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Statements

Subject Item
n2:RIV%2F68378050%3A_____%2F08%3A00315276%21RIV09-AV0-68378050
rdf:type
skos:Concept n12:Vysledek
dcterms:description
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 on cytoplasmic 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 the cell 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. TRAIL, ligand z TNFa rodiny, indukuje svou vazbou na receptory smrti TRAIL-R1/DR4 a TRAIL-R2/DR5 apoptózu nádorových buněk. TRAILem indukovaná apoptóza je regulována na mnoha úrovních, jedna z nich je přítomnost a relativní množství TRAIL pro a anti-apoptotických receptorů na cytoplazmatické membráně. Kvasinkovým dvou-hybridním vyhledáváním proteinů interagujících s intracelulární část (ICP) DR4 jsme objevili ARAP1, adaptérový protein s ArfGAP a RhoGAP doménami. V kvasinkách interaguje DR4 (ICP) s alternativně sestřiženým ARAP1, kterému chybí 11 aminokyselin z PH5 domény. Transfekovaný ARAP1 koprecipituje s DR4 a kolokalizuje s ním v membránách ER /Golgi, cytoplazmy a také v raných endosomech. Potlačení exprese ARAP1 významně snižuje lokalizaci DR4 na povrchu některých nádorových buněk a zpomaluje TRAILem indukovanou apoptózu. Naše data ukazují, že ARAP1 se pravděpodobně podílí na regulaci buněčně-specifického transportu DR4 a může tak ovlivnit účinnost TRAILem indukované apoptózy. 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 on cytoplasmic 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 the cell 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.
dcterms:title
Arf and Rho GAP adapter protein ARAP1 participates in the mobilization of TRAIL-R1/DR4 to the plasma membrane Adaptérový protein ARAP1 s ARF a Rho GAP doménami se podílí na mobilizaci TRAIL-R1/DR4 na plasmatickou membránu Arf and Rho GAP adapter protein ARAP1 participates in the mobilization of TRAIL-R1/DR4 to the plasma membrane
skos:prefLabel
Adaptérový protein ARAP1 s ARF a Rho GAP doménami se podílí na mobilizaci TRAIL-R1/DR4 na plasmatickou membránu Arf and Rho GAP adapter protein ARAP1 participates in the mobilization of TRAIL-R1/DR4 to the plasma membrane Arf and Rho GAP adapter protein ARAP1 participates in the mobilization of TRAIL-R1/DR4 to the plasma membrane
skos:notation
RIV/68378050:_____/08:00315276!RIV09-AV0-68378050
n3:aktivita
n10:Z n10:P
n3:aktivity
P(1M0506), Z(AV0Z50520514)
n3:cisloPeriodika
3
n3:dodaniDat
n15:2009
n3:domaciTvurceVysledku
n4:6099017 n4:9065695 n4:4290798 n4:8623171 n4:9022643
n3:druhVysledku
n13:J
n3:duvernostUdaju
n9:S
n3:entitaPredkladatele
n18:predkladatel
n3:idSjednocenehoVysledku
357003
n3:idVysledku
RIV/68378050:_____/08:00315276
n3:jazykVysledku
n17:eng
n3:klicovaSlova
apoptosis; TRAIL; receptor trafficking
n3:klicoveSlovo
n5:receptor%20trafficking n5:apoptosis n5:TRAIL
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[F33CAB2D211B]
n3:nazevZdroje
Apoptosis
n3:obor
n11:EB
n3:pocetDomacichTvurcuVysledku
5
n3:pocetTvurcuVysledku
5
n3:projekt
n14:1M0506
n3:rokUplatneniVysledku
n15:2008
n3:svazekPeriodika
13
n3:tvurceVysledku
Šímová, Šárka Klíma, Martin Šourková, Vladimíra Anděra, Ladislav Čermák, Lukáš
n3:wos
000253574000010
n3:zamer
n16:AV0Z50520514
s:issn
1360-8185
s:numberOfPages
14