A new family of small, palmitoylated, membrane-associated proteins, characterized by the presence of a cysteine-rich hydrophobic motif

被引：12

作者：

Cools, J ^{[1
]}

Mentens, N ^{[1
]}

Marynen, P ^{[1
]}

机构：

[1] Katholieke Univ Leuven VIB, Ctr Human Genet, Lab Human Genome, B-3000 Leuven, Belgium

来源：

FEBS LETTERS | 2001年 / 492卷 / 03期

关键词：

palmitoylation; cysteine; membrane protein; protein family; leukemia;

D O I：

10.1016/S0014-5793(01)02240-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We recently cloned the CHIC2 gene (previously BTL) by virtue of its involvement in a chromosomal translocation t(4;12)(q11;p13) occurring in acute myeloid leukemias. In this study we show that CHIC2 is a member of a highly conserved family of proteins characterized by the presence of a striking cysteine-rich hydrophobic (CHIC) motif. Our data illustrate that cysteines in this central CHIC motif are palmitoylated and that CHIC2 is associated with vesicular structures and the plasma membrane. The CHIC proteins thus resemble the cysteine string proteins, which function in regulated exocytosis. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：204 / 209

页数：6