Ignet

Gene Information

Gene symbol: CD2AP

Gene name: CD2-associated protein

HGNC ID: 14258

Synonyms: CMS

Related Genes

#	Gene Symbol	Number of hits
1	ACTN4	1 hits
2	BCAR1	1 hits
3	CD2	1 hits
4	LAMB2	1 hits
5	NPHS1	1 hits
6	NPHS2	1 hits
7	PKD2	1 hits
8	SRPR	1 hits

Related Sentences

#	PMID	Sentence
1	10913159	In vivo interaction of the adapter protein CD2-associated protein with the type 2 polycystic kidney disease protein, polycystin-2.
2	10913159	The deduced 70.5-kDa protein, originally named METS-1 (mesenchyme-to-epithelium transition protein with SH3 domains), has since been cloned as a CD2-associated protein (CD2AP).
3	10913159	Independent yeast two-hybrid screens using the COOH-terminal region of either CD2AP or polycystin-2 as bait identified the COOH termini of polycystin-2 and CD2AP, respectively, as strong interacting partners.
4	10913159	This interaction was confirmed in cultured cells by co-immunoprecipitation of endogenous polycystin-2 with endogenous CD2AP and vice versa.
5	10913159	CD2AP shows a diffuse reticular cytoplasmic and perinuclear pattern of distribution, similar to polycystin-2, in cultured cells, and the two proteins co-localize by indirect double immunofluorescence microscopy.
6	10913159	Such a function fits well with that hypothesized for the polycystin proteins in renal tubular epithelial cells, and the present findings suggest that CD2AP has a role in polycystin-2 function.
7	10913159	In vivo interaction of the adapter protein CD2-associated protein with the type 2 polycystic kidney disease protein, polycystin-2.
8	10913159	The deduced 70.5-kDa protein, originally named METS-1 (mesenchyme-to-epithelium transition protein with SH3 domains), has since been cloned as a CD2-associated protein (CD2AP).
9	10913159	Independent yeast two-hybrid screens using the COOH-terminal region of either CD2AP or polycystin-2 as bait identified the COOH termini of polycystin-2 and CD2AP, respectively, as strong interacting partners.
10	10913159	This interaction was confirmed in cultured cells by co-immunoprecipitation of endogenous polycystin-2 with endogenous CD2AP and vice versa.
11	10913159	CD2AP shows a diffuse reticular cytoplasmic and perinuclear pattern of distribution, similar to polycystin-2, in cultured cells, and the two proteins co-localize by indirect double immunofluorescence microscopy.
12	10913159	Such a function fits well with that hypothesized for the polycystin proteins in renal tubular epithelial cells, and the present findings suggest that CD2AP has a role in polycystin-2 function.
13	10913159	In vivo interaction of the adapter protein CD2-associated protein with the type 2 polycystic kidney disease protein, polycystin-2.
14	10913159	The deduced 70.5-kDa protein, originally named METS-1 (mesenchyme-to-epithelium transition protein with SH3 domains), has since been cloned as a CD2-associated protein (CD2AP).
15	10913159	Independent yeast two-hybrid screens using the COOH-terminal region of either CD2AP or polycystin-2 as bait identified the COOH termini of polycystin-2 and CD2AP, respectively, as strong interacting partners.
16	10913159	This interaction was confirmed in cultured cells by co-immunoprecipitation of endogenous polycystin-2 with endogenous CD2AP and vice versa.
17	10913159	CD2AP shows a diffuse reticular cytoplasmic and perinuclear pattern of distribution, similar to polycystin-2, in cultured cells, and the two proteins co-localize by indirect double immunofluorescence microscopy.
18	10913159	Such a function fits well with that hypothesized for the polycystin proteins in renal tubular epithelial cells, and the present findings suggest that CD2AP has a role in polycystin-2 function.
19	10913159	In vivo interaction of the adapter protein CD2-associated protein with the type 2 polycystic kidney disease protein, polycystin-2.
20	10913159	The deduced 70.5-kDa protein, originally named METS-1 (mesenchyme-to-epithelium transition protein with SH3 domains), has since been cloned as a CD2-associated protein (CD2AP).
21	10913159	Independent yeast two-hybrid screens using the COOH-terminal region of either CD2AP or polycystin-2 as bait identified the COOH termini of polycystin-2 and CD2AP, respectively, as strong interacting partners.
22	10913159	This interaction was confirmed in cultured cells by co-immunoprecipitation of endogenous polycystin-2 with endogenous CD2AP and vice versa.
23	10913159	CD2AP shows a diffuse reticular cytoplasmic and perinuclear pattern of distribution, similar to polycystin-2, in cultured cells, and the two proteins co-localize by indirect double immunofluorescence microscopy.
24	10913159	Such a function fits well with that hypothesized for the polycystin proteins in renal tubular epithelial cells, and the present findings suggest that CD2AP has a role in polycystin-2 function.
25	10913159	In vivo interaction of the adapter protein CD2-associated protein with the type 2 polycystic kidney disease protein, polycystin-2.
26	10913159	The deduced 70.5-kDa protein, originally named METS-1 (mesenchyme-to-epithelium transition protein with SH3 domains), has since been cloned as a CD2-associated protein (CD2AP).
27	10913159	Independent yeast two-hybrid screens using the COOH-terminal region of either CD2AP or polycystin-2 as bait identified the COOH termini of polycystin-2 and CD2AP, respectively, as strong interacting partners.
28	10913159	This interaction was confirmed in cultured cells by co-immunoprecipitation of endogenous polycystin-2 with endogenous CD2AP and vice versa.
29	10913159	CD2AP shows a diffuse reticular cytoplasmic and perinuclear pattern of distribution, similar to polycystin-2, in cultured cells, and the two proteins co-localize by indirect double immunofluorescence microscopy.
30	10913159	Such a function fits well with that hypothesized for the polycystin proteins in renal tubular epithelial cells, and the present findings suggest that CD2AP has a role in polycystin-2 function.
31	10913159	In vivo interaction of the adapter protein CD2-associated protein with the type 2 polycystic kidney disease protein, polycystin-2.
32	10913159	The deduced 70.5-kDa protein, originally named METS-1 (mesenchyme-to-epithelium transition protein with SH3 domains), has since been cloned as a CD2-associated protein (CD2AP).
33	10913159	Independent yeast two-hybrid screens using the COOH-terminal region of either CD2AP or polycystin-2 as bait identified the COOH termini of polycystin-2 and CD2AP, respectively, as strong interacting partners.
34	10913159	This interaction was confirmed in cultured cells by co-immunoprecipitation of endogenous polycystin-2 with endogenous CD2AP and vice versa.
35	10913159	CD2AP shows a diffuse reticular cytoplasmic and perinuclear pattern of distribution, similar to polycystin-2, in cultured cells, and the two proteins co-localize by indirect double immunofluorescence microscopy.
36	10913159	Such a function fits well with that hypothesized for the polycystin proteins in renal tubular epithelial cells, and the present findings suggest that CD2AP has a role in polycystin-2 function.
37	10997929	CD2AP is expressed with nephrin in developing podocytes and is found widely in mature kidney and elsewhere.
38	10997929	CD2-associated protein (CD2AP) is an adapter molecule that can bind to the cytoplasmic domain of nephrin, a component of the glomerular slit diaphragm.
39	10997929	Mice lacking CD2AP exhibit a congenital nephrotic syndrome characterized by extensive foot process effacement, suggesting that CD2AP-nephrin interactions are critical to maintaining slit diaphragm function.
40	10997929	We have examined the patterns of expression of both CD2AP and nephrin in developing mouse and human kidney.
41	10997929	Kidneys from Cd2ap -/- mice initially exhibited normal nephrin localization, but as the mice aged and foot processes became effaced, nephrin disappeared.
42	10997929	In laminin-beta(2) mutant mice exhibiting nephrotic syndrome, CD2AP in glomeruli was aberrantly localized in a primarily punctate pattern.
43	10997929	CD2AP is expressed with nephrin in developing podocytes and is found widely in mature kidney and elsewhere.
44	10997929	CD2-associated protein (CD2AP) is an adapter molecule that can bind to the cytoplasmic domain of nephrin, a component of the glomerular slit diaphragm.
45	10997929	Mice lacking CD2AP exhibit a congenital nephrotic syndrome characterized by extensive foot process effacement, suggesting that CD2AP-nephrin interactions are critical to maintaining slit diaphragm function.
46	10997929	We have examined the patterns of expression of both CD2AP and nephrin in developing mouse and human kidney.
47	10997929	Kidneys from Cd2ap -/- mice initially exhibited normal nephrin localization, but as the mice aged and foot processes became effaced, nephrin disappeared.
48	10997929	In laminin-beta(2) mutant mice exhibiting nephrotic syndrome, CD2AP in glomeruli was aberrantly localized in a primarily punctate pattern.
49	10997929	CD2AP is expressed with nephrin in developing podocytes and is found widely in mature kidney and elsewhere.
50	10997929	CD2-associated protein (CD2AP) is an adapter molecule that can bind to the cytoplasmic domain of nephrin, a component of the glomerular slit diaphragm.
51	10997929	Mice lacking CD2AP exhibit a congenital nephrotic syndrome characterized by extensive foot process effacement, suggesting that CD2AP-nephrin interactions are critical to maintaining slit diaphragm function.
52	10997929	We have examined the patterns of expression of both CD2AP and nephrin in developing mouse and human kidney.
53	10997929	Kidneys from Cd2ap -/- mice initially exhibited normal nephrin localization, but as the mice aged and foot processes became effaced, nephrin disappeared.
54	10997929	In laminin-beta(2) mutant mice exhibiting nephrotic syndrome, CD2AP in glomeruli was aberrantly localized in a primarily punctate pattern.
55	10997929	CD2AP is expressed with nephrin in developing podocytes and is found widely in mature kidney and elsewhere.
56	10997929	CD2-associated protein (CD2AP) is an adapter molecule that can bind to the cytoplasmic domain of nephrin, a component of the glomerular slit diaphragm.
57	10997929	Mice lacking CD2AP exhibit a congenital nephrotic syndrome characterized by extensive foot process effacement, suggesting that CD2AP-nephrin interactions are critical to maintaining slit diaphragm function.
58	10997929	We have examined the patterns of expression of both CD2AP and nephrin in developing mouse and human kidney.
59	10997929	Kidneys from Cd2ap -/- mice initially exhibited normal nephrin localization, but as the mice aged and foot processes became effaced, nephrin disappeared.
60	10997929	In laminin-beta(2) mutant mice exhibiting nephrotic syndrome, CD2AP in glomeruli was aberrantly localized in a primarily punctate pattern.
61	10997929	CD2AP is expressed with nephrin in developing podocytes and is found widely in mature kidney and elsewhere.
62	10997929	CD2-associated protein (CD2AP) is an adapter molecule that can bind to the cytoplasmic domain of nephrin, a component of the glomerular slit diaphragm.
63	10997929	Mice lacking CD2AP exhibit a congenital nephrotic syndrome characterized by extensive foot process effacement, suggesting that CD2AP-nephrin interactions are critical to maintaining slit diaphragm function.
64	10997929	We have examined the patterns of expression of both CD2AP and nephrin in developing mouse and human kidney.
65	10997929	Kidneys from Cd2ap -/- mice initially exhibited normal nephrin localization, but as the mice aged and foot processes became effaced, nephrin disappeared.
66	10997929	In laminin-beta(2) mutant mice exhibiting nephrotic syndrome, CD2AP in glomeruli was aberrantly localized in a primarily punctate pattern.
67	10997929	CD2AP is expressed with nephrin in developing podocytes and is found widely in mature kidney and elsewhere.
68	10997929	CD2-associated protein (CD2AP) is an adapter molecule that can bind to the cytoplasmic domain of nephrin, a component of the glomerular slit diaphragm.
69	10997929	Mice lacking CD2AP exhibit a congenital nephrotic syndrome characterized by extensive foot process effacement, suggesting that CD2AP-nephrin interactions are critical to maintaining slit diaphragm function.
70	10997929	We have examined the patterns of expression of both CD2AP and nephrin in developing mouse and human kidney.
71	10997929	Kidneys from Cd2ap -/- mice initially exhibited normal nephrin localization, but as the mice aged and foot processes became effaced, nephrin disappeared.
72	10997929	In laminin-beta(2) mutant mice exhibiting nephrotic syndrome, CD2AP in glomeruli was aberrantly localized in a primarily punctate pattern.
73	11195047	CD2-associated protein and the kidney.
74	11195047	In particular, two proteins, CD2-associated protein and nephrin, have been identified as critical podocyte proteins that are both required for normal glomerular filtration.
75	11195047	CD2-associated protein and the kidney.
76	11195047	In particular, two proteins, CD2-associated protein and nephrin, have been identified as critical podocyte proteins that are both required for normal glomerular filtration.
77	11458036	However, more recent studies on nephrin, a key component of the slit diaphragm, as well as the podocyte and slit diaphragm-associated intracellular proteins, CD2-associated protein, podocin and alpha-actinin-4, have emphasized the role of the slit diaphragm as a central size-selective filtration barrier.
78	11553524	CD2AP and p130Cas localize to different F-actin structures in podocytes.
79	11553524	Mice lacking the 80-kDa CD2-associated protein (CD2AP) develop progressive renal failure that starts soon after birth with proteinuria and foot process effacement by unknown mechanisms.
80	11553524	CD2AP has been identified and cloned independently by virtue of its interaction with the T cell protein CD2 and with the docking protein p130Cas.
81	11553524	In the present study we examined the localization of CD2AP and p130Cas in the mouse glomerulus and in cultured podocytes.
82	11553524	In glomeruli, CD2AP and p130Cas immunofluorescence were observed in podocytes, where they colocalized with F-actin in foot processes.
83	11553524	In cultured podocytes, p130Cas was enriched at sites of focal adhesions, where it colocalized like vinculin with F-actin at stress fiber ends.
84	11553524	The spot-shaped F-actin structures were also stained by antibodies against the actin nucleation Arp2/3 complex and cortactin, both contributing to dynamic actin assembly.
85	11553524	Moreover, CD2AP spots in cultured podocytes were in close spatial association with actinin-4, but not actinin-1.
86	11553524	Our results suggest that CD2AP and p130Cas, which both colocalize with F-actin in podocytes in situ, possess different functions.
87	11553524	Whereas p130Cas is found in focal adhesions, CD2AP seems to be involved in the regulation of highly dynamic F-actin structures in podocyte foot processes.
88	11553524	CD2AP and p130Cas localize to different F-actin structures in podocytes.
89	11553524	Mice lacking the 80-kDa CD2-associated protein (CD2AP) develop progressive renal failure that starts soon after birth with proteinuria and foot process effacement by unknown mechanisms.
90	11553524	CD2AP has been identified and cloned independently by virtue of its interaction with the T cell protein CD2 and with the docking protein p130Cas.
91	11553524	In the present study we examined the localization of CD2AP and p130Cas in the mouse glomerulus and in cultured podocytes.
92	11553524	In glomeruli, CD2AP and p130Cas immunofluorescence were observed in podocytes, where they colocalized with F-actin in foot processes.
93	11553524	In cultured podocytes, p130Cas was enriched at sites of focal adhesions, where it colocalized like vinculin with F-actin at stress fiber ends.
94	11553524	The spot-shaped F-actin structures were also stained by antibodies against the actin nucleation Arp2/3 complex and cortactin, both contributing to dynamic actin assembly.
95	11553524	Moreover, CD2AP spots in cultured podocytes were in close spatial association with actinin-4, but not actinin-1.
96	11553524	Our results suggest that CD2AP and p130Cas, which both colocalize with F-actin in podocytes in situ, possess different functions.
97	11553524	Whereas p130Cas is found in focal adhesions, CD2AP seems to be involved in the regulation of highly dynamic F-actin structures in podocyte foot processes.
98	11553524	CD2AP and p130Cas localize to different F-actin structures in podocytes.
99	11553524	Mice lacking the 80-kDa CD2-associated protein (CD2AP) develop progressive renal failure that starts soon after birth with proteinuria and foot process effacement by unknown mechanisms.
100	11553524	CD2AP has been identified and cloned independently by virtue of its interaction with the T cell protein CD2 and with the docking protein p130Cas.
101	11553524	In the present study we examined the localization of CD2AP and p130Cas in the mouse glomerulus and in cultured podocytes.
102	11553524	In glomeruli, CD2AP and p130Cas immunofluorescence were observed in podocytes, where they colocalized with F-actin in foot processes.
103	11553524	In cultured podocytes, p130Cas was enriched at sites of focal adhesions, where it colocalized like vinculin with F-actin at stress fiber ends.
104	11553524	The spot-shaped F-actin structures were also stained by antibodies against the actin nucleation Arp2/3 complex and cortactin, both contributing to dynamic actin assembly.
105	11553524	Moreover, CD2AP spots in cultured podocytes were in close spatial association with actinin-4, but not actinin-1.
106	11553524	Our results suggest that CD2AP and p130Cas, which both colocalize with F-actin in podocytes in situ, possess different functions.
107	11553524	Whereas p130Cas is found in focal adhesions, CD2AP seems to be involved in the regulation of highly dynamic F-actin structures in podocyte foot processes.
108	11553524	CD2AP and p130Cas localize to different F-actin structures in podocytes.
109	11553524	Mice lacking the 80-kDa CD2-associated protein (CD2AP) develop progressive renal failure that starts soon after birth with proteinuria and foot process effacement by unknown mechanisms.
110	11553524	CD2AP has been identified and cloned independently by virtue of its interaction with the T cell protein CD2 and with the docking protein p130Cas.
111	11553524	In the present study we examined the localization of CD2AP and p130Cas in the mouse glomerulus and in cultured podocytes.
112	11553524	In glomeruli, CD2AP and p130Cas immunofluorescence were observed in podocytes, where they colocalized with F-actin in foot processes.
113	11553524	In cultured podocytes, p130Cas was enriched at sites of focal adhesions, where it colocalized like vinculin with F-actin at stress fiber ends.
114	11553524	The spot-shaped F-actin structures were also stained by antibodies against the actin nucleation Arp2/3 complex and cortactin, both contributing to dynamic actin assembly.
115	11553524	Moreover, CD2AP spots in cultured podocytes were in close spatial association with actinin-4, but not actinin-1.
116	11553524	Our results suggest that CD2AP and p130Cas, which both colocalize with F-actin in podocytes in situ, possess different functions.
117	11553524	Whereas p130Cas is found in focal adhesions, CD2AP seems to be involved in the regulation of highly dynamic F-actin structures in podocyte foot processes.
118	11553524	CD2AP and p130Cas localize to different F-actin structures in podocytes.
119	11553524	Mice lacking the 80-kDa CD2-associated protein (CD2AP) develop progressive renal failure that starts soon after birth with proteinuria and foot process effacement by unknown mechanisms.
120	11553524	CD2AP has been identified and cloned independently by virtue of its interaction with the T cell protein CD2 and with the docking protein p130Cas.
121	11553524	In the present study we examined the localization of CD2AP and p130Cas in the mouse glomerulus and in cultured podocytes.
122	11553524	In glomeruli, CD2AP and p130Cas immunofluorescence were observed in podocytes, where they colocalized with F-actin in foot processes.
123	11553524	In cultured podocytes, p130Cas was enriched at sites of focal adhesions, where it colocalized like vinculin with F-actin at stress fiber ends.
124	11553524	The spot-shaped F-actin structures were also stained by antibodies against the actin nucleation Arp2/3 complex and cortactin, both contributing to dynamic actin assembly.
125	11553524	Moreover, CD2AP spots in cultured podocytes were in close spatial association with actinin-4, but not actinin-1.
126	11553524	Our results suggest that CD2AP and p130Cas, which both colocalize with F-actin in podocytes in situ, possess different functions.
127	11553524	Whereas p130Cas is found in focal adhesions, CD2AP seems to be involved in the regulation of highly dynamic F-actin structures in podocyte foot processes.
128	11553524	CD2AP and p130Cas localize to different F-actin structures in podocytes.
129	11553524	Mice lacking the 80-kDa CD2-associated protein (CD2AP) develop progressive renal failure that starts soon after birth with proteinuria and foot process effacement by unknown mechanisms.
130	11553524	CD2AP has been identified and cloned independently by virtue of its interaction with the T cell protein CD2 and with the docking protein p130Cas.
131	11553524	In the present study we examined the localization of CD2AP and p130Cas in the mouse glomerulus and in cultured podocytes.
132	11553524	In glomeruli, CD2AP and p130Cas immunofluorescence were observed in podocytes, where they colocalized with F-actin in foot processes.
133	11553524	In cultured podocytes, p130Cas was enriched at sites of focal adhesions, where it colocalized like vinculin with F-actin at stress fiber ends.
134	11553524	The spot-shaped F-actin structures were also stained by antibodies against the actin nucleation Arp2/3 complex and cortactin, both contributing to dynamic actin assembly.
135	11553524	Moreover, CD2AP spots in cultured podocytes were in close spatial association with actinin-4, but not actinin-1.
136	11553524	Our results suggest that CD2AP and p130Cas, which both colocalize with F-actin in podocytes in situ, possess different functions.
137	11553524	Whereas p130Cas is found in focal adhesions, CD2AP seems to be involved in the regulation of highly dynamic F-actin structures in podocyte foot processes.
138	11553524	CD2AP and p130Cas localize to different F-actin structures in podocytes.
139	11553524	Mice lacking the 80-kDa CD2-associated protein (CD2AP) develop progressive renal failure that starts soon after birth with proteinuria and foot process effacement by unknown mechanisms.
140	11553524	CD2AP has been identified and cloned independently by virtue of its interaction with the T cell protein CD2 and with the docking protein p130Cas.
141	11553524	In the present study we examined the localization of CD2AP and p130Cas in the mouse glomerulus and in cultured podocytes.
142	11553524	In glomeruli, CD2AP and p130Cas immunofluorescence were observed in podocytes, where they colocalized with F-actin in foot processes.
143	11553524	In cultured podocytes, p130Cas was enriched at sites of focal adhesions, where it colocalized like vinculin with F-actin at stress fiber ends.
144	11553524	The spot-shaped F-actin structures were also stained by antibodies against the actin nucleation Arp2/3 complex and cortactin, both contributing to dynamic actin assembly.
145	11553524	Moreover, CD2AP spots in cultured podocytes were in close spatial association with actinin-4, but not actinin-1.
146	11553524	Our results suggest that CD2AP and p130Cas, which both colocalize with F-actin in podocytes in situ, possess different functions.
147	11553524	Whereas p130Cas is found in focal adhesions, CD2AP seems to be involved in the regulation of highly dynamic F-actin structures in podocyte foot processes.
148	11553524	CD2AP and p130Cas localize to different F-actin structures in podocytes.
149	11553524	Mice lacking the 80-kDa CD2-associated protein (CD2AP) develop progressive renal failure that starts soon after birth with proteinuria and foot process effacement by unknown mechanisms.
150	11553524	CD2AP has been identified and cloned independently by virtue of its interaction with the T cell protein CD2 and with the docking protein p130Cas.
151	11553524	In the present study we examined the localization of CD2AP and p130Cas in the mouse glomerulus and in cultured podocytes.
152	11553524	In glomeruli, CD2AP and p130Cas immunofluorescence were observed in podocytes, where they colocalized with F-actin in foot processes.
153	11553524	In cultured podocytes, p130Cas was enriched at sites of focal adhesions, where it colocalized like vinculin with F-actin at stress fiber ends.
154	11553524	The spot-shaped F-actin structures were also stained by antibodies against the actin nucleation Arp2/3 complex and cortactin, both contributing to dynamic actin assembly.
155	11553524	Moreover, CD2AP spots in cultured podocytes were in close spatial association with actinin-4, but not actinin-1.
156	11553524	Our results suggest that CD2AP and p130Cas, which both colocalize with F-actin in podocytes in situ, possess different functions.
157	11553524	Whereas p130Cas is found in focal adhesions, CD2AP seems to be involved in the regulation of highly dynamic F-actin structures in podocyte foot processes.
158	11562357	Interaction with podocin facilitates nephrin signaling.
159	11562357	Mutations of NPHS1 or NPHS2, the genes encoding for the glomerular podocyte proteins nephrin and podocin, cause steroid-resistant proteinuria.
160	11562357	In addition, mice lacking CD2-associated protein (CD2AP) develop a nephrotic syndrome that resembles NPHS mutations suggesting that all three proteins are essential for the integrity of glomerular podocytes.
161	11562357	Nephrin-induced signaling is greatly enhanced by podocin, which binds to the cytoplasmic tail of nephrin.
162	11562357	Mutational analysis suggests that abnormal or inefficient signaling through the nephrin-podocin complex contributes to the development of podocyte dysfunction and proteinuria.
163	11701993	The identification of nephrin, a component of the slit diaphragm, and the intracellular slit diaphragm associated proteins CD2AP and podocin has demonstrated the existence of proteins that directly contribute to a functional kidney filter.