Počet záznamů: 1
The inositol phosphatase SHIP2 enables sustained ERK activation downstream of FGF receptors by recruiting Src kinases
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SYSNO ASEP 0494325 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název The inositol phosphatase SHIP2 enables sustained ERK activation downstream of FGF receptors by recruiting Src kinases Tvůrce(i) Fafílek, B. (CZ)
Bálek, L. (CZ)
Kunová Bosáková, M. (CZ)
Vařecha, M. (CZ)
Nita, A. (CZ)
Gregor, T. (CZ)
Gudernová, I. (CZ)
Křenová, J. (CZ)
Ghosh, S. (DE)
Piskáček, M. (CZ)
Jonatová, L. (CZ)
Cernohorsky, N. (CZ)
Zieba, J. T. (US)
Kostas, M. (PL)
Haugsten, E. M. (NO)
Wesche, J. (NO)
Erneux, C. (BE)
Trantírek, L. (CZ)
Krakow, D. (US)
Krejčí, Pavel (UZFG-Y) ORCIDČíslo článku eaap8608 Zdroj.dok. Science Signaling. - : American Association for the Advancement of Science - ISSN 1945-0877
Roč. 11, č. 548 (2018)Poč.str. 14 s. Forma vydání Tištěná - P Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova fibroblast growth factor ; Src kinases Vědní obor RIV EA - Morfologické obory a cytologie Obor OECD Biochemistry and molecular biology CEP GA17-09525S GA ČR - Grantová agentura ČR Institucionální podpora UZFG-Y - RVO:67985904 UT WOS 000444825300002 EID SCOPUS 85053548953 DOI 10.1126/scisignal.aap8608 Anotace Sustained activation of extracellular signal-regulated kinase (ERK) drives pathologies caused by mutations in fibroblast growth factor receptors (FGFRs). We previously identified the inositol phosphatase SHIP2 (also known as INPPL1) as an FGFR-interacting protein and a target of the tyrosine kinase activities of FGFR1, FGFR3, and FGFR4. We report that loss of SHIP2 converted FGF-mediated sustained ERK activation into a transient signal and rescued cell phenotypes triggered by pathologic FGFR-ERK signaling. Mutant forms of SHIP2 lacking phosphoinositide phosphatase activity still associated with FGFRs and did not prevent FGF-induced sustained ERK activation, demonstrating that the adaptor rather than the catalytic activity of SHIP2 was required. SHIP2 recruited Src family kinases to the FGFRs, which promoted FGFR-mediated phosphorylation and assembly of protein complexes that relayed signaling to ERK. SHIP2 interacted with FGFRs, was phosphorylated by active FGFRs, and promoted FGFR-ERK signaling at the level of phosphorylation of the adaptor FRS2 and recruitment of the tyrosine phosphatase PTPN11. Thus, SHIP2 is an essential component of canonical FGF-FGFR signal transduction and a potential therapeutic target in FGFR-related disorders. Pracoviště Ústav živočišné fyziologie a genetiky Kontakt Jana Zásmětová, knihovna@iapg.cas.cz, Tel.: 315 639 554 Rok sběru 2019
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