Matches in SemOpenAlex for { <https://semopenalex.org/work/W4238227436> ?p ?o ?g. }
Showing items 1 to 77 of
77
with 100 items per page.
- W4238227436 endingPage "5297" @default.
- W4238227436 startingPage "5291" @default.
- W4238227436 abstract "The insulin receptor substrate-1 (IRS-1) is rapidly phosphorylated on several tyrosine residues by the activated insulin receptor. Phosphorylated IRS-1 acts as a docking protein for Src homology-2 (SH2) domain-containing proteins involved in insulin signaling. These include in vivo the regulatory subunit p85 of the phosphatidylinositol 3-kinase (PI3-K) and the phosphotyrosine phosphatase-2C (PTP2C). In this report, we examined which tyrosine residues of IRS-1 are required for the interactions of IRS-1 with PI3-K and PTP2C. To address this issue, we constructed different rat IRS-1 mutants containing mutations in the tyrosine residues that interact with the SH2 domains of PI3-K and PTP2C in vitro. Each of the IRS-1 mutants obtained have been transiently expressed in 293 EBNA cells to study their ability to interact with PI3-K and PTP2C in vivo. Our results demonstrate that mutation of tyrosine 608 affects the PI3-K activity associated with IRS-1, suggesting that this tyrosine is likely to be a principal site of interaction with the SH2 domains of p85 in response to insulin. Furthermore, we found that mutation of tyrosines 1172 and 1222 totally prevents the insulin-induced association of IRS-1 with the SH2 domains of PTP2C, demonstrating that both tyrosines 1172 and 1222 are key elements in the binding sites for the SH2 domains of PTP2C. Finally, we found that the ability of purified PTP2C to dephosphorylate IRS-1 is dependent on the association of PTP2C with phosphorylated IRS-1." @default.
- W4238227436 created "2022-05-12" @default.
- W4238227436 creator A5055769358 @default.
- W4238227436 date "1995-12-01" @default.
- W4238227436 modified "2023-10-16" @default.
- W4238227436 title "Identification by mutation of the tyrosine residues in the insulin receptor substrate-1 affecting association with the tyrosine phosphatase 2C and phosphatidylinositol 3-kinase" @default.
- W4238227436 doi "https://doi.org/10.1210/en.136.12.5291" @default.
- W4238227436 hasPublicationYear "1995" @default.
- W4238227436 type Work @default.
- W4238227436 citedByCount "0" @default.
- W4238227436 countsByYear W42382274362013 @default.
- W4238227436 crossrefType "journal-article" @default.
- W4238227436 hasAuthorship W4238227436A5055769358 @default.
- W4238227436 hasConcept C101544691 @default.
- W4238227436 hasConcept C104317684 @default.
- W4238227436 hasConcept C108636557 @default.
- W4238227436 hasConcept C112446052 @default.
- W4238227436 hasConcept C11960822 @default.
- W4238227436 hasConcept C134018914 @default.
- W4238227436 hasConcept C143065580 @default.
- W4238227436 hasConcept C178666793 @default.
- W4238227436 hasConcept C185967709 @default.
- W4238227436 hasConcept C197153747 @default.
- W4238227436 hasConcept C201624660 @default.
- W4238227436 hasConcept C2776165026 @default.
- W4238227436 hasConcept C2777391703 @default.
- W4238227436 hasConcept C2777553839 @default.
- W4238227436 hasConcept C2779306644 @default.
- W4238227436 hasConcept C2780610907 @default.
- W4238227436 hasConcept C42362537 @default.
- W4238227436 hasConcept C55493867 @default.
- W4238227436 hasConcept C62478195 @default.
- W4238227436 hasConcept C85528070 @default.
- W4238227436 hasConcept C86333721 @default.
- W4238227436 hasConcept C86803240 @default.
- W4238227436 hasConceptScore W4238227436C101544691 @default.
- W4238227436 hasConceptScore W4238227436C104317684 @default.
- W4238227436 hasConceptScore W4238227436C108636557 @default.
- W4238227436 hasConceptScore W4238227436C112446052 @default.
- W4238227436 hasConceptScore W4238227436C11960822 @default.
- W4238227436 hasConceptScore W4238227436C134018914 @default.
- W4238227436 hasConceptScore W4238227436C143065580 @default.
- W4238227436 hasConceptScore W4238227436C178666793 @default.
- W4238227436 hasConceptScore W4238227436C185967709 @default.
- W4238227436 hasConceptScore W4238227436C197153747 @default.
- W4238227436 hasConceptScore W4238227436C201624660 @default.
- W4238227436 hasConceptScore W4238227436C2776165026 @default.
- W4238227436 hasConceptScore W4238227436C2777391703 @default.
- W4238227436 hasConceptScore W4238227436C2777553839 @default.
- W4238227436 hasConceptScore W4238227436C2779306644 @default.
- W4238227436 hasConceptScore W4238227436C2780610907 @default.
- W4238227436 hasConceptScore W4238227436C42362537 @default.
- W4238227436 hasConceptScore W4238227436C55493867 @default.
- W4238227436 hasConceptScore W4238227436C62478195 @default.
- W4238227436 hasConceptScore W4238227436C85528070 @default.
- W4238227436 hasConceptScore W4238227436C86333721 @default.
- W4238227436 hasConceptScore W4238227436C86803240 @default.
- W4238227436 hasIssue "12" @default.
- W4238227436 hasLocation W42382274361 @default.
- W4238227436 hasOpenAccess W4238227436 @default.
- W4238227436 hasPrimaryLocation W42382274361 @default.
- W4238227436 hasRelatedWork W1909946134 @default.
- W4238227436 hasRelatedWork W2006709223 @default.
- W4238227436 hasRelatedWork W2015820956 @default.
- W4238227436 hasRelatedWork W2027995286 @default.
- W4238227436 hasRelatedWork W2061941570 @default.
- W4238227436 hasRelatedWork W2096032969 @default.
- W4238227436 hasRelatedWork W2171277650 @default.
- W4238227436 hasRelatedWork W4244757397 @default.
- W4238227436 hasRelatedWork W4247927249 @default.
- W4238227436 hasRelatedWork W4252597221 @default.
- W4238227436 hasVolume "136" @default.
- W4238227436 isParatext "false" @default.
- W4238227436 isRetracted "false" @default.
- W4238227436 workType "article" @default.