
60	16934223	In the current study, we characterized the interaction of rat nephrin with Nck and further addressed its impact on cell morphology.
61	16934223	Rat nephrin expressed in Cos-1 cells co-immunoprecipitated with Nck in a manner dependent on the phosphorylation of Y1204 and Y1228.
62	16934223	Nephrin from normal rat glomeruli was also tyrosine phosphorylated and associated with Nck.
63	16934223	Taken together, we propose that Nck couples nephrin to the actin cytoskeleton in glomerular podocytes and contributes to the maintenance of normal morphology and function of podocytes.
64	16934223	Rat nephrin modulates cell morphology via the adaptor protein Nck.
65	16934223	We and others reported previously that the cytoplasmic domain of human and mouse nephrin interacts with the adaptor protein, Nck, in a tyrosine phosphorylation-dependent manner.
66	16934223	In the current study, we characterized the interaction of rat nephrin with Nck and further addressed its impact on cell morphology.
67	16934223	Rat nephrin expressed in Cos-1 cells co-immunoprecipitated with Nck in a manner dependent on the phosphorylation of Y1204 and Y1228.
68	16934223	Nephrin from normal rat glomeruli was also tyrosine phosphorylated and associated with Nck.
69	16934223	Taken together, we propose that Nck couples nephrin to the actin cytoskeleton in glomerular podocytes and contributes to the maintenance of normal morphology and function of podocytes.
70	17766183	The intracellular domain of nephrin is associated with linker proteins, such as CD2-associated protein and Nck proteins that can connect nephrin to the actin cytoskeleton.
71	18212058	The clustering of nephrin induces its tyrosine phosphorylation, Nck recruitment, and sustained localized actin polymerization.
72	18212058	Any one of three phosphorylated (p)YDXV motifs on nephrin is sufficient to recruit Nck through its Src homology 2 (SH2) domain and induce localized actin polymerization at these clusters.
73	18212058	Similarly, Nck SH3 mutants in which only the second or third SH3 domain is functional can mediate nephrin-induced actin polymerization.
74	18212058	However, combining such nephrin and Nck mutants attenuates actin polymerization at nephrin-Nck clusters.
75	18212058	We propose that the multiple Nck SH2-binding motifs on nephrin and the multiple SH3 domains of Nck act cooperatively to recruit the high local concentration of effectors at sites of nephrin activation that is required to initiate and maintain actin polymerization in vivo.
76	18212058	The clustering of nephrin induces its tyrosine phosphorylation, Nck recruitment, and sustained localized actin polymerization.
77	18212058	Any one of three phosphorylated (p)YDXV motifs on nephrin is sufficient to recruit Nck through its Src homology 2 (SH2) domain and induce localized actin polymerization at these clusters.
78	18212058	Similarly, Nck SH3 mutants in which only the second or third SH3 domain is functional can mediate nephrin-induced actin polymerization.
79	18212058	However, combining such nephrin and Nck mutants attenuates actin polymerization at nephrin-Nck clusters.
80	18212058	We propose that the multiple Nck SH2-binding motifs on nephrin and the multiple SH3 domains of Nck act cooperatively to recruit the high local concentration of effectors at sites of nephrin activation that is required to initiate and maintain actin polymerization in vivo.
81	18212058	The clustering of nephrin induces its tyrosine phosphorylation, Nck recruitment, and sustained localized actin polymerization.
82	18212058	Any one of three phosphorylated (p)YDXV motifs on nephrin is sufficient to recruit Nck through its Src homology 2 (SH2) domain and induce localized actin polymerization at these clusters.
83	18212058	Similarly, Nck SH3 mutants in which only the second or third SH3 domain is functional can mediate nephrin-induced actin polymerization.
84	18212058	However, combining such nephrin and Nck mutants attenuates actin polymerization at nephrin-Nck clusters.
85	18212058	We propose that the multiple Nck SH2-binding motifs on nephrin and the multiple SH3 domains of Nck act cooperatively to recruit the high local concentration of effectors at sites of nephrin activation that is required to initiate and maintain actin polymerization in vivo.
86	18212058	The clustering of nephrin induces its tyrosine phosphorylation, Nck recruitment, and sustained localized actin polymerization.
87	18212058	Any one of three phosphorylated (p)YDXV motifs on nephrin is sufficient to recruit Nck through its Src homology 2 (SH2) domain and induce localized actin polymerization at these clusters.
88	18212058	Similarly, Nck SH3 mutants in which only the second or third SH3 domain is functional can mediate nephrin-induced actin polymerization.
89	18212058	However, combining such nephrin and Nck mutants attenuates actin polymerization at nephrin-Nck clusters.
90	18212058	We propose that the multiple Nck SH2-binding motifs on nephrin and the multiple SH3 domains of Nck act cooperatively to recruit the high local concentration of effectors at sites of nephrin activation that is required to initiate and maintain actin polymerization in vivo.
91	18212058	The clustering of nephrin induces its tyrosine phosphorylation, Nck recruitment, and sustained localized actin polymerization.
92	18212058	Any one of three phosphorylated (p)YDXV motifs on nephrin is sufficient to recruit Nck through its Src homology 2 (SH2) domain and induce localized actin polymerization at these clusters.
93	18212058	Similarly, Nck SH3 mutants in which only the second or third SH3 domain is functional can mediate nephrin-induced actin polymerization.
94	18212058	However, combining such nephrin and Nck mutants attenuates actin polymerization at nephrin-Nck clusters.
95	18212058	We propose that the multiple Nck SH2-binding motifs on nephrin and the multiple SH3 domains of Nck act cooperatively to recruit the high local concentration of effectors at sites of nephrin activation that is required to initiate and maintain actin polymerization in vivo.
96	18256598	Phosphorylation of tyrosine residue (Y1204) of rat nephrin by Fyn kinase allows Nck adaptor protein binding to nephrin motifs, which include the phosphorylated tyrosine.
97	18256598	Here, we generated an antibody recognizing phosphorylated nephrin at the Nck binding sites pY1204 and pY1228 to determine the phosphorylation status of nephrin using a rat model of puromycin aminonucleoside-induced nephrosis.
98	18256598	Phosphorylation of tyrosine residue (Y1204) of rat nephrin by Fyn kinase allows Nck adaptor protein binding to nephrin motifs, which include the phosphorylated tyrosine.
99	18256598	Here, we generated an antibody recognizing phosphorylated nephrin at the Nck binding sites pY1204 and pY1228 to determine the phosphorylation status of nephrin using a rat model of puromycin aminonucleoside-induced nephrosis.
100	19443634	We recently established that the Nck family of Src homology 2 (SH2)/SH3 cytoskeletal adaptor proteins can mediate nephrin-dependent actin reorganization.
101	19443634	These data suggest that Nck is required to maintain adult podocytes and that phosphotyrosine-based interactions with nephrin may occur in foot processes of resting, mature podocytes.
102	19443634	We recently established that the Nck family of Src homology 2 (SH2)/SH3 cytoskeletal adaptor proteins can mediate nephrin-dependent actin reorganization.
103	19443634	These data suggest that Nck is required to maintain adult podocytes and that phosphotyrosine-based interactions with nephrin may occur in foot processes of resting, mature podocytes.
104	20071462	The tyrosine phosphorylation of nephrin is reported to regulate podocyte morphology via the Nck adaptor proteins.
105	20071462	In mouse podocytes, Pak2 was predominantly phosphorylated, concentrated at the tips of the cellular processes, and its expression and/or phosphorylation were further increased when differentiated.
106	20071462	Overexpression of rat nephrin in podocytes increased Pak1/2 phosphorylation, which was abolished when the Nck binding sites were mutated.
107	20071462	Furthermore, dominant-negative Nck constructs blocked the Pak1 phosphorylation induced by antibody-mediated cross linking of nephrin.
108	20071462	Transient transfection of constitutively kinase-active Pak1 into differentiated mouse podocytes decreased stress fibers, increased cortical F-actin, and extended the cellular processes, whereas kinase-dead mutant, kinase inhibitory construct, and Pak2 knockdown by shRNA had the opposite effect.
109	20071462	In a rat model of puromycin aminonucleoside nephrosis, Pak1/2 phosphorylation was decreased in glomeruli, concomitantly with a decrease of nephrin tyrosine phosphorylation.
110	20071462	The tyrosine phosphorylation of nephrin is reported to regulate podocyte morphology via the Nck adaptor proteins.
111	20071462	In mouse podocytes, Pak2 was predominantly phosphorylated, concentrated at the tips of the cellular processes, and its expression and/or phosphorylation were further increased when differentiated.
112	20071462	Overexpression of rat nephrin in podocytes increased Pak1/2 phosphorylation, which was abolished when the Nck binding sites were mutated.
113	20071462	Furthermore, dominant-negative Nck constructs blocked the Pak1 phosphorylation induced by antibody-mediated cross linking of nephrin.
114	20071462	Transient transfection of constitutively kinase-active Pak1 into differentiated mouse podocytes decreased stress fibers, increased cortical F-actin, and extended the cellular processes, whereas kinase-dead mutant, kinase inhibitory construct, and Pak2 knockdown by shRNA had the opposite effect.
115	20071462	In a rat model of puromycin aminonucleoside nephrosis, Pak1/2 phosphorylation was decreased in glomeruli, concomitantly with a decrease of nephrin tyrosine phosphorylation.
116	20071462	The tyrosine phosphorylation of nephrin is reported to regulate podocyte morphology via the Nck adaptor proteins.
117	20071462	In mouse podocytes, Pak2 was predominantly phosphorylated, concentrated at the tips of the cellular processes, and its expression and/or phosphorylation were further increased when differentiated.
118	20071462	Overexpression of rat nephrin in podocytes increased Pak1/2 phosphorylation, which was abolished when the Nck binding sites were mutated.
119	20071462	Furthermore, dominant-negative Nck constructs blocked the Pak1 phosphorylation induced by antibody-mediated cross linking of nephrin.
120	20071462	Transient transfection of constitutively kinase-active Pak1 into differentiated mouse podocytes decreased stress fibers, increased cortical F-actin, and extended the cellular processes, whereas kinase-dead mutant, kinase inhibitory construct, and Pak2 knockdown by shRNA had the opposite effect.
121	20071462	In a rat model of puromycin aminonucleoside nephrosis, Pak1/2 phosphorylation was decreased in glomeruli, concomitantly with a decrease of nephrin tyrosine phosphorylation.
122	20484117	Moreover, c-mip inhibited interactions between Fyn and the cytoskeletal regulator N-WASP (neural Wiskott-Aldrich syndrome protein) and between the adaptor protein Nck and nephrin, potentially accounting for cytoskeletal disorganization and the effacement of foot processes seen in idiopathic nephrotic syndromes.
123	21937443	Vascular endothelial growth factor receptor 2 direct interaction with nephrin links VEGF-A signals to actin in kidney podocytes.
124	21937443	Accumulating evidence suggests a cross-talk between VEGF-A and nephrin signaling pathways.
125	21937443	We previously showed that in vivo nephrin associates with VEGF receptor-2 (VEGFR2), the signaling receptor for VEGF-A.
126	21937443	In the present work, we characterized the interaction between nephrin and VEGFR2 in cultured cells and in vitro.
127	21937443	This interaction occurs through VEGFR2 and nephrin cytoplasmic domains.
128	21937443	Furthermore, the nephrin-VEGFR2 complex involves Nck and actin.
129	21937443	We propose that the nephrin-VEGFR2 complex acts as a key mediator to transduce local VEGF-A signals to the podocyte actin cytoskeleton, regulating the foot process structure and glomerular filter integrity.
130	22662192	In podocytes, IQGAP1 is associated with nephrin in the glomerular slit diaphragm (SD) complex, but its role remains ill-defined.
131	22662192	IC, IP, and IsPL experiments showed colocalizations and/or interactions between IQGAP1 and SD proteins (nephrin, MAGI-1, CD2AP, NCK 1/2, podocin), podocalyxin, and cytoskeletal proteins (α-actinin-4).
132	23188823	Direct regulation of nephrin tyrosine phosphorylation by Nck adaptor proteins.
133	23188823	We have recently reported that tyrosine phosphorylation of the cytoplasmic tail of nephrin facilitates recruitment of Nck SH2/SH3 adaptor proteins and subsequent actin remodeling and that phosphorylation of the Nck binding sites on nephrin is decreased during podocyte injury.
134	23188823	We now demonstrate that Nck directly modulates nephrin phosphorylation through formation of a signaling complex with the Src family kinase Fyn.
135	23188823	The ability of Nck to enhance nephrin phosphorylation is compromised in the presence of a Src family kinase inhibitor and when the SH3 domains of Nck are mutated.
136	23188823	Furthermore, induced loss of Nck expression in podocytes in vivo is associated with a rapid reduction in nephrin tyrosine phosphorylation.
137	23188823	Our results suggest that Nck may facilitate dynamic signaling events at the slit diaphragm by promoting Fyn-dependent phosphorylation of nephrin, which may be important in the regulation of foot process morphology and response to podocyte injury.
138	23188823	Direct regulation of nephrin tyrosine phosphorylation by Nck adaptor proteins.
139	23188823	We have recently reported that tyrosine phosphorylation of the cytoplasmic tail of nephrin facilitates recruitment of Nck SH2/SH3 adaptor proteins and subsequent actin remodeling and that phosphorylation of the Nck binding sites on nephrin is decreased during podocyte injury.
140	23188823	We now demonstrate that Nck directly modulates nephrin phosphorylation through formation of a signaling complex with the Src family kinase Fyn.
141	23188823	The ability of Nck to enhance nephrin phosphorylation is compromised in the presence of a Src family kinase inhibitor and when the SH3 domains of Nck are mutated.
142	23188823	Furthermore, induced loss of Nck expression in podocytes in vivo is associated with a rapid reduction in nephrin tyrosine phosphorylation.
143	23188823	Our results suggest that Nck may facilitate dynamic signaling events at the slit diaphragm by promoting Fyn-dependent phosphorylation of nephrin, which may be important in the regulation of foot process morphology and response to podocyte injury.
144	23188823	Direct regulation of nephrin tyrosine phosphorylation by Nck adaptor proteins.
145	23188823	We have recently reported that tyrosine phosphorylation of the cytoplasmic tail of nephrin facilitates recruitment of Nck SH2/SH3 adaptor proteins and subsequent actin remodeling and that phosphorylation of the Nck binding sites on nephrin is decreased during podocyte injury.
146	23188823	We now demonstrate that Nck directly modulates nephrin phosphorylation through formation of a signaling complex with the Src family kinase Fyn.
147	23188823	The ability of Nck to enhance nephrin phosphorylation is compromised in the presence of a Src family kinase inhibitor and when the SH3 domains of Nck are mutated.
148	23188823	Furthermore, induced loss of Nck expression in podocytes in vivo is associated with a rapid reduction in nephrin tyrosine phosphorylation.
149	23188823	Our results suggest that Nck may facilitate dynamic signaling events at the slit diaphragm by promoting Fyn-dependent phosphorylation of nephrin, which may be important in the regulation of foot process morphology and response to podocyte injury.
150	23188823	Direct regulation of nephrin tyrosine phosphorylation by Nck adaptor proteins.
151	23188823	We have recently reported that tyrosine phosphorylation of the cytoplasmic tail of nephrin facilitates recruitment of Nck SH2/SH3 adaptor proteins and subsequent actin remodeling and that phosphorylation of the Nck binding sites on nephrin is decreased during podocyte injury.
152	23188823	We now demonstrate that Nck directly modulates nephrin phosphorylation through formation of a signaling complex with the Src family kinase Fyn.
153	23188823	The ability of Nck to enhance nephrin phosphorylation is compromised in the presence of a Src family kinase inhibitor and when the SH3 domains of Nck are mutated.
154	23188823	Furthermore, induced loss of Nck expression in podocytes in vivo is associated with a rapid reduction in nephrin tyrosine phosphorylation.
155	23188823	Our results suggest that Nck may facilitate dynamic signaling events at the slit diaphragm by promoting Fyn-dependent phosphorylation of nephrin, which may be important in the regulation of foot process morphology and response to podocyte injury.
156	23188823	Direct regulation of nephrin tyrosine phosphorylation by Nck adaptor proteins.
157	23188823	We have recently reported that tyrosine phosphorylation of the cytoplasmic tail of nephrin facilitates recruitment of Nck SH2/SH3 adaptor proteins and subsequent actin remodeling and that phosphorylation of the Nck binding sites on nephrin is decreased during podocyte injury.
158	23188823	We now demonstrate that Nck directly modulates nephrin phosphorylation through formation of a signaling complex with the Src family kinase Fyn.
159	23188823	The ability of Nck to enhance nephrin phosphorylation is compromised in the presence of a Src family kinase inhibitor and when the SH3 domains of Nck are mutated.
160	23188823	Furthermore, induced loss of Nck expression in podocytes in vivo is associated with a rapid reduction in nephrin tyrosine phosphorylation.
161	23188823	Our results suggest that Nck may facilitate dynamic signaling events at the slit diaphragm by promoting Fyn-dependent phosphorylation of nephrin, which may be important in the regulation of foot process morphology and response to podocyte injury.
162	23188823	Direct regulation of nephrin tyrosine phosphorylation by Nck adaptor proteins.
163	23188823	We have recently reported that tyrosine phosphorylation of the cytoplasmic tail of nephrin facilitates recruitment of Nck SH2/SH3 adaptor proteins and subsequent actin remodeling and that phosphorylation of the Nck binding sites on nephrin is decreased during podocyte injury.
164	23188823	We now demonstrate that Nck directly modulates nephrin phosphorylation through formation of a signaling complex with the Src family kinase Fyn.
165	23188823	The ability of Nck to enhance nephrin phosphorylation is compromised in the presence of a Src family kinase inhibitor and when the SH3 domains of Nck are mutated.
166	23188823	Furthermore, induced loss of Nck expression in podocytes in vivo is associated with a rapid reduction in nephrin tyrosine phosphorylation.
167	23188823	Our results suggest that Nck may facilitate dynamic signaling events at the slit diaphragm by promoting Fyn-dependent phosphorylation of nephrin, which may be important in the regulation of foot process morphology and response to podocyte injury.
168	24175259	These adaptor proteins, such as CD2-associated protein, zonula occludens 1, β-catenin, Nck and p130Cas, located at the intracellular SD insertion area near lipid rafts, have important structural and functional roles.
169	24287595	Proteasomal degradation of Nck1 but not Nck2 regulates RhoA activation and actin dynamics.
170	24287595	Here we show that Nck1, but not Nck2, is a substrate of c-Cbl-mediated ubiquitination.
171	24287595	We uncover lysine 178 in Nck1 as the evolutionarily conserved ubiquitin acceptor site.
172	24287595	We previously reported that synaptopodin, a proline-rich actin-binding protein, induces stress fibres by blocking the Smurf1-mediated ubiquitination of RhoA.
173	24287595	We now find that synaptopodin competes with c-Cbl for binding to Nck1, which prevents the ubiquitination of Nck1 by c-Cbl.
174	24287595	Gene silencing of c-Cbl restores Nck1 protein abundance and stress fibres in synaptopodin knockdown cells.
175	24287595	Similarly, expression of c-Cbl-resistant Nck1(K178R) or Nck2 containing the SH3 domain 2 of Nck1 restores stress fibres in synaptopodin-depleted podocytes through activation of RhoA signalling.
176	24287595	These findings reveal proteasomal regulation as a key factor in the distinct and non-redundant effects of Nck on RhoA-mediated actin dynamics.
177	24287595	Proteasomal degradation of Nck1 but not Nck2 regulates RhoA activation and actin dynamics.
178	24287595	Here we show that Nck1, but not Nck2, is a substrate of c-Cbl-mediated ubiquitination.
179	24287595	We uncover lysine 178 in Nck1 as the evolutionarily conserved ubiquitin acceptor site.
180	24287595	We previously reported that synaptopodin, a proline-rich actin-binding protein, induces stress fibres by blocking the Smurf1-mediated ubiquitination of RhoA.
181	24287595	We now find that synaptopodin competes with c-Cbl for binding to Nck1, which prevents the ubiquitination of Nck1 by c-Cbl.
182	24287595	Gene silencing of c-Cbl restores Nck1 protein abundance and stress fibres in synaptopodin knockdown cells.
183	24287595	Similarly, expression of c-Cbl-resistant Nck1(K178R) or Nck2 containing the SH3 domain 2 of Nck1 restores stress fibres in synaptopodin-depleted podocytes through activation of RhoA signalling.
184	24287595	These findings reveal proteasomal regulation as a key factor in the distinct and non-redundant effects of Nck on RhoA-mediated actin dynamics.
185	24287595	Proteasomal degradation of Nck1 but not Nck2 regulates RhoA activation and actin dynamics.
186	24287595	Here we show that Nck1, but not Nck2, is a substrate of c-Cbl-mediated ubiquitination.
187	24287595	We uncover lysine 178 in Nck1 as the evolutionarily conserved ubiquitin acceptor site.
188	24287595	We previously reported that synaptopodin, a proline-rich actin-binding protein, induces stress fibres by blocking the Smurf1-mediated ubiquitination of RhoA.
189	24287595	We now find that synaptopodin competes with c-Cbl for binding to Nck1, which prevents the ubiquitination of Nck1 by c-Cbl.
190	24287595	Gene silencing of c-Cbl restores Nck1 protein abundance and stress fibres in synaptopodin knockdown cells.
191	24287595	Similarly, expression of c-Cbl-resistant Nck1(K178R) or Nck2 containing the SH3 domain 2 of Nck1 restores stress fibres in synaptopodin-depleted podocytes through activation of RhoA signalling.
192	24287595	These findings reveal proteasomal regulation as a key factor in the distinct and non-redundant effects of Nck on RhoA-mediated actin dynamics.
193	24287595	Proteasomal degradation of Nck1 but not Nck2 regulates RhoA activation and actin dynamics.
194	24287595	Here we show that Nck1, but not Nck2, is a substrate of c-Cbl-mediated ubiquitination.
195	24287595	We uncover lysine 178 in Nck1 as the evolutionarily conserved ubiquitin acceptor site.
196	24287595	We previously reported that synaptopodin, a proline-rich actin-binding protein, induces stress fibres by blocking the Smurf1-mediated ubiquitination of RhoA.
197	24287595	We now find that synaptopodin competes with c-Cbl for binding to Nck1, which prevents the ubiquitination of Nck1 by c-Cbl.
198	24287595	Gene silencing of c-Cbl restores Nck1 protein abundance and stress fibres in synaptopodin knockdown cells.
199	24287595	Similarly, expression of c-Cbl-resistant Nck1(K178R) or Nck2 containing the SH3 domain 2 of Nck1 restores stress fibres in synaptopodin-depleted podocytes through activation of RhoA signalling.
200	24287595	These findings reveal proteasomal regulation as a key factor in the distinct and non-redundant effects of Nck on RhoA-mediated actin dynamics.
201	24287595	Proteasomal degradation of Nck1 but not Nck2 regulates RhoA activation and actin dynamics.
202	24287595	Here we show that Nck1, but not Nck2, is a substrate of c-Cbl-mediated ubiquitination.
203	24287595	We uncover lysine 178 in Nck1 as the evolutionarily conserved ubiquitin acceptor site.
204	24287595	We previously reported that synaptopodin, a proline-rich actin-binding protein, induces stress fibres by blocking the Smurf1-mediated ubiquitination of RhoA.
205	24287595	We now find that synaptopodin competes with c-Cbl for binding to Nck1, which prevents the ubiquitination of Nck1 by c-Cbl.
206	24287595	Gene silencing of c-Cbl restores Nck1 protein abundance and stress fibres in synaptopodin knockdown cells.
207	24287595	Similarly, expression of c-Cbl-resistant Nck1(K178R) or Nck2 containing the SH3 domain 2 of Nck1 restores stress fibres in synaptopodin-depleted podocytes through activation of RhoA signalling.
208	24287595	These findings reveal proteasomal regulation as a key factor in the distinct and non-redundant effects of Nck on RhoA-mediated actin dynamics.
209	24287595	Proteasomal degradation of Nck1 but not Nck2 regulates RhoA activation and actin dynamics.
210	24287595	Here we show that Nck1, but not Nck2, is a substrate of c-Cbl-mediated ubiquitination.
211	24287595	We uncover lysine 178 in Nck1 as the evolutionarily conserved ubiquitin acceptor site.
212	24287595	We previously reported that synaptopodin, a proline-rich actin-binding protein, induces stress fibres by blocking the Smurf1-mediated ubiquitination of RhoA.
213	24287595	We now find that synaptopodin competes with c-Cbl for binding to Nck1, which prevents the ubiquitination of Nck1 by c-Cbl.
214	24287595	Gene silencing of c-Cbl restores Nck1 protein abundance and stress fibres in synaptopodin knockdown cells.
215	24287595	Similarly, expression of c-Cbl-resistant Nck1(K178R) or Nck2 containing the SH3 domain 2 of Nck1 restores stress fibres in synaptopodin-depleted podocytes through activation of RhoA signalling.
216	24287595	These findings reveal proteasomal regulation as a key factor in the distinct and non-redundant effects of Nck on RhoA-mediated actin dynamics.
217	24287595	Proteasomal degradation of Nck1 but not Nck2 regulates RhoA activation and actin dynamics.
218	24287595	Here we show that Nck1, but not Nck2, is a substrate of c-Cbl-mediated ubiquitination.
219	24287595	We uncover lysine 178 in Nck1 as the evolutionarily conserved ubiquitin acceptor site.
220	24287595	We previously reported that synaptopodin, a proline-rich actin-binding protein, induces stress fibres by blocking the Smurf1-mediated ubiquitination of RhoA.
221	24287595	We now find that synaptopodin competes with c-Cbl for binding to Nck1, which prevents the ubiquitination of Nck1 by c-Cbl.
222	24287595	Gene silencing of c-Cbl restores Nck1 protein abundance and stress fibres in synaptopodin knockdown cells.
223	24287595	Similarly, expression of c-Cbl-resistant Nck1(K178R) or Nck2 containing the SH3 domain 2 of Nck1 restores stress fibres in synaptopodin-depleted podocytes through activation of RhoA signalling.
224	24287595	These findings reveal proteasomal regulation as a key factor in the distinct and non-redundant effects of Nck on RhoA-mediated actin dynamics.
225	24515388	Role of nephrin phosphorylation inducted by dexamethasone and angiotensin II in podocytes.
226	24515388	In this study, we observated the effect of Dex and angiotensin II (AngII) on the change of nephrin phosphorylation in cultured podocytes.
227	24515388	Nck or Fyn were silenced by small interfering RNA (siRNA), nephrin and its phosphorylation expression were analyzed by Western blotting.
228	24515388	In vitro, the phosphorylation of nephrin was significantly reduced after AngII stimulation (P < 0.05).
229	24515388	Dex significantly resisted podocyte injury inducted by AngII via increasing the phosphorylation of nephrin (P < 0.05), siRNA silencing Nck can partially inhibited nephrin phosphorylation, siRNA silencing Fyn can completely inhibited nephrin phosphorylation.
230	24515388	Role of nephrin phosphorylation inducted by dexamethasone and angiotensin II in podocytes.
231	24515388	In this study, we observated the effect of Dex and angiotensin II (AngII) on the change of nephrin phosphorylation in cultured podocytes.
232	24515388	Nck or Fyn were silenced by small interfering RNA (siRNA), nephrin and its phosphorylation expression were analyzed by Western blotting.
233	24515388	In vitro, the phosphorylation of nephrin was significantly reduced after AngII stimulation (P < 0.05).
234	24515388	Dex significantly resisted podocyte injury inducted by AngII via increasing the phosphorylation of nephrin (P < 0.05), siRNA silencing Nck can partially inhibited nephrin phosphorylation, siRNA silencing Fyn can completely inhibited nephrin phosphorylation.
235	26802179	Evidence indicates that tyrosine phosphorylation of the intracellular tail of nephrin initiates signaling events, including recruitment of cytoplasmic adaptor proteins Nck1 and Nck2 that regulate actin cytoskeletal dynamics.
236	26802179	To explore this possibility, we generated and analyzed knockin mice with mutations that disrupt nephrin tyrosine phosphorylation and Nck1/2 binding (nephrin(Y3F/Y3F) mice).
237	26802179	Evidence indicates that tyrosine phosphorylation of the intracellular tail of nephrin initiates signaling events, including recruitment of cytoplasmic adaptor proteins Nck1 and Nck2 that regulate actin cytoskeletal dynamics.
238	26802179	To explore this possibility, we generated and analyzed knockin mice with mutations that disrupt nephrin tyrosine phosphorylation and Nck1/2 binding (nephrin(Y3F/Y3F) mice).
239	27033705	Nephrin Suppresses Hippo Signaling through the Adaptor Proteins Nck and WTIP.
240	27033705	We have previously established that tyrosine phosphorylation of the transmembrane protein nephrin promotes recruitment of the Nck1/2 cytoskeletal adaptor proteins and downstream actin remodeling.
241	27033705	We now reveal that Nck integrates nephrin with the Hippo kinase cascade through association with the adaptor protein WTIP.
242	27033705	Using mutational analysis, we show that Nck sequesters WTIP and its binding partner Lats1 to phosphorylated nephrin, resulting in decreased phospho-activation of Lats1.
243	27033705	We further demonstrate that, coincident with nephrin dephosphorylation in a transient model of podocyte injury in mice, Lats1 is rapidly activated, and this precedes significant down-regulation of the transcription regulator Yap.
244	27033705	Nephrin Suppresses Hippo Signaling through the Adaptor Proteins Nck and WTIP.
245	27033705	We have previously established that tyrosine phosphorylation of the transmembrane protein nephrin promotes recruitment of the Nck1/2 cytoskeletal adaptor proteins and downstream actin remodeling.
246	27033705	We now reveal that Nck integrates nephrin with the Hippo kinase cascade through association with the adaptor protein WTIP.
247	27033705	Using mutational analysis, we show that Nck sequesters WTIP and its binding partner Lats1 to phosphorylated nephrin, resulting in decreased phospho-activation of Lats1.
248	27033705	We further demonstrate that, coincident with nephrin dephosphorylation in a transient model of podocyte injury in mice, Lats1 is rapidly activated, and this precedes significant down-regulation of the transcription regulator Yap.
249	27033705	Nephrin Suppresses Hippo Signaling through the Adaptor Proteins Nck and WTIP.
250	27033705	We have previously established that tyrosine phosphorylation of the transmembrane protein nephrin promotes recruitment of the Nck1/2 cytoskeletal adaptor proteins and downstream actin remodeling.
251	27033705	We now reveal that Nck integrates nephrin with the Hippo kinase cascade through association with the adaptor protein WTIP.
252	27033705	Using mutational analysis, we show that Nck sequesters WTIP and its binding partner Lats1 to phosphorylated nephrin, resulting in decreased phospho-activation of Lats1.
253	27033705	We further demonstrate that, coincident with nephrin dephosphorylation in a transient model of podocyte injury in mice, Lats1 is rapidly activated, and this precedes significant down-regulation of the transcription regulator Yap.
254	27033705	Nephrin Suppresses Hippo Signaling through the Adaptor Proteins Nck and WTIP.
255	27033705	We have previously established that tyrosine phosphorylation of the transmembrane protein nephrin promotes recruitment of the Nck1/2 cytoskeletal adaptor proteins and downstream actin remodeling.
256	27033705	We now reveal that Nck integrates nephrin with the Hippo kinase cascade through association with the adaptor protein WTIP.
257	27033705	Using mutational analysis, we show that Nck sequesters WTIP and its binding partner Lats1 to phosphorylated nephrin, resulting in decreased phospho-activation of Lats1.
258	27033705	We further demonstrate that, coincident with nephrin dephosphorylation in a transient model of podocyte injury in mice, Lats1 is rapidly activated, and this precedes significant down-regulation of the transcription regulator Yap.
259	31974115	Assembly of signaling molecules into micrometer-sized clusters is driven by multivalent protein-protein interactions, such as those found within the nephrin-Nck (Nck1 or Nck2) complex.
260	31974115	Phosphorylation on multiple tyrosine residues within the tail of the nephrin transmembrane receptor induces recruitment of the cytoplasmic adaptor protein Nck, which binds via its triple SH3 domains to various effectors, leading to actin assembly.
261	31974115	We also reveal a connection between clustering and endocytosis, which appears to be driven by threshold levels of nephrin tyrosine phosphorylation and Nck SH3 domain signaling.
262	31974115	Assembly of signaling molecules into micrometer-sized clusters is driven by multivalent protein-protein interactions, such as those found within the nephrin-Nck (Nck1 or Nck2) complex.
263	31974115	Phosphorylation on multiple tyrosine residues within the tail of the nephrin transmembrane receptor induces recruitment of the cytoplasmic adaptor protein Nck, which binds via its triple SH3 domains to various effectors, leading to actin assembly.
264	31974115	We also reveal a connection between clustering and endocytosis, which appears to be driven by threshold levels of nephrin tyrosine phosphorylation and Nck SH3 domain signaling.
265	31974115	Assembly of signaling molecules into micrometer-sized clusters is driven by multivalent protein-protein interactions, such as those found within the nephrin-Nck (Nck1 or Nck2) complex.
266	31974115	Phosphorylation on multiple tyrosine residues within the tail of the nephrin transmembrane receptor induces recruitment of the cytoplasmic adaptor protein Nck, which binds via its triple SH3 domains to various effectors, leading to actin assembly.
267	31974115	We also reveal a connection between clustering and endocytosis, which appears to be driven by threshold levels of nephrin tyrosine phosphorylation and Nck SH3 domain signaling.
268	34558601	The non-catalytic region of tyrosine kinase (Nck) family of adaptors, consisting of Nck1 and Nck2, contributes to selectivity and specificity in the flow of cellular information by recruiting components of signaling networks.
269	34558601	In this Cell Science at a Glance and the accompanying poster, we highlight the molecular organization and functions of the Nck family, focusing on key interactions and pathways, regulation of cellular processes, development, homeostasis and pathogenesis, as well as emerging and non-redundant functions of Nck1 compared to those of Nck2.
270	34558601	The non-catalytic region of tyrosine kinase (Nck) family of adaptors, consisting of Nck1 and Nck2, contributes to selectivity and specificity in the flow of cellular information by recruiting components of signaling networks.
271	34558601	In this Cell Science at a Glance and the accompanying poster, we highlight the molecular organization and functions of the Nck family, focusing on key interactions and pathways, regulation of cellular processes, development, homeostasis and pathogenesis, as well as emerging and non-redundant functions of Nck1 compared to those of Nck2.