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IGF1R phosphorylates IRS1. 72 / 92
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"IGF1/IGF1R signal phosphorylates IRS1, activating PI3K and thereby also activating AKT."

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"IGF1R phosphorylates IRS1 (Insulin receptor substrate-1) and recruits its downstream effectors ( xref )."

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"Hyperinsulinemia and elevated IGFR activates the phosphorylation of IRS-1, resulting in the activation of multiple cytokine pathways, including PI3K/AKT/mTOR and MAPK cascade, which modulate cell cycle and may potentially enhance tumor progression of HCC (35).3.2 Wnt/beta-catenin pathway."

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"IGF-1R activation leads to IRS-1 phosphorylation, which initiates recruitment of downstream effectors."

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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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"Otherwise, IGF-1R is activated through phosphorylation, and subsequently phosphorylates insulin receptor substrate 1 (IRS-1)."

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"Another study showed that concurrent blockade of IGF1R and its EGFR/Her-2 simultaneously inhibited the pancreatic tumor growth and the stimulation of IRS-1, Akt, and MAPK phosphorylation."

sparser
"Both IGF-I and IGF-II bind the tyrosine kinase receptor IGF1R, which in turn phosphorylates the insulin receptor substrates IRS-1 and IRS-2."

sparser
"Therefore, our studies define a unique signaling mechanism by which the IGF-I receptor phosphorylates IRS-1, allowing it to function as a molecular scaffold for assembly of a complex that is necessary to enable IGF-I to stimulate vimentin binding to RPTPβ ( xref )."

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"Rosiglitazone enhanced the phosphorylation of insulin receptor substrate 1 (IRS1, phosphorylated at Ser 636/639), which is considered to be the main activator of the Akt and mTOR pathway by IGF-1R."

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"The activated IGF-1R recruits and phosphorylates the intracellular substrate IRS-1, and the phosphorylated IRS-1 is in turn recognized by SH2 domain–containing proteins, such as the p85 regulatory subunit of PI3K, and triggers activation of downstream signaling pathways."

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"Upon binding the IGF ligand, IGF1R is activated through autophosphorylation and subsequently phosphorylates insulin receptor substrate 1 (IRS1)."

trips
"In the absence of IGF-I stimulation, or if mutated IGF-IR fails to phosphorylate IRS-1, localization of Rad51 to the sites of damaged DNA is diminished."

sparser
"Activation of PI3K thus requires both PKA-mediated relief of IRS1 inhibition and IGF-1R-dependent tyrosine phosphorylation of IRS1."

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"The phosphorylation of the IGF-I receptor beta subunit is coincidental with the tyrosine phosphorylation of its adapter IRS-1, suggesting that the IGF-I receptor phosphorylates IRS-1 in response to An[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Upon engagement with IGFs, IGF1R phosphorylates IRS1, which then activates the PI3K/AKT/mTOR pathway to promote cartilage matrix synthesis [ xref , xref ]."

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"Since activated IGF-1R phosphorylates IRS-1, we first examined whether TRAF4 affects IGF-1-induced IGF-1R activation in control or TRAF4-overexpressing MCF-7 cells."

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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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"Indeed, the effect of IGF1 is time-limited by the phosphorylation of IRS1 by IGF1R and its subsequent ubiquitination and proteasome-mediated degradation."

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"Following IRS1 activation, IGF1R phosphorylates IRS1 leading to its ubiquitination by FBXO40 and its degradation by the 26S proteasome, in cultured myotube and in mice [ xref , xref ]."

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"It is widely known that the PI3K/Akt pathway is downstream of IRS-1, and IRS-1 could be phosphorylated by IGF-1R [ 22 ]."

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"Both IGF-I and IGF-II bind the tyrosine kinase receptor IGF1R, which in turn phosphorylates the insulin receptor substrates IRS-1 and IRS-2."

sparser
"Purified insulin receptor and IGF-I receptor phosphorylated recombinant baculovirus-produced IRS-1 on similar sites in vitro, and phosphorylated baculovirus-produced IRS-1 bound PtdIns 3'-kinase activity from lysates of quiescent cells."

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"1 Upon binding the IGF ligand, IGF-1R is activated through autophosporylation, and subsequently phosphorylates insulin receptor substrate 1 (IRS-1)."

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"The homologous insulin- like growth factor 1 receptor also phosphorylates IRS-1 in a similar manner [71."

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"This would also suggest that, although IGF-1R-dependent IRS-1 phosphorylation is reduced in OA Obs, Syp phosphorylation and activity could compensate for this reduction."

sparser
"As for IGF1 induced phosphorylation of IRS1, the E3 ligase that modulates IRS1 levels after IGF1R phosphorylation of IRS1 is the Fbxo40–SCF complex (Shi et al ., xref ) ( xref )."

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"To analyze the mechanism by which stimulation of IGF-IR led to PKCzeta mediated vimentin phosphorylation, we determined if vimentin and PKCzeta were co-recruited to the scaffolding protein IRS-1, which is directly phosphorylated by IGF-IR."

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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."

sparser
"It is widely known that the PI3K/Akt pathway is downstream of IRS-1, and IRS-1 could be phosphorylated by IGF-1R [ 22 ]."

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"PIK3CA small interfering RNA (siRNA) silencing of p110α neither affected the increased phosphorylation of RTKs and IRS-1 nor total HER3 and IGF-1R levels (SI Appendix, Fig. S5), indicating that RTK activation by these driver mutations is p110α-independent.We established a CRISPR/Cas9-mediated W333R knock-in in the human colon cancer cell line HCT116, because PIK3R1 mutations frequently manifest in colon cancer patients."

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"Therefore, our studies define a unique signaling mechanism by which the IGF-I receptor phosphorylates IRS-1, allowing it to function as a molecular scaffold for assembly of a complex that is necessary to enable IGF-I to stimulate vimentin binding to RPTPbeta (XREF_FIG)."

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"We conclude that the human IL-4R has distinct domains that have predominant roles in growth stimulation and in gene induction; possession of the I4R motif alone, although allowing 4PS/IRS -1 phosphory[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"One pathway involves IRS-1, which becomes tyrosine phosphorylated by IGF-IR and binds the Grb2/Sos complex through the SH2 domain of Grb2."

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"Similarly, IGF-1R activation results in phosphorylation of the receptor substrate IRS-1 and activation of AKT at the cilium (Zhu et al., 2009)."

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"TNF-alpha also reduces phosphorylation of IRS-1 and IRS-2 by IGF1R, thus inhibiting signaling of IGF-1 in muscle cell development [XREF_BIBR]."

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"In prostate cancer cells, co-inhibition of epidermal growth factor receptor and IGF-1R reduced phosphorylation of IRS-1 and its interaction with RAD51, suppressing HR and increasing radio-sensitivity [XREF_BIBR]."

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"IGF1R phosphorylates IRS1 (Insulin receptor substrate-1) and recruits its downstream effectors."

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"Indeed, IGF-IR internalization was required for Shc activation but not for IRS-1 phosphorylation, which was mediated by both cell surface and endosomal IGF-IR."

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"IGF-1 signaling begins when IGF-1 binds with its cell surface receptor, IGF-1R, forming a homodimer signaling complex, phosphorylating IGF-1R, which then phosphorylates intracellular insulin receptor substrate 1 (IRS-1) for its downstream targets."

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"The signaling cascade begins by the binding of ligand IGF (token number of 5) with the receptor (IGF-1R) which leads to the phosphorylation of IRS-1."

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"Another study from the same group [XREF_BIBR] established that phosphorylation of AKT on Thr308 and Ser473 increases following treatment of ALL cells with AICAR and demonstrated that AKT phosphorylation on Thr 308 is mediated by AMPK induced IGF-1R activation and phosphorylation of IRS-1."

sparser
"Generally, IGF1R is activated via autophosphorylation and subsequently phosphorylates IRS1 after IGF ligand binds to it."

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"Generally, IGF1R is activated via autophosphorylation and subsequently phosphorylates IRS1 after IGF ligand binds to it."

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"It markedly inhibited IRS1 and Shc phosphorylation and downregulated mitRaf.In addition, IGF-1R inhibition led to a decrease of cell survival and induced apoptosis in a manner depending on the approach used for the receptor inhibition, with IGF-1R-siRNA being the most effective apoptosis inducer.These findings suggest that blocking of several IGF1R signaling pathways may be necessary to effectively induce apotosis in lung cancer cells."

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"Activated IGF-IR recruits and phosphorylates insulin receptor substrate proteins, IRS-1 and IRS-2 which in turn serve as multisite docking proteins by binding to numerous SH2 domain-containing protein[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"In the absence of IGF-I stimulation, or if mutated IGF-IR fails to phosphorylate IRS-1, localization of Rad51 to the sites of damaged DNA is diminished."

sparser
"IGF-IR ligand binding causes phosphorylation of insulin receptor substrate-1 and -2 (IRS1, IRS2), which promote growth by transmitting signals to MAPK/ERK, PI3K/AKT and JAK/STAT in cell type specific manners [ xref , xref ]."

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"In particular they act as competitive inhibitors of IGF-IR, promote inhibitory phosphorylation and degradation of IRS1 and IRS2 leading to the elimination of IRS1/2 and finally to cell death 27."

sparser
"Upon binding the IGF ligand, IGF1R is activated through autophosphorylation and subsequently phosphorylates insulin receptor substrate 1 (IRS1)."

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"A previous study showed that the simultaneous blockade of IGF1R and EGFR/HER2 synergistically inhibited pancreatic tumor growth and eliminated the activation of IRS-1, Akt, and MAPK phosphorylation."

sparser
"In cells only stimulated by IGF-I ( Fig. 8 A), the IGF-IR induces the tyrosine phosphorylation of IRS-1 which recruits docking proteins such as PI 3-kinase and initiates specific IGF-I downstream sign[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"The phosphorylation of the IGF-I receptor β subunit is coincidental with the tyrosine phosphorylation of its adapter IRS-1, suggesting that the IGF-I receptor phosphorylates IRS-1 in response to AngII[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Wheat germ agglutinin-purified mutant receptors were as active in phosphorylating poly-(Glu,Tyr) 4:1 as wild-type IGF-I receptors, suggesting that, in intact cells, additional factors are necessary in order for the IGF-I receptor to phosphorylate IRS-1."

sparser
"Phosphorylation of IRS1 by IGF1R further stimulated ubiquitin conjugation, consistent with the observation that IRS1 must be phosphorylated by IGF1R first, and only then is targeted for degradation by[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Upon engagement with IGFs, IGF1R phosphorylates IRS1, which then activates the PI3K/AKT/mTOR pathway to promote cartilage matrix synthesis [XREF_BIBR, XREF_BIBR]."

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"Activated igf1r phosphorylates specific reaction components, including IRS-1, IRS-2, and SRC homology collagen, and it regulates downstream responses through the phosphatidylinositol 3-kinase (PI3K)/AKT and mitogen-activated protein kinase (MAPK) pathways [1,37]."

sparser
"After the ligand binds to the receptor, IGF-1R will be activated via autophosphorylation and will phosphorylate the insulin receptor substrate 1 (IRS-1)."

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"IGF-1R phosphorylates insulin receptor substrate 1 (IRS-1), which also contains pYXXM motifs that bind the SH2 domains of p85 [ xref ]."

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"Phosphorylation of IRS1 by IGF1R further stimulated ubiquitin conjugation, consistent with the observation that IRS1 must be phosphorylated by IGF1R first, and only then is targeted for degradation by[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Compared to the immunoprecipitated IGF-IR from siCtrl cells, the immunoprecipitated IGF-IR from siGRP78 cells exhibited lower levels of tyrosine phosphorylation and induced lower levels of IRS1 phosph[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"As for IGF1 induced phosphorylation of IRS1, the E3 ligase that modulates IRS1 levels after IGF1R phosphorylation of IRS1 is the Fbxo40 and SCF complex (XREF_FIG)."

sparser
"Activated PP1 is sufficient to dephosphorylate at least four IRS1 Ser residues, Ser 318 , Ser 346 , Ser 612 , and Ser 789 , and promotes IRS1 YXXM phosphorylation by the IGF1R to activate the PI3K/AKT cascade."

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"TNF-α also reduces phosphorylation of IRS-1 and IRS-2 by IGF1R, thus inhibiting signaling of IGF-1 in muscle cell development [ xref ]."

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

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"InsR or IGF1R binds to IRS-1 via the phosphotyrosine-binding domain and phosphorylates multiple sites on tyrosine in IRS-1, leading to the association with several signaling molecules such as PI3K, GRB2 and SHP2 [ xref , xref ]."

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"While stimulation of IGF-1R by IGFs triggers autophosphorylation and subsequent phosphorylation of either insulin receptor substrate-1 (IRS-1) or insulin receptor substrate-2 (IRS-2), it is clear that these adapter proteins are activated by both IR 15 and IGF-1R."

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"Upon ligation, IGF1R recruits and phosphorylates IRS1."

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"Insulin receptor substrate 1 (IRS-1), which is known to be phosphorylated by autoactivated IGF-1R upon ligand binding, was shown to be involved in IGF-1R-mediated 4-OH-TAM resistance."

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"IGF-1R phosphorylates insulin receptor substrate 1 (IRS-1), which also contains pYXXM motifs that bind the SH2 domains of p85 [XREF_BIBR]."

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"61 Insulin receptor substrate-1 (IRS-1) levels, which is phosphorylated by IGF-IR activation, was found to predict worse disease-free survival in small (< 2 cm) OR negative tumours."

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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 ], but also protects from apoptosis as a result of activation of PI3K-Akt through phosphorylation and subsequent inactivation of BAD[ xref ]."