Ignet

Gene Information

Gene symbol: CRK

Gene name: v-crk sarcoma virus CT10 oncogene homolog (avian)

HGNC ID: 2362

Related Genes

#	Gene Symbol	Number of hits
1	ABL1	1 hits
2	CRKL	1 hits
3	DOK4	1 hits
4	GAB1	1 hits
5	GRB2	1 hits
6	HGF	1 hits
7	IGF1	1 hits
8	INS	1 hits
9	INSR	1 hits
10	IRS1	1 hits
11	IRS4	1 hits
12	LCK	1 hits
13	MAPK1	1 hits
14	NCK1	1 hits
15	PIK3CA	1 hits
16	PIK3R1	1 hits
17	PLCG1	1 hits
18	PPP1R13B	1 hits
19	PTPN11	1 hits
20	PXN	1 hits
21	RACGAP1	1 hits
22	RAPGEF1	1 hits
23	RASA1	1 hits
24	SH3YL1	1 hits
25	SHC1	1 hits
26	SRC	1 hits

Related Sentences

#	PMID	Sentence
1	7520528	Second, we demonstrate a direct binding between purified SH2 and SH3 domains of Fyn and Lck Src family kinases.
2	7520528	Heterologous binding between SH2 and SH3 domains of closely related members of the Src family, namely, Fyn, Lck, and Src, was also observed.
3	7520528	In contrast, Grb2, Crk, Abl, p85 phosphatidylinositol 3-kinase, and GTPase-activating protein SH2 domains showed lower or no binding to Fyn or Lck SH3 domains.
4	7520528	SH3-SH2 binding was observed in the presence of proline-rich peptides or when a point mutation (W119K) was introduced in the putative ligand-binding pouch of the Fyn SH3 domain, although these treatments completely abolished the binding to p85 phosphatidylinositol 3-kinase and other SH3-specific polypeptides.
5	7534289	Insulin-like growth factor-I stimulates tyrosine phosphorylation of endogenous c-Crk.
6	7534289	Crk, a cellular homolog of v-crk, is an SH2 and SH3 domain-containing adaptor protein related to Grb2 and Nck, two proteins which have been shown to be involved in growth factor signal transduction.
7	7534289	Crk proteins have recently been found to associate with two guanine nucleotide releasing proteins, mSos and C3G, and thus appear to lie on the Ras pathway.
8	7534289	We investigated whether Crk is a target for the insulin-like growth factor I (IGF-I) receptor tyrosine kinase.
9	7534289	We show that IGF-I stimulates tyrosine phosphorylation of Crk II via stimulation of endogenous IGF-I receptors in both 293 cells and NIH-3T3 cells.
10	7534289	IGF-I stimulated tyrosine phosphorylation of Crk II in a dose- and time-dependent manner.
11	7534289	In 293 cells, which express both IGF-I and insulin receptors, insulin also induced a dose-dependent tyrosine phosphorylation of Crk II, but with somewhat reduced sensitivity, compared to IGF-I.
12	7534289	In NIH 3T3 cells, IGF-I also stimulated tyrosine phosphorylation of a 45- kDa protein which co-immunoprecipitated with Crk II.
13	7534289	These findings indicate that Crk II is an endogenous substrate of the IGF-I receptor tyrosine kinase and provide the first demonstration that a mitogenic growth factor induces tyrosine phosphorylation of endogenous c-Crk.
14	7534289	Insulin-like growth factor-I stimulates tyrosine phosphorylation of endogenous c-Crk.
15	7534289	Crk, a cellular homolog of v-crk, is an SH2 and SH3 domain-containing adaptor protein related to Grb2 and Nck, two proteins which have been shown to be involved in growth factor signal transduction.
16	7534289	Crk proteins have recently been found to associate with two guanine nucleotide releasing proteins, mSos and C3G, and thus appear to lie on the Ras pathway.
17	7534289	We investigated whether Crk is a target for the insulin-like growth factor I (IGF-I) receptor tyrosine kinase.
18	7534289	We show that IGF-I stimulates tyrosine phosphorylation of Crk II via stimulation of endogenous IGF-I receptors in both 293 cells and NIH-3T3 cells.
19	7534289	IGF-I stimulated tyrosine phosphorylation of Crk II in a dose- and time-dependent manner.
20	7534289	In 293 cells, which express both IGF-I and insulin receptors, insulin also induced a dose-dependent tyrosine phosphorylation of Crk II, but with somewhat reduced sensitivity, compared to IGF-I.
21	7534289	In NIH 3T3 cells, IGF-I also stimulated tyrosine phosphorylation of a 45- kDa protein which co-immunoprecipitated with Crk II.
22	7534289	These findings indicate that Crk II is an endogenous substrate of the IGF-I receptor tyrosine kinase and provide the first demonstration that a mitogenic growth factor induces tyrosine phosphorylation of endogenous c-Crk.
23	7534289	Insulin-like growth factor-I stimulates tyrosine phosphorylation of endogenous c-Crk.
24	7534289	Crk, a cellular homolog of v-crk, is an SH2 and SH3 domain-containing adaptor protein related to Grb2 and Nck, two proteins which have been shown to be involved in growth factor signal transduction.
25	7534289	Crk proteins have recently been found to associate with two guanine nucleotide releasing proteins, mSos and C3G, and thus appear to lie on the Ras pathway.
26	7534289	We investigated whether Crk is a target for the insulin-like growth factor I (IGF-I) receptor tyrosine kinase.
27	7534289	We show that IGF-I stimulates tyrosine phosphorylation of Crk II via stimulation of endogenous IGF-I receptors in both 293 cells and NIH-3T3 cells.
28	7534289	IGF-I stimulated tyrosine phosphorylation of Crk II in a dose- and time-dependent manner.
29	7534289	In 293 cells, which express both IGF-I and insulin receptors, insulin also induced a dose-dependent tyrosine phosphorylation of Crk II, but with somewhat reduced sensitivity, compared to IGF-I.
30	7534289	In NIH 3T3 cells, IGF-I also stimulated tyrosine phosphorylation of a 45- kDa protein which co-immunoprecipitated with Crk II.
31	7534289	These findings indicate that Crk II is an endogenous substrate of the IGF-I receptor tyrosine kinase and provide the first demonstration that a mitogenic growth factor induces tyrosine phosphorylation of endogenous c-Crk.
32	7534289	Insulin-like growth factor-I stimulates tyrosine phosphorylation of endogenous c-Crk.
33	7534289	Crk, a cellular homolog of v-crk, is an SH2 and SH3 domain-containing adaptor protein related to Grb2 and Nck, two proteins which have been shown to be involved in growth factor signal transduction.
34	7534289	Crk proteins have recently been found to associate with two guanine nucleotide releasing proteins, mSos and C3G, and thus appear to lie on the Ras pathway.
35	7534289	We investigated whether Crk is a target for the insulin-like growth factor I (IGF-I) receptor tyrosine kinase.
36	7534289	We show that IGF-I stimulates tyrosine phosphorylation of Crk II via stimulation of endogenous IGF-I receptors in both 293 cells and NIH-3T3 cells.
37	7534289	IGF-I stimulated tyrosine phosphorylation of Crk II in a dose- and time-dependent manner.
38	7534289	In 293 cells, which express both IGF-I and insulin receptors, insulin also induced a dose-dependent tyrosine phosphorylation of Crk II, but with somewhat reduced sensitivity, compared to IGF-I.
39	7534289	In NIH 3T3 cells, IGF-I also stimulated tyrosine phosphorylation of a 45- kDa protein which co-immunoprecipitated with Crk II.
40	7534289	These findings indicate that Crk II is an endogenous substrate of the IGF-I receptor tyrosine kinase and provide the first demonstration that a mitogenic growth factor induces tyrosine phosphorylation of endogenous c-Crk.
41	7534289	Insulin-like growth factor-I stimulates tyrosine phosphorylation of endogenous c-Crk.
42	7534289	Crk, a cellular homolog of v-crk, is an SH2 and SH3 domain-containing adaptor protein related to Grb2 and Nck, two proteins which have been shown to be involved in growth factor signal transduction.
43	7534289	Crk proteins have recently been found to associate with two guanine nucleotide releasing proteins, mSos and C3G, and thus appear to lie on the Ras pathway.
44	7534289	We investigated whether Crk is a target for the insulin-like growth factor I (IGF-I) receptor tyrosine kinase.
45	7534289	We show that IGF-I stimulates tyrosine phosphorylation of Crk II via stimulation of endogenous IGF-I receptors in both 293 cells and NIH-3T3 cells.
46	7534289	IGF-I stimulated tyrosine phosphorylation of Crk II in a dose- and time-dependent manner.
47	7534289	In 293 cells, which express both IGF-I and insulin receptors, insulin also induced a dose-dependent tyrosine phosphorylation of Crk II, but with somewhat reduced sensitivity, compared to IGF-I.
48	7534289	In NIH 3T3 cells, IGF-I also stimulated tyrosine phosphorylation of a 45- kDa protein which co-immunoprecipitated with Crk II.
49	7534289	These findings indicate that Crk II is an endogenous substrate of the IGF-I receptor tyrosine kinase and provide the first demonstration that a mitogenic growth factor induces tyrosine phosphorylation of endogenous c-Crk.
50	7534289	Insulin-like growth factor-I stimulates tyrosine phosphorylation of endogenous c-Crk.
51	7534289	Crk, a cellular homolog of v-crk, is an SH2 and SH3 domain-containing adaptor protein related to Grb2 and Nck, two proteins which have been shown to be involved in growth factor signal transduction.
52	7534289	Crk proteins have recently been found to associate with two guanine nucleotide releasing proteins, mSos and C3G, and thus appear to lie on the Ras pathway.
53	7534289	We investigated whether Crk is a target for the insulin-like growth factor I (IGF-I) receptor tyrosine kinase.
54	7534289	We show that IGF-I stimulates tyrosine phosphorylation of Crk II via stimulation of endogenous IGF-I receptors in both 293 cells and NIH-3T3 cells.
55	7534289	IGF-I stimulated tyrosine phosphorylation of Crk II in a dose- and time-dependent manner.
56	7534289	In 293 cells, which express both IGF-I and insulin receptors, insulin also induced a dose-dependent tyrosine phosphorylation of Crk II, but with somewhat reduced sensitivity, compared to IGF-I.
57	7534289	In NIH 3T3 cells, IGF-I also stimulated tyrosine phosphorylation of a 45- kDa protein which co-immunoprecipitated with Crk II.
58	7534289	These findings indicate that Crk II is an endogenous substrate of the IGF-I receptor tyrosine kinase and provide the first demonstration that a mitogenic growth factor induces tyrosine phosphorylation of endogenous c-Crk.
59	7534289	Insulin-like growth factor-I stimulates tyrosine phosphorylation of endogenous c-Crk.
60	7534289	Crk, a cellular homolog of v-crk, is an SH2 and SH3 domain-containing adaptor protein related to Grb2 and Nck, two proteins which have been shown to be involved in growth factor signal transduction.
61	7534289	Crk proteins have recently been found to associate with two guanine nucleotide releasing proteins, mSos and C3G, and thus appear to lie on the Ras pathway.
62	7534289	We investigated whether Crk is a target for the insulin-like growth factor I (IGF-I) receptor tyrosine kinase.
63	7534289	We show that IGF-I stimulates tyrosine phosphorylation of Crk II via stimulation of endogenous IGF-I receptors in both 293 cells and NIH-3T3 cells.
64	7534289	IGF-I stimulated tyrosine phosphorylation of Crk II in a dose- and time-dependent manner.
65	7534289	In 293 cells, which express both IGF-I and insulin receptors, insulin also induced a dose-dependent tyrosine phosphorylation of Crk II, but with somewhat reduced sensitivity, compared to IGF-I.
66	7534289	In NIH 3T3 cells, IGF-I also stimulated tyrosine phosphorylation of a 45- kDa protein which co-immunoprecipitated with Crk II.
67	7534289	These findings indicate that Crk II is an endogenous substrate of the IGF-I receptor tyrosine kinase and provide the first demonstration that a mitogenic growth factor induces tyrosine phosphorylation of endogenous c-Crk.
68	7534289	Insulin-like growth factor-I stimulates tyrosine phosphorylation of endogenous c-Crk.
69	7534289	Crk, a cellular homolog of v-crk, is an SH2 and SH3 domain-containing adaptor protein related to Grb2 and Nck, two proteins which have been shown to be involved in growth factor signal transduction.
70	7534289	Crk proteins have recently been found to associate with two guanine nucleotide releasing proteins, mSos and C3G, and thus appear to lie on the Ras pathway.
71	7534289	We investigated whether Crk is a target for the insulin-like growth factor I (IGF-I) receptor tyrosine kinase.
72	7534289	We show that IGF-I stimulates tyrosine phosphorylation of Crk II via stimulation of endogenous IGF-I receptors in both 293 cells and NIH-3T3 cells.
73	7534289	IGF-I stimulated tyrosine phosphorylation of Crk II in a dose- and time-dependent manner.
74	7534289	In 293 cells, which express both IGF-I and insulin receptors, insulin also induced a dose-dependent tyrosine phosphorylation of Crk II, but with somewhat reduced sensitivity, compared to IGF-I.
75	7534289	In NIH 3T3 cells, IGF-I also stimulated tyrosine phosphorylation of a 45- kDa protein which co-immunoprecipitated with Crk II.
76	7534289	These findings indicate that Crk II is an endogenous substrate of the IGF-I receptor tyrosine kinase and provide the first demonstration that a mitogenic growth factor induces tyrosine phosphorylation of endogenous c-Crk.
77	9346905	In vivo regulation of CrkII and CrkL proto-oncogenes in the uterus by insulin-like growth factor-I.
78	9346905	Changes in CrkII and CrkL phosphorylation are associated with insulin-like growth factor receptor activation in cultured cells.
79	9346905	We examined whether similar changes also occur following administration of recombinant human insulin-like growth factor-I to the intact animal.
80	9346905	In female rats starved overnight, CrkL phosphorylation was significantly increased 12 min after insulin-like growth factor-I administration.
81	9346905	Paxillin, a 65-70-kDa phosphoprotein containing high affinity binding sites common for the Src homology 2 (SH2) domains of CrkII and CrkL, was observed in both CrkII and CrkL immunoprecipitates.
82	9346905	Insulin-like growth factor-I treatment stimulated the association of CrkII with paxillin.
83	9346905	Similar effects of insulin-like growth factor-I treatment on the association of CrkL with tyrosine phosphorylated paxillin were observed in fibroblasts overexpressing CrkL.
84	9346905	This study demonstrates that the activation of the insulin-like growth factor-I receptor induces changes in the tyrosine phosphorylation and protein-protein interactions of the Crk proteins in vivo.
85	9346905	The different responses of CrkL and CrkII to insulin-like growth factor-I receptor activation suggest distinct roles for these two adapter proteins in signal transduction.
86	9346905	In vivo regulation of CrkII and CrkL proto-oncogenes in the uterus by insulin-like growth factor-I.
87	9346905	Changes in CrkII and CrkL phosphorylation are associated with insulin-like growth factor receptor activation in cultured cells.
88	9346905	We examined whether similar changes also occur following administration of recombinant human insulin-like growth factor-I to the intact animal.
89	9346905	In female rats starved overnight, CrkL phosphorylation was significantly increased 12 min after insulin-like growth factor-I administration.
90	9346905	Paxillin, a 65-70-kDa phosphoprotein containing high affinity binding sites common for the Src homology 2 (SH2) domains of CrkII and CrkL, was observed in both CrkII and CrkL immunoprecipitates.
91	9346905	Insulin-like growth factor-I treatment stimulated the association of CrkII with paxillin.
92	9346905	Similar effects of insulin-like growth factor-I treatment on the association of CrkL with tyrosine phosphorylated paxillin were observed in fibroblasts overexpressing CrkL.
93	9346905	This study demonstrates that the activation of the insulin-like growth factor-I receptor induces changes in the tyrosine phosphorylation and protein-protein interactions of the Crk proteins in vivo.
94	9346905	The different responses of CrkL and CrkII to insulin-like growth factor-I receptor activation suggest distinct roles for these two adapter proteins in signal transduction.
95	9346905	In vivo regulation of CrkII and CrkL proto-oncogenes in the uterus by insulin-like growth factor-I.
96	9346905	Changes in CrkII and CrkL phosphorylation are associated with insulin-like growth factor receptor activation in cultured cells.
97	9346905	We examined whether similar changes also occur following administration of recombinant human insulin-like growth factor-I to the intact animal.
98	9346905	In female rats starved overnight, CrkL phosphorylation was significantly increased 12 min after insulin-like growth factor-I administration.
99	9346905	Paxillin, a 65-70-kDa phosphoprotein containing high affinity binding sites common for the Src homology 2 (SH2) domains of CrkII and CrkL, was observed in both CrkII and CrkL immunoprecipitates.
100	9346905	Insulin-like growth factor-I treatment stimulated the association of CrkII with paxillin.
101	9346905	Similar effects of insulin-like growth factor-I treatment on the association of CrkL with tyrosine phosphorylated paxillin were observed in fibroblasts overexpressing CrkL.
102	9346905	This study demonstrates that the activation of the insulin-like growth factor-I receptor induces changes in the tyrosine phosphorylation and protein-protein interactions of the Crk proteins in vivo.
103	9346905	The different responses of CrkL and CrkII to insulin-like growth factor-I receptor activation suggest distinct roles for these two adapter proteins in signal transduction.
104	9346905	In vivo regulation of CrkII and CrkL proto-oncogenes in the uterus by insulin-like growth factor-I.
105	9346905	Changes in CrkII and CrkL phosphorylation are associated with insulin-like growth factor receptor activation in cultured cells.
106	9346905	We examined whether similar changes also occur following administration of recombinant human insulin-like growth factor-I to the intact animal.
107	9346905	In female rats starved overnight, CrkL phosphorylation was significantly increased 12 min after insulin-like growth factor-I administration.
108	9346905	Paxillin, a 65-70-kDa phosphoprotein containing high affinity binding sites common for the Src homology 2 (SH2) domains of CrkII and CrkL, was observed in both CrkII and CrkL immunoprecipitates.
109	9346905	Insulin-like growth factor-I treatment stimulated the association of CrkII with paxillin.
110	9346905	Similar effects of insulin-like growth factor-I treatment on the association of CrkL with tyrosine phosphorylated paxillin were observed in fibroblasts overexpressing CrkL.
111	9346905	This study demonstrates that the activation of the insulin-like growth factor-I receptor induces changes in the tyrosine phosphorylation and protein-protein interactions of the Crk proteins in vivo.
112	9346905	The different responses of CrkL and CrkII to insulin-like growth factor-I receptor activation suggest distinct roles for these two adapter proteins in signal transduction.
113	9346905	In vivo regulation of CrkII and CrkL proto-oncogenes in the uterus by insulin-like growth factor-I.
114	9346905	Changes in CrkII and CrkL phosphorylation are associated with insulin-like growth factor receptor activation in cultured cells.
115	9346905	We examined whether similar changes also occur following administration of recombinant human insulin-like growth factor-I to the intact animal.
116	9346905	In female rats starved overnight, CrkL phosphorylation was significantly increased 12 min after insulin-like growth factor-I administration.
117	9346905	Paxillin, a 65-70-kDa phosphoprotein containing high affinity binding sites common for the Src homology 2 (SH2) domains of CrkII and CrkL, was observed in both CrkII and CrkL immunoprecipitates.
118	9346905	Insulin-like growth factor-I treatment stimulated the association of CrkII with paxillin.
119	9346905	Similar effects of insulin-like growth factor-I treatment on the association of CrkL with tyrosine phosphorylated paxillin were observed in fibroblasts overexpressing CrkL.
120	9346905	This study demonstrates that the activation of the insulin-like growth factor-I receptor induces changes in the tyrosine phosphorylation and protein-protein interactions of the Crk proteins in vivo.
121	9346905	The different responses of CrkL and CrkII to insulin-like growth factor-I receptor activation suggest distinct roles for these two adapter proteins in signal transduction.
122	9480911	Interaction in vitro of the product of the c-Crk-II proto-oncogene with the insulin-like growth factor I receptor.
123	9480911	The Crk proto-oncogene product is an SH2 and SH3 domain-containing adaptor protein.
124	9480911	We have previously demonstrated that Crk-II becomes rapidly tyrosine-phosphorylated in response to stimulation with insulin-like growth factor I (IGF-I) and might be involved in the IGF-I receptor signalling pathway.
125	9480911	To determine whether this involvement includes the direct interaction of Crk-II with the cytoplasmic region of the receptor, studies were performed in vitro with glutathione S-transferase (GST) fusion proteins containing various domains of Crk-II.
126	9480911	The kinase assay in vitro showed that activated IGF-I receptors efficiently phosphorylated the GST-Crk-II fusion protein.
127	9480911	Different domains of the IGF-I receptor were expressed as (His)6-tagged fusion peptides, phosphorylated with activated wheat germ agglutinin-purified IGF-I receptors and tested for association with GST-Crk-II fusion proteins.
128	9614078	Interplay of the proto-oncogene proteins CrkL and CrkII in insulin-like growth factor-I receptor-mediated signal transduction.
129	9614078	The closely related proto-oncogene proteins CrkII and CrkL consist of one SH2 and two SH3 domains and share 60% overall homology with the highest identity within their functional domains.
130	9614078	In this study we show that CrkL and CrkII may play overlapping but different roles in insulin-like growth factor (IGF)-I receptor-mediated signal transduction.
131	9614078	Evidence supporting this hypothesis includes (a) the oncogenic potential of CrkL versus the absence of this potential in CrkII overexpressing cell lines, (b) the inhibition of IGF-I-dependent cell cycle progression by overexpression of CrkII, and (c) the differential regulation of the phosphorylation status of selective proteins in CrkII and CrkL overexpressing cell lines.
132	9614078	In addition we demonstrate the specific association of CrkL and CrkII with the newly characterized IRS-4 protein, again in a differential manner.
133	9614078	Whereas CrkL strongly interacts with IRS-4 via its SH2 and N-terminal SH3 domains, CrkII interacts only via its SH2 domain, possibly explaining the unstable nature of IRS-4-CrkII association.
134	9614078	The results obtained allow us to propose a unique mechanism of CrkL and CrkII tyrosine phosphorylation in response to IGF-I stimulation.
135	9614078	Interplay of the proto-oncogene proteins CrkL and CrkII in insulin-like growth factor-I receptor-mediated signal transduction.
136	9614078	The closely related proto-oncogene proteins CrkII and CrkL consist of one SH2 and two SH3 domains and share 60% overall homology with the highest identity within their functional domains.
137	9614078	In this study we show that CrkL and CrkII may play overlapping but different roles in insulin-like growth factor (IGF)-I receptor-mediated signal transduction.
138	9614078	Evidence supporting this hypothesis includes (a) the oncogenic potential of CrkL versus the absence of this potential in CrkII overexpressing cell lines, (b) the inhibition of IGF-I-dependent cell cycle progression by overexpression of CrkII, and (c) the differential regulation of the phosphorylation status of selective proteins in CrkII and CrkL overexpressing cell lines.
139	9614078	In addition we demonstrate the specific association of CrkL and CrkII with the newly characterized IRS-4 protein, again in a differential manner.
140	9614078	Whereas CrkL strongly interacts with IRS-4 via its SH2 and N-terminal SH3 domains, CrkII interacts only via its SH2 domain, possibly explaining the unstable nature of IRS-4-CrkII association.
141	9614078	The results obtained allow us to propose a unique mechanism of CrkL and CrkII tyrosine phosphorylation in response to IGF-I stimulation.
142	9614078	Interplay of the proto-oncogene proteins CrkL and CrkII in insulin-like growth factor-I receptor-mediated signal transduction.
143	9614078	The closely related proto-oncogene proteins CrkII and CrkL consist of one SH2 and two SH3 domains and share 60% overall homology with the highest identity within their functional domains.
144	9614078	In this study we show that CrkL and CrkII may play overlapping but different roles in insulin-like growth factor (IGF)-I receptor-mediated signal transduction.
145	9614078	Evidence supporting this hypothesis includes (a) the oncogenic potential of CrkL versus the absence of this potential in CrkII overexpressing cell lines, (b) the inhibition of IGF-I-dependent cell cycle progression by overexpression of CrkII, and (c) the differential regulation of the phosphorylation status of selective proteins in CrkII and CrkL overexpressing cell lines.
146	9614078	In addition we demonstrate the specific association of CrkL and CrkII with the newly characterized IRS-4 protein, again in a differential manner.
147	9614078	Whereas CrkL strongly interacts with IRS-4 via its SH2 and N-terminal SH3 domains, CrkII interacts only via its SH2 domain, possibly explaining the unstable nature of IRS-4-CrkII association.
148	9614078	The results obtained allow us to propose a unique mechanism of CrkL and CrkII tyrosine phosphorylation in response to IGF-I stimulation.
149	9614078	Interplay of the proto-oncogene proteins CrkL and CrkII in insulin-like growth factor-I receptor-mediated signal transduction.
150	9614078	The closely related proto-oncogene proteins CrkII and CrkL consist of one SH2 and two SH3 domains and share 60% overall homology with the highest identity within their functional domains.
151	9614078	In this study we show that CrkL and CrkII may play overlapping but different roles in insulin-like growth factor (IGF)-I receptor-mediated signal transduction.
152	9614078	Evidence supporting this hypothesis includes (a) the oncogenic potential of CrkL versus the absence of this potential in CrkII overexpressing cell lines, (b) the inhibition of IGF-I-dependent cell cycle progression by overexpression of CrkII, and (c) the differential regulation of the phosphorylation status of selective proteins in CrkII and CrkL overexpressing cell lines.
153	9614078	In addition we demonstrate the specific association of CrkL and CrkII with the newly characterized IRS-4 protein, again in a differential manner.
154	9614078	Whereas CrkL strongly interacts with IRS-4 via its SH2 and N-terminal SH3 domains, CrkII interacts only via its SH2 domain, possibly explaining the unstable nature of IRS-4-CrkII association.
155	9614078	The results obtained allow us to propose a unique mechanism of CrkL and CrkII tyrosine phosphorylation in response to IGF-I stimulation.
156	9614078	Interplay of the proto-oncogene proteins CrkL and CrkII in insulin-like growth factor-I receptor-mediated signal transduction.
157	9614078	The closely related proto-oncogene proteins CrkII and CrkL consist of one SH2 and two SH3 domains and share 60% overall homology with the highest identity within their functional domains.
158	9614078	In this study we show that CrkL and CrkII may play overlapping but different roles in insulin-like growth factor (IGF)-I receptor-mediated signal transduction.
159	9614078	Evidence supporting this hypothesis includes (a) the oncogenic potential of CrkL versus the absence of this potential in CrkII overexpressing cell lines, (b) the inhibition of IGF-I-dependent cell cycle progression by overexpression of CrkII, and (c) the differential regulation of the phosphorylation status of selective proteins in CrkII and CrkL overexpressing cell lines.
160	9614078	In addition we demonstrate the specific association of CrkL and CrkII with the newly characterized IRS-4 protein, again in a differential manner.
161	9614078	Whereas CrkL strongly interacts with IRS-4 via its SH2 and N-terminal SH3 domains, CrkII interacts only via its SH2 domain, possibly explaining the unstable nature of IRS-4-CrkII association.
162	9614078	The results obtained allow us to propose a unique mechanism of CrkL and CrkII tyrosine phosphorylation in response to IGF-I stimulation.
163	9614078	Interplay of the proto-oncogene proteins CrkL and CrkII in insulin-like growth factor-I receptor-mediated signal transduction.
164	9614078	The closely related proto-oncogene proteins CrkII and CrkL consist of one SH2 and two SH3 domains and share 60% overall homology with the highest identity within their functional domains.
165	9614078	In this study we show that CrkL and CrkII may play overlapping but different roles in insulin-like growth factor (IGF)-I receptor-mediated signal transduction.
166	9614078	Evidence supporting this hypothesis includes (a) the oncogenic potential of CrkL versus the absence of this potential in CrkII overexpressing cell lines, (b) the inhibition of IGF-I-dependent cell cycle progression by overexpression of CrkII, and (c) the differential regulation of the phosphorylation status of selective proteins in CrkII and CrkL overexpressing cell lines.
167	9614078	In addition we demonstrate the specific association of CrkL and CrkII with the newly characterized IRS-4 protein, again in a differential manner.
168	9614078	Whereas CrkL strongly interacts with IRS-4 via its SH2 and N-terminal SH3 domains, CrkII interacts only via its SH2 domain, possibly explaining the unstable nature of IRS-4-CrkII association.
169	9614078	The results obtained allow us to propose a unique mechanism of CrkL and CrkII tyrosine phosphorylation in response to IGF-I stimulation.
170	9614078	Interplay of the proto-oncogene proteins CrkL and CrkII in insulin-like growth factor-I receptor-mediated signal transduction.
171	9614078	The closely related proto-oncogene proteins CrkII and CrkL consist of one SH2 and two SH3 domains and share 60% overall homology with the highest identity within their functional domains.
172	9614078	In this study we show that CrkL and CrkII may play overlapping but different roles in insulin-like growth factor (IGF)-I receptor-mediated signal transduction.
173	9614078	Evidence supporting this hypothesis includes (a) the oncogenic potential of CrkL versus the absence of this potential in CrkII overexpressing cell lines, (b) the inhibition of IGF-I-dependent cell cycle progression by overexpression of CrkII, and (c) the differential regulation of the phosphorylation status of selective proteins in CrkII and CrkL overexpressing cell lines.
174	9614078	In addition we demonstrate the specific association of CrkL and CrkII with the newly characterized IRS-4 protein, again in a differential manner.
175	9614078	Whereas CrkL strongly interacts with IRS-4 via its SH2 and N-terminal SH3 domains, CrkII interacts only via its SH2 domain, possibly explaining the unstable nature of IRS-4-CrkII association.
176	9614078	The results obtained allow us to propose a unique mechanism of CrkL and CrkII tyrosine phosphorylation in response to IGF-I stimulation.
177	9972281	Insulin-like growth factor-I receptor signal transduction: at the interface between physiology and cell biology.
178	9972281	The insulin-like growth factor-I receptor (IGF-IR) mediates the biological actions of IGF-I and IGF-II.
179	9972281	The insulin-receptor substrate (IRS), SHC, GRB2, CRKII and CRKL adaptor proteins have all been implicated in transmitting signals to the nucleus of the cell.
180	10660596	Tyrosine dephosphorylation and deactivation of insulin receptor substrate-1 by protein-tyrosine phosphatase 1B.
181	10660596	The specific activity of four candidate protein-tyrosine phosphatases (protein-tyrosine phosphatase 1B (PTP1B), SH2 domain-containing PTPase-2 (SHP-2), leukocyte common antigen-related (LAR), and leukocyte antigen-related phosphatase) (LRP) toward IRS-1 dephosphorylation was studied using recombinant proteins in vitro.
182	10660596	When evaluated as a ratio of activity versus IRS-1 to that versus p-nitrophenyl phosphate, PTP1B remained significantly more active by 3.1-293-fold, respectively.
183	10660596	Overlay blots with recombinant Src homology 2 domains of IRS-1 adaptor proteins showed that the loss of IRS-1 binding of Crk, GRB2, SHP-2, and the p85 subunit of phosphatidylinositol 3'-kinase paralleled the rate of overall IRS-1 dephosphorylation.
184	10660596	Further studies revealed that the adaptor protein GRB2 strongly promoted the formation of a stable protein complex between tyrosine-phosphorylated IRS-1 and catalytically inactive PTP1B, increasing their co-immunoprecipitation from an equimolar solution by 13.5 +/- 3.3-fold (n = 7; p < 0.01).
185	10660596	Inclusion of GRB2 in a reaction mixture of IRS-1 and active PTP1B also increased the overall rate of IRS-1 tyrosine dephosphorylation by 2.7-3.9-fold (p < 0.01).
186	10660596	These results provide new insight into novel molecular interactions involving PTP1B and GRB2 that may influence the steady-state capacity of IRS-1 to function as a phosphotyrosine scaffold and possibly affect the balance of postreceptor insulin signaling.
187	12730241	Because the other known PH-PTB proteins (insulin receptor substrates: IRS-1, IRS-2, IRS-3, and IRS-4, and the downstream of kinases: DOK-1, DOK-2, and DOK-3) are substrates of insulin and insulin-like growth factor (IGF)-1 receptors, we asked whether these new proteins, termed IRS5/DOK4 and IRS6/DOK5, might also have roles in insulin and IGF-1 signaling.
188	12730241	Both proteins are tyrosine-phosphorylated in response to insulin and IGF-1 in transfected cells, although the kinetics differ.
189	12730241	Insulin receptor-phosphorylated IRS5/DOK4 associates with RasGAP, Crk, Src, and Fyn, but not phosphatidylinositol 3-kinase p85, Grb2, SHP-2, Nck, or phospholipase Cgamma Src homology 2 domains, and activates MAPK in cells.
190	12730241	IRS5/DOK4 and IRS6/DOK5 represent two new signaling proteins with potential roles in insulin and IGF-1 action.
191	16185843	The scaffolding/adapter protein, Gab1, is a key signaling molecule for numerous stimuli including growth factors and G protein-coupled-receptors (GPCRs).
192	16185843	HGF and EGF stimulated total Gab1 tyrosine phosphorylation (TyrP) and TyrP of Gab1 phospho-specific sites (Y307, Y627), but not other pancreatic growth factors, GI GPCRs (CCK, bombesin, carbachol, VIP, secretin), or agents directly activating PKC or increasing Ca2+.
193	16185843	HGF-stimulated Y307 Gab1 TyrP differed in kinetics from total and Y627.
194	16185843	In unstimulated cells>95% of Gab1 was cytosolic and HGF stimulated a 3-fold increase in membrane Gab1.
195	16185843	HGF stimulated equal increases in pY307 and pY627 Gab1 in cytosol/membrane.
196	16185843	HGF stimulated Gab1 association with c-Met, Grb2, SHP2, PI3K, Shc, Crk isoforms and CrkL, but not with PLCgamma1.
197	16185843	These results demonstrate that only a subset of pancreatic growth factors (HGF/EGF) stimulates Gab1 signaling and no pancreatic hormones/neurotransmitters.