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UCSC Genome Browser Gene Interaction Graph
Gene interactions and pathways from curated databases and text-mining

◀ Back to IGF1

IGF1 — SHC1

Pathways - manually collected, often from reviews:

Text-mined interactions from Literome

Soon et al., Mol Cell Biol 1999 : Grb2 association with SHC and mitogen activated protein kinase ( MAPK ) activity was also enhanced in response to IGF-I stimulation
Ariga et al., Biochem J 2000 : We found that the IGF-I dependent tyrosine phosphorylation of 66 kDa Shc ( Src homology collagen ) was markedly increased by cAMP pretreatment, and that this change was mainly due to an increase in the levels of 66 kDa Shc protein ... Under these conditions, cAMP pretreatment significantly increased binding of Grb2 ( growth-factor-receptor bound protein 2 ) to Shc in response to IGF-I , and activation of MAP kinase ( mitogen activated protein kinase ) induced by IGF-I was also enhanced by cAMP
Hermanto et al., Mol Cell Biol 2002 : While IGF-I induced activation of IRS-1, Shc , PI3K, and MAPK pathways was unaffected, IGF-I-inducible beta1 integrin associated kinase activity and association of Crk with p130 ( CAS ) were significantly inhibited by RACK1 overexpression
Mincione et al., Exp Cell Res 2003 : Conversely, TGF-beta 1 did not alter IGF-I stimulated IRS-1 associated phosphatidylinositol 3-kinase activity, IGF-I induced tyrosine phosphorylation of Shc , and its binding to Grb2
Biedi et al., Endocrinology 2003 : Here we show that IGF-I induces Shc tyrosine phosphorylation in the caveolae with a time course significantly different from that observed in the nonraft cellular fractions
Panetta et al., Biochem Biophys Res Commun 2004 : Recently, we have demonstrated that IGF-I could specifically regulate Shc phosphorylation in caveolae
Wadsworth et al., Endocrinology 2004 : There was no effect on IGF-I induced phosphorylation of MAPK, IGF-IR, or Shc
Xin et al., Am J Physiol Gastrointest Liver Physiol 2004 (Crohn Disease) : Immunoprecipitation studies demonstrated that IGF-I stimulation resulted in tyrosine phosphorylation of IRS-1, IRS-2, and Shc
Vincent et al., Neurobiol Dis 2004 : IGF-I : IGF-IR signaling involves phosphorylation of IRS-1 and Shc , but not IRS-2
Kiely et al., J Biol Chem 2005 : Shc was not phosphorylated in response to IGF-I in cells expressing the Y1250F/Y1251F mutant and remained associated with protein phosphatase 2A
Maile et al., Mol Endocrinol 2006 : In the presence of this antibody, IGF-I stimulated Shc phosphorylation and ERK 1/2 activation were impaired, and this was associated with an inhibition in the ability of IGF-I to stimulate an increase in migration or proliferation ... This was associated with a loss of IGF-I stimulated Shc phosphorylation and impaired smooth muscle cell proliferation in response to IGF-I
Lieskovska et al., J Biol Chem 2006 (MAP Kinase Signaling System) : Our previous studies have shown that IGF-I induced Shc phosphorylation is necessary for sustained activation of MAPK and increased cell proliferation of SMCs, and both Shc and the tyrosine phosphatase SHP-2 must be recruited to the membrane protein SHPS-1 in order for Shc to be phosphorylated ... These studies were undertaken to determine whether Src kinase activity is required to phosphorylate Shc in response to IGF-I in SMC and because SHP-2 binds to Src whether their interaction was also required for IGF-I stimulated mitogenesis ... Our results show that IGF-I induces activation of Src kinase and that is required for Shc phosphorylation and for optimal MAPK activation ... SMCs expressing an SHP-2 mutant that had the polyproline-rich region of SH2 deleted ( SHP-2Delta10 ) had disrupted SHP-2/Src association, impaired IGF-I dependent Shc phosphorylation, and an attenuated mitogenic response
Maile et al., Endocrinology 2007 (Hyperglycemia) : IGF-I stimulated an increase in Shc phosphorylation and enhanced activation of the MAPK pathway in SMCs grown in 25 mM glucose, whereas in cells maintained in 5 mM glucose, IGF-I had no effect on Shc phosphorylation, and the MAPK response to IGF-I was markedly reduced ... The addition of these alphaVbeta3 ligands to SMCs grown in 5 mM glucose was sufficient to permit IGF-I stimulated Shc phosphorylation and downstream signaling ... Because we have shown previously that alphaVbeta3 ligand occupancy is required for IGF-I stimulated Shc phosphorylation and stimulation of SMC growth, our data are consistent with a model in which 25 mM glucose stimulates increases in the concentrations of these extracellular matrix proteins, thus enhancing alphaVbeta3 ligand occupancy, which leads to increased Shc phosphorylation and enhanced cell migration and proliferation in response to IGF-I
Clemmons et al., Growth Horm IGF Res 2007 (Hyperglycemia) : With hyperglycemia there is a marked increased in alphaVbeta3 ligands and Shc phosphorylation in response to IGF-I is sustained
Salani et al., Endocrinology 2008 : These results demonstrate that : 1 ) Cav-1 down-regulation negatively affects IGF-IR tyrosine phosphorylation ; 2 ) this effect causes a reduced activation of insulin receptor substrate-1, Shc , and Akt ; and 3 ) Cav-1 is involved in IGF-IR antiapoptotic signaling after serum deprivation
Radhakrishnan et al., J Biol Chem 2008 (MAP Kinase Signaling System) : Cellular exposure to 25 mm glucose, which is required for Shc phosphorylation in response to IGF-I , resulted in enhanced Grb2 binding to p85, activation of PI3K activity, and increased AKT phosphorylation as compared with cells exposed to 5 mm glucose
Radhakrishnan et al., J Biol Chem 2010 (MAP Kinase Signaling System) : These cultures showed reduced SHPS-1 phosphorylation, transfer of SHP-2 to SHPS-1, and impaired Shc and MAPK phosphorylation and cell proliferation in response to IGF-I
Tartare-Deckert et al., J Biol Chem 1995 : Our findings can be summarized as follows : ( i ) the tyrosine kinase activity of the IGF-IR is essential for the interaction with p52Shc and IRS-1, ( ii ) p52Shc and IRS-1 bind to the IGF-IR in the NPEY-juxtamembrane motif, ( iii ) contrary to p52Shc, IRS-1 binds also to the major autophosphorylation sites ( Tyr-1131, -1135, and -1136 ) of the IGF-IR, and ( iv ) the amino-terminal domain of p52Shc is required for its association with the IR and the IGF-IR
Giorgetti et al., Eur J Biochem 1994 : Here we approached the insulin induced and the insulin-like-growth-factor-I induced ( IGF-I induced ) phosphorylation of SHC proteins, and the possible role of these proteins in insulin and IGF-I signaling
Sasaoka et al., Endocrinology 1996 : Insulin and IGF-1 stimulated tyrosine phosphorylation of IRS-1 and Shc in a similar dose- and time dependent manner
Esposito et al., Endocrinology 1997 (Cell Transformation, Neoplastic) : IGF-I stimulated autophosphorylation of the IGF-IR and tyrosine phosphorylation of IRS-1 and SHC , known substrates in the IGF-IR signal transduction pathway, were studied
Chow et al., J Biol Chem 1998 : A mutation in the C terminus of the IGF-I receptor decreased both the rate of receptor internalization and IGF-I stimulated Shc phosphorylation by more than 50 %, but did not affect IRS-1 phosphorylation
Kim et al., J Biol Chem 1998 (Neuroblastoma) : Insulin receptor substrate 2 and Shc play different roles in insulin-like growth factor I signaling ... In the current study, we report that IGF-I induces a sustained tyrosine phosphorylation of Shc and its association with Grb2 in SH-SY5Y human neuroblastoma cells