FEBS Letters | |
A new family of small, palmitoylated, membrane‐associated proteins, characterized by the presence of a cysteine‐rich hydrophobic motif | |
Cools, Jan1  Mentens, Nicole1  Marynen, Peter1  | |
[1] The Human Genome Laboratory, Center for Human Genetics, University of Leuven, Flanders Interuniversity Institute for Biotechnology (VIB), Herestraat 49, B-3000 Leuven, Belgium | |
关键词: Palmitoylation; Cysteine; Membrane protein; Protein family; Leukemia; CSP; cysteine string protein; EGFP; enhanced green fluorescent protein; ORF; open reading frame; | |
DOI : 10.1016/S0014-5793(01)02240-2 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
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【 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.
【 授权许可】
Unknown
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