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Titolo:
Functional effects of APS and SH2-B on insulin receptor signalling
Autore:
Ahmed, Z; Pillay, TS;
Indirizzi:
Univ Nottingham, Sch Med, Queens Med Ctr, Inst Cell Signalling,Mol Endocrinol Grp, Nottingham NG7 2UH, England Univ Nottingham Nottingham England NG7 2UH , Nottingham NG7 2UH, England Univ Nottingham, Sch Med, Queens Med Ctr, Sch Biomed Sci, Nottingham NG7 2UH, England Univ Nottingham Nottingham England NG7 2UH , Nottingham NG7 2UH, England
Titolo Testata:
BIOCHEMICAL SOCIETY TRANSACTIONS
, volume: 29, anno: 2001,
parte:, 4
pagine: 529 - 534
SICI:
0300-5127(200108)29:<529:FEOAAS>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
C-CBL; ADAPTER PROTEIN; PROTOONCOGENE PRODUCT; 3T3-L1 ADIPOCYTES; GRB-IR; DOMAIN; KINASE; SUBSTRATE; BINDING; PH;
Keywords:
adapter protein; insulin; insulin receptor phosphorylation; SH2 domain;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Pillay, TS Univ Nottingham, Sch Med, Queens Med Ctr, Inst Cell Signalling,Mol Endocrinol Grp, Nottingham NG7 2UH, England Univ Nottingham Nottingham England NG7 2UH m NG7 2UH, England
Citazione:
Z. Ahmed e T.S. Pillay, "Functional effects of APS and SH2-B on insulin receptor signalling", BIOCH SOC T, 29, 2001, pp. 529-534

Abstract

APS [for 'adapter protein with a pleckstrin homology (PH) and Src homology2 (SH2) domain'] belongs to a family of adapter proteins involved in signalling by the receptors for insulin, insulin-like growth factor 1, platelet-derived growth factor and nerve growth factor. Other members include alternatively spliced SH2-B isoforms (SH2B alpha, SH2-B beta and SH2-B gamma) andLnk. These have a C-terminal SH2 domain, a central PH domain and an N-terminal proline-rich region. SH2B alpha, APS and Lnk have a conserved C-terminal tyrosine phosphorylation site, whereas the alternatively spliced SH2-B beta and SH2-B gamma have distinct C-termini. There is considerable sequencesimilarity between APS, SH2-B and Lnk, particularly in the SH2 domain. Both APS and SH2-B alpha interact with the insulin-receptor activation loop phosphorylation sites and undergo insulin-stimulated tyrosine phosphorylation, although the phosphorylation of SH2-B is considerably weaker. APS couplesc-Cb1 to the insulin receptor, resulting in ubiquitination of the insulin receptor. We established cell lines [Chinese hamster ovary (CHO). T-APS andCHO. T-SH2-B cells] overexpressing APS and SH2-B alpha to study their roles in insulin receptor signalling. Either adapter protein enhances insulin receptor and ERK (extracellular-signal-regulated kinase) phosphorylation. InCHO. T-APS cells, Akt phosphorylation is observed earlier than in CHO.T-SH2-B cells. Both enhance insulin-stimulated Akt activation but APS seems to cause greater activation. Thus APS and SH2-B have similar effects on insulin receptor signalling, although the effects of SH2-B are independent of itsphosphorylation.

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Documento generato il 02/04/20 alle ore 12:15:33