Adaptérový protein ARAP1 s ARF a Rho GAP doménami se podílí na mobilizaci TRAIL-R1/DR4 na plasmatickou membránu

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F08%3A00315276" target="_blank" >RIV/68378050:_____/08:00315276 - isvavai.cz</a>

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

Arf and Rho GAP adapter protein ARAP1 participates in the mobilization of TRAIL-R1/DR4 to the plasma membrane

Popis výsledku v původním jazyce

TRAIL, a TNFa family ligand, induces apoptosis of cancer cells upon binding to receptors TRAIL-R1/DR4 and TRAIL-R2/DR5. This apoptosis is regulated at multiple levels; one is the presence and relative number of TRAIL pro- and anti-apoptotic receptors oncytoplasmic membrane. In a yeast two-hybrid search for proteins interacting with the intracellular part (ICP) of DR4 we picked ARAP1, an adapter protein with ArfGAP and RhoGAP activities. In yeast DR4(ICP) interacts with alternatively spliced ARAP1 lacking 11 aa from PH5 domain. Transfected ARAP1 co-precipitates with DR4 and co-localizes with it in the ER/Golgi, at the cytoplasmic membrane and in early endosomes of TRAIL-treated cells. ARAP1 knockdown significantly compromises localization of DR4 at thecell surface of several tumor cell lines and slows down their TRAIL-induced death. ARAP1 is thus likely involved in the regulation of cell-specific trafficking of DR4 and might affect the efficacy of TRAIL-induced apoptosis.

Název v anglickém jazyce

Arf and Rho GAP adapter protein ARAP1 participates in the mobilization of TRAIL-R1/DR4 to the plasma membrane

Popis výsledku anglicky

TRAIL, a TNFa family ligand, induces apoptosis of cancer cells upon binding to receptors TRAIL-R1/DR4 and TRAIL-R2/DR5. This apoptosis is regulated at multiple levels; one is the presence and relative number of TRAIL pro- and anti-apoptotic receptors oncytoplasmic membrane. In a yeast two-hybrid search for proteins interacting with the intracellular part (ICP) of DR4 we picked ARAP1, an adapter protein with ArfGAP and RhoGAP activities. In yeast DR4(ICP) interacts with alternatively spliced ARAP1 lacking 11 aa from PH5 domain. Transfected ARAP1 co-precipitates with DR4 and co-localizes with it in the ER/Golgi, at the cytoplasmic membrane and in early endosomes of TRAIL-treated cells. ARAP1 knockdown significantly compromises localization of DR4 at thecell surface of several tumor cell lines and slows down their TRAIL-induced death. ARAP1 is thus likely involved in the regulation of cell-specific trafficking of DR4 and might affect the efficacy of TRAIL-induced apoptosis.

Druh

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

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

—

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

Apoptosis

ISSN

1360-8185

e-ISSN

—

Svazek periodika

13

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

14

Strana od-do

—

Kód UT WoS článku

000253574000010

EID výsledku v databázi Scopus

—