Csk-vážící protein PAG reguluje Src-indukovanou mitogenní signalizaci PDGF via GM1

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F08%3A00315261" target="_blank" >RIV/68378050:_____/08:00315261 - 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

The Csk-binding protein PAG regulates PDGF-induced Src mitogenic signaling via GM1

Popis výsledku v původním jazyce

Cholesterol-enriched membrane domains, such as caveolae, regulate association of SRC family protein tyrosine kinases (SFK) with the platelet-derived growth factor receptor (PDGFR), which is needed for mitogenic signaling. PAG, a ubiquitously expressed member of the transmembrane adaptor protein family, is known to negatively regulate SFK signaling though binding to Csk. PAG was found to modulate PDGFR levels in caveolae and SFK mitogenic signaling through a Csk-independent mechanism. Regulation of SFK mitogenic activity by PAG requires the first N-terminal 97 aa (PAG-N), which include the extracellular and transmembrane domains, palmitoylation sites, and a short cytoplasmic sequence. PAG-N increases ganglioside GM1 levels at the cell surface and, thus,displaces PDGFR from caveolae, a process that requires the ganglioside-specific sialidase Neu-3. PAG regulates PDGFR membrane partitioning and SFK mitogenic signaling by modulating GM1 levels within caveolae independently from Csk.

Název v anglickém jazyce

The Csk-binding protein PAG regulates PDGF-induced Src mitogenic signaling via GM1

Popis výsledku anglicky

Cholesterol-enriched membrane domains, such as caveolae, regulate association of SRC family protein tyrosine kinases (SFK) with the platelet-derived growth factor receptor (PDGFR), which is needed for mitogenic signaling. PAG, a ubiquitously expressed member of the transmembrane adaptor protein family, is known to negatively regulate SFK signaling though binding to Csk. PAG was found to modulate PDGFR levels in caveolae and SFK mitogenic signaling through a Csk-independent mechanism. Regulation of SFK mitogenic activity by PAG requires the first N-terminal 97 aa (PAG-N), which include the extracellular and transmembrane domains, palmitoylation sites, and a short cytoplasmic sequence. PAG-N increases ganglioside GM1 levels at the cell surface and, thus,displaces PDGFR from caveolae, a process that requires the ganglioside-specific sialidase Neu-3. PAG regulates PDGFR membrane partitioning and SFK mitogenic signaling by modulating GM1 levels within caveolae independently from Csk.

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

<a href="/cs/project/1M0506" target="_blank" >1M0506: Centrum molekulární a buněčné imunologie</a><br>

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

Journal of Cell Biology

ISSN

0021-9525

e-ISSN

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Svazek periodika

182

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

12

Strana od-do

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Kód UT WoS článku

000258529100018

EID výsledku v databázi Scopus

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