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IGF1R phosphorylates IRS1 on tyrosine. 16 / 20
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"IGF-I rapidly stimulated beta-chain IGF-I receptor autophosphorylation, which peaked at a physiological and mitogenic concentration (1.4 nM) and also stimulated tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1)."

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"Notably, IGF-1R also phosphorylates tyrosine residues of IRS1 and Shc, creating docking platforms for PI3K and Grb2, which activate the Akt and ERK pathways, respectively [54]."

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"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."

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"Evidence of an EGFR-IRS-1 interaction arises from reports by Fujioka and colleagues [XREF_BIBR, XREF_BIBR], who reported that the phosphorylated NPXY motifs in activated IR and IGF-IR to which IRS molecules bind are also present in the C-terminus region of activated EGFR and were indispensable for EGF induced IRS-1 tyrosine phosphorylation in EGFR transfected CHO cells [XREF_BIBR]."

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"IGF-1R is a tyrosine kinase receptor that is activated by IGFs, the activated IGF-1R not only phosphorylates IRS-1 and SHC to activate the MAPK cascade, which stimulates cell growth and proliferation [XREF_BIBR], but also protects from apoptosis as a result of activation of PI3K-Akt through phosphorylation and subsequent inactivation of BAD [XREF_BIBR]."

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"IGF-1R phosphorylates the insulin receptor substrate-1 (IRS-1) at the tyrosine site, leading to aberrant activation of downstream signaling pathways, such as the PI3K/Akt pathway [ 19–21 ]."

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"Phosphorylation of various tyrosine residues on IRS-1 by IR or IGF-1R creates docking sites for several SH2 domain-containing proteins, such as growth factor receptor binding protein-2 (Grb2), the p85[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Upon binding of IGF-I or IGF-II, IGF-1R, a tyrosine kinase, phosphorylates tyrosine residues on two major substrates, IRS-1 and Shc, which subsequently signal through the Ras and Raf and PI 3-kinase/AKT pathways (7)."

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"Phosphorylation of various tyrosine residues on IRS-1 by IR or IGF-1R creates docking sites for several SH2 domain-containing proteins, such as growth factor receptor binding protein-2 (Grb2), the p85[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"In immature rat GCs, FSH signals via its G protein coupled receptor to promote the protein kinase A (PKA)-dependent activation of the PI3K pathway by regulating the tyrosine phosphorylation of IRS1 by the IGF 1 R."

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"Then, IGF-1R phosphorylates IRS1 and Shc on tyrosine residues [ xref ], forming docking sites for PI3K and GRB2, and activating Akt and ERK pathways, respectively [ xref ] ( xref )."

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"When cells are only stimulated by IGF-I, the IGF-IR induces the tyrosine phosphorylation of IRS-1 which recruits docking proteins such as PI 3-kinase and initiates specific IGF downstream signaling pa[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Downregulation of beta 1 blocks IGF stimulated cell proliferation and transformation of prostate cancer cells, but the effect of beta 1 downregulation on activation of IGF-IR and tyrosine phosphorylation of insulin receptor substrate 1 (IRS-1) has never been described."

sparser
"Notably, IGF-1R also phosphorylates tyrosine residues of IRS1 and Shc, creating docking platforms for PI3K and Grb2, which activate the Akt and ERK pathways, respectively [ xref ]."

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"On ligand stimulation, IGF-IR, a receptor tyrosine kinase, phosphorylates tyrosine residues on two major substrates, IRS-1 and Shc, which subsequently signal through the Ras and mitogen activated protein kinase and phosphatidylinositol 3-kinase/AKT pathways."

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"Insulin like growth factor 1 receptor is an RTK, and phosphorylates multiple tyrosine residues of IRS1 to activate PI3K and its downstream signal pathway including Akt, mTOR, and S6K1."