Functional analysis of the posttranslational modifications of the death receptor 6

0333980 - ÚMG 2010 RIV NL eng J - Journal Article
Klíma, Martin - Zájedová, Jitka - Doubravská, Lenka - Anděra, Ladislav
Functional analysis of the posttranslational modifications of the death receptor 6.
Biochimica Et Biophysica Acta-Molecular Cell Research. Roč. 1793, č. 10 (2009), s. 1579-1587. ISSN 0167-4889. E-ISSN 1879-2596
R&D Projects: GA MŠMT 1M0506
Institutional research plan: CEZ:AV0Z50520514
Keywords : N- and O-glycosylations * Death receptor 6 * lipid rafts
Subject RIV: EB - Genetics ; Molecular Biology
Impact factor: 4.374, year: 2009

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.
Permanent Link: http://hdl.handle.net/11104/0178830