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

Citation
J. Cools et al., A new family of small, palmitoylated, membrane-associated proteins, characterized by the presence of a cysteine-rich hydrophobic motif, FEBS LETTER, 492(3), 2001, pp. 204-209
Citations number
13
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
492
Issue
3
Year of publication
2001
Pages
204 - 209
Database
ISI
SICI code
0014-5793(20010316)492:3<204:ANFOSP>2.0.ZU;2-J
Abstract
We recently cloned the CHIC2 gene (previously BTL) by virtue of its involve ment in a chromosomal translocation t(4;12)(q11;p13) occurring in acute mye loid leukemias. In this study we show that CHIC2 is a member of a highly co nserved family of proteins characterized by the presence of a striking cyst eine-rich hydrophobic (CHIC) motif. Our data illustrate that cysteines in t his central CHIC motif are palmitoylated and that CHIC2 is associated with vesicular structures and the plasma membrane. The CHIC proteins thus resemb le 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.