| First Author | Cools J | Year | 2001 |
| Journal | FEBS Lett | Volume | 492 |
| Issue | 3 | Pages | 204-9 |
| PubMed ID | 11257495 | Mgi Jnum | J:68154 |
| Mgi Id | MGI:1932194 | Doi | 10.1016/s0014-5793(01)02240-2 |
| Citation | Cools J, et al. (2001) A new family of small, palmitoylated, membrane-associated proteins, characterized by the presence of a cysteine-rich hydrophobic motif(1). FEBS Lett 492(3):204-9 |
| abstractText | 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. |
