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A new family of small, palmitoylated, membrane‐associated proteins, characterized by the presence of a cysteine‐rich hydrophobic motif
Author(s) -
Cools Jan,
Mentens Nicole,
Marynen Peter
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02240-2
Subject(s) - cysteine , microbiology and biotechnology , chemistry , exocytosis , gene , chromosomal translocation , biology , biochemistry , membrane , enzyme
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.