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

FEBS Lett. 2001 Mar 16;492(3):204-9. doi: 10.1016/s0014-5793(01)02240-2.

Abstract

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.

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Cell Membrane / metabolism
  • Cysteine / chemistry*
  • Cysteine / metabolism
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / classification
  • DNA-Binding Proteins / metabolism*
  • Green Fluorescent Proteins
  • Humans
  • K562 Cells
  • Luminescent Proteins / metabolism
  • Membrane Proteins / chemistry*
  • Membrane Proteins / classification
  • Membrane Proteins / metabolism
  • Mice
  • Molecular Sequence Data
  • Proto-Oncogene Proteins c-myc / metabolism
  • Rats
  • Sequence Homology, Amino Acid
  • Subcellular Fractions
  • Transcription Factors / chemistry
  • Transcription Factors / classification
  • Transcription Factors / metabolism*
  • Transport Vesicles / metabolism

Substances

  • CHIC2 protein, human
  • DNA-Binding Proteins
  • Luminescent Proteins
  • Membrane Proteins
  • Proto-Oncogene Proteins c-myc
  • Transcription Factors
  • Green Fluorescent Proteins
  • Cysteine

Associated data

  • GENBANK/AF248541