Functional analysis of the posttranslational modifications of the death receptor 6

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F09%3A00333980" target="_blank" >RIV/68378050:_____/09:00333980 - 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

Functional analysis of the posttranslational modifications of the death receptor 6

Popis výsledku v původním jazyce

Death receptor 6 (DR6/TNFRSF21) is a death domain-containing receptor of the TNFR superfamily with an apparent regulatory function in hematopoietic and neuronal cells. In this study we document that DR6 is an extensively posttranslationally modified transmembrane protein and that N- and O-glycosylations of amino acids in its extracellular part are mainly responsible for its approximately 40 kDa mobility shift. All 6 extracellular Asn are N-glycosylated and that the Ser/Thr/Pro cluster in the "stalk" domain is a major site for O-glycosylation. Deletion of the linker region between CRDs and TM leads to intracellular retention of DR6. Biosynthetic labeling revealed that the membrane-proximal Cys368 in the intracellular part of DR6 is S-palmitoylated. Palmitoylation of Cys368 is apparently not, in contrast to the N-glycosylation of the extracellular part, required for DR6 targeting into Brij-98 insoluble lipid rafts.

Název v anglickém jazyce

Functional analysis of the posttranslational modifications of the death receptor 6

Popis výsledku anglicky

Death receptor 6 (DR6/TNFRSF21) is a death domain-containing receptor of the TNFR superfamily with an apparent regulatory function in hematopoietic and neuronal cells. In this study we document that DR6 is an extensively posttranslationally modified transmembrane protein and that N- and O-glycosylations of amino acids in its extracellular part are mainly responsible for its approximately 40 kDa mobility shift. All 6 extracellular Asn are N-glycosylated and that the Ser/Thr/Pro cluster in the "stalk" domain is a major site for O-glycosylation. Deletion of the linker region between CRDs and TM leads to intracellular retention of DR6. Biosynthetic labeling revealed that the membrane-proximal Cys368 in the intracellular part of DR6 is S-palmitoylated. Palmitoylation of Cys368 is apparently not, in contrast to the N-glycosylation of the extracellular part, required for DR6 targeting into Brij-98 insoluble lipid rafts.

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

2009

Kód důvěrnosti údajů

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

Název periodika

Biochimica Et Biophysica Acta-Molecular Cell Research

ISSN

0167-4889

e-ISSN

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Svazek periodika

1793

Číslo periodika v rámci svazku

10

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

9

Strana od-do

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Kód UT WoS článku

000270481600004

EID výsledku v databázi Scopus

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