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Functional analysis of the posttranslational modifications of the death receptor 6
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SYSNO ASEP 0333980 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Functional analysis of the posttranslational modifications of the death receptor 6 Author(s) Klíma, Martin (UMG-J)
Zájedová, Jitka (UMG-J)
Doubravská, Lenka (UMG-J)
Anděra, Ladislav (UMG-J) RIDNumber of authors 4 Source Title Biochimica Et Biophysica Acta-Molecular Cell Research. - : Elsevier - ISSN 0167-4889
Roč. 1793, č. 10 (2009), s. 1579-1587Number of pages 9 s. Language eng - English Country NL - Netherlands Keywords N- and O-glycosylations ; Death receptor 6 ; lipid rafts Subject RIV EB - Genetics ; Molecular Biology R&D Projects 1M0506 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z50520514 - UMG-J (2005-2011) UT WOS 000270481600004 DOI 10.1016/j.bbamcr.2009.07.008 Annotation 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. Workplace Institute of Molecular Genetics Contact Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Year of Publishing 2010
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