A novel interaction between fibroblast growth factor receptor 3 and the p85 subunit of phosphoinositide 3-kinase: activation-dependent regulation of ERK by p85 in multiple myeloma cells

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F08%3A00039939" target="_blank" >RIV/00216224:14310/08:00039939 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

A novel interaction between fibroblast growth factor receptor 3 and the p85 subunit of phosphoinositide 3-kinase: activation-dependent regulation of ERK by p85 in multiple myeloma cells

Popis výsledku v původním jazyce

Ectopic activation of fibroblast growth factor receptor 3 (FGFR3) is associated with several cancers, including multiple myeloma (MM). FGFR3 inhibition in these cells inhibits proliferation and induces apoptosis, validating FGFR3 signaling as a therapeutic target in t(4;14) MM cases. We have identified the PI3K regulatory subunit, p85 alpha, as a novel interactor of FGFR3 by yeast two-hybrid, and confirmed an interaction with both p85 alpha and p85 beta in mammalian cells. The interaction of FGFR3 withp85 is dependent upon receptor activation. In contrast to the Gab1-mediated association of FGFRs with p85, the FGFR3-p85 interaction we observed requires FGFR3 Y760, previously identified as a PLC gamma binding site. The interaction of p85 with FGFR3 does not require PLC gamma, suggesting the p85 interaction is direct and independent of PLC gamma binding. FGFR3 and p85 proteins also interact in MM cell lines which consistently express p85 alpha and p85 beta, but not p50 or p55 subunits.

Název v anglickém jazyce

A novel interaction between fibroblast growth factor receptor 3 and the p85 subunit of phosphoinositide 3-kinase: activation-dependent regulation of ERK by p85 in multiple myeloma cells

Popis výsledku anglicky

Ectopic activation of fibroblast growth factor receptor 3 (FGFR3) is associated with several cancers, including multiple myeloma (MM). FGFR3 inhibition in these cells inhibits proliferation and induces apoptosis, validating FGFR3 signaling as a therapeutic target in t(4;14) MM cases. We have identified the PI3K regulatory subunit, p85 alpha, as a novel interactor of FGFR3 by yeast two-hybrid, and confirmed an interaction with both p85 alpha and p85 beta in mammalian cells. The interaction of FGFR3 withp85 is dependent upon receptor activation. In contrast to the Gab1-mediated association of FGFRs with p85, the FGFR3-p85 interaction we observed requires FGFR3 Y760, previously identified as a PLC gamma binding site. The interaction of p85 with FGFR3 does not require PLC gamma, suggesting the p85 interaction is direct and independent of PLC gamma binding. FGFR3 and p85 proteins also interact in MM cell lines which consistently express p85 alpha and p85 beta, but not p50 or p55 subunits.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2008

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

HUMAN MOLECULAR GENETICS

ISSN

0964-6906

e-ISSN

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Svazek periodika

18

Číslo periodika v rámci svazku

11

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

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Kód UT WoS článku

000265951600005

EID výsledku v databázi Scopus

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