A specific type of membrane microdomains is involved in the maintenance and translocation of kinase active Lck to lipid rafts

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F12%3A00377765" target="_blank" >RIV/68378050:_____/12:00377765 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.imlet.2012.01.001" target="_blank" >http://dx.doi.org/10.1016/j.imlet.2012.01.001</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.imlet.2012.01.001" target="_blank" >10.1016/j.imlet.2012.01.001</a>

Jazyk výsledku

angličtina

Název v původním jazyce

A specific type of membrane microdomains is involved in the maintenance and translocation of kinase active Lck to lipid rafts

Popis výsledku v původním jazyce

Lck is the principal signal-generating tyrosine kinase of the T cell activation mechanism. We have previously demonstrated that induced Lck activation outside of lipid rafts (LR) results in the rapid translocation of a fraction of Lck to LR. While this translocation predicates the subsequent production of IL-2, the mechanism underpinning this process is unknown. Here, we describe the main attributes of this translocating pool of Lck. Using fractionation of Brij58 lysates, derived from primary naive non-activated CD4(+) T cells, we show that a significant portion of Lck is associated with high molecular weight complexes representing a special type of detergent-resistant membranes (DRMs) of relatively high density and sensitivity to laurylmaltoside, thuscalled heavy DRMs. TcR/CD4 coaggregation-mediated activation resulted in the redistribution of more than 50% of heavy DRM-associated Lck to LR in a microtubular network-dependent fashion. Remarkably, in non-activated CD4(+) T-cells, only

Název v anglickém jazyce

A specific type of membrane microdomains is involved in the maintenance and translocation of kinase active Lck to lipid rafts

Popis výsledku anglicky

Lck is the principal signal-generating tyrosine kinase of the T cell activation mechanism. We have previously demonstrated that induced Lck activation outside of lipid rafts (LR) results in the rapid translocation of a fraction of Lck to LR. While this translocation predicates the subsequent production of IL-2, the mechanism underpinning this process is unknown. Here, we describe the main attributes of this translocating pool of Lck. Using fractionation of Brij58 lysates, derived from primary naive non-activated CD4(+) T cells, we show that a significant portion of Lck is associated with high molecular weight complexes representing a special type of detergent-resistant membranes (DRMs) of relatively high density and sensitivity to laurylmaltoside, thuscalled heavy DRMs. TcR/CD4 coaggregation-mediated activation resulted in the redistribution of more than 50% of heavy DRM-associated Lck to LR in a microtubular network-dependent fashion. Remarkably, in non-activated CD4(+) T-cells, only

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/GA310%2F09%2F2084" target="_blank" >GA310/09/2084: Charakterizace molekulárního mechanismu regulujícího kompartmentalizaci signálních molekul do lipidových raftů</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Immunology Letters

ISSN

0165-2478

e-ISSN

—

Svazek periodika

142

Číslo periodika v rámci svazku

1-2

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

11

Strana od-do

64-74

Kód UT WoS článku

000301683800009

EID výsledku v databázi Scopus

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