About: Functional analysis of the posttranslational modifications of the death receptor 6

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Functional analysis of the posttranslational modifications of the death receptor 6 Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	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 %22stalk%22 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. 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 %22stalk%22 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. (en)
Title	Functional analysis of the posttranslational modifications of the death receptor 6 Functional analysis of the posttranslational modifications of the death receptor 6 (en)
skos:prefLabel	Functional analysis of the posttranslational modifications of the death receptor 6 Functional analysis of the posttranslational modifications of the death receptor 6 (en)
skos:notation	RIV/68378050:_____/09:00333980!RIV10-MSM-68378050
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(1M0506), Z(AV0Z50520514)
http://linked.open...iv/cisloPeriodika	10
http://linked.open...vai/riv/dodaniDat	2010
http://linked.open...aciTvurceVysledku	Zájedová, Jitka Anděra, Ladislav Doubravská, Lenka Klíma, Martin
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Ústav molekulární genetiky AV ČR, v. v. i.
http://linked.open...dnocenehoVysledku	315705
http://linked.open...ai/riv/idVysledku	RIV/68378050:_____/09:00333980
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	N- and O-glycosylations; Death receptor 6; lipid rafts (en)
http://linked.open.../riv/klicoveSlovo	Death receptor 6 N- and O-glycosylations lipid rafts
http://linked.open...odStatuVydavatele	NL - Nizozemsko
http://linked.open...ontrolniKodProRIV	[1A0BD9137D4E]
http://linked.open...i/riv/nazevZdroje	Biochimica Et Biophysica Acta-Molecular Cell Research
http://linked.open...in/vavai/riv/obor	EB
http://linked.open...ichTvurcuVysledku	4 (xsd:int)
http://linked.open...cetTvurcuVysledku	4 (xsd:int)
http://linked.open...vavai/riv/projekt	Center of Molecular and Cellular Immunology
http://linked.open...UplatneniVysledku	2009
http://linked.open...v/svazekPeriodika	1793
http://linked.open...iv/tvurceVysledku	Anděra, Ladislav Doubravská, Lenka Klíma, Martin Zájedová, Jitka
http://linked.open...ain/vavai/riv/wos	000270481600004
http://linked.open...n/vavai/riv/zamer	Molekulárně genetické a buněčné základy klíčových biologických procesů: genová exprese, onkogeneze, replikace virů, imunita a vývoj organismů
issn	0167-4889
number of pages	9 (xsd:int)

Faceted Search & Find service v1.16.118 as of Jun 21 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 49 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software