c-Cbl binds to tyrosine-phosphorylated neurotrophin receptor p75 and induces its ubiquitination

被引：22

作者：

Ohrt, T

Mancini, A

Tamura, T

Niedenthal, R ^{[1
]}

机构：

[1] Hannover Med Sch, Inst Biochem, D-30625 Hannover, Germany

[2] Tech Univ Dresden, Inst Biophys, D-01307 Dresden, Germany

来源：

CELLULAR SIGNALLING | 2004年 / 16卷 / 11期

关键词：

neurotrophin receptor p75; tyrosine phosphorylation; ubiquitination; signal transduction;

D O I：

10.1016/j.cellsig.2004.03.017

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The p75 neurotrophin receptor (p75(NTR)) has dual functions in cell survival and cell death but its intracellular signalling pathways are not understood. Here we describe that in rat brain and in pervanadate-stimulated PCNA and HEK293 cells p75(NTR) is phosphorylated at a single tyrosine residue within the cytosolic C-terminus. Phosphorylated tyrosine 308 constitutes a binding site for the ubiquitin ligase c-Cbl. This interaction is a prerequisite for ubiquitination of p75(NTR). Our data suggest a c-Cbl-dependent ubiquitination of p75(NTR) involved in the regulation of p75 NTR signalling. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：1291 / 1298

页数：8

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