CLIC4 (p64H1) and its putative transmembrane domain form poorly selective, redox-regulated ion channels.

@article{Singh2007CLIC4A,
  title={CLIC4 (p64H1) and its putative transmembrane domain form poorly selective, redox-regulated ion channels.},
  author={Harpreet Singh and Richard H. Ashley},
  journal={Molecular membrane biology},
  year={2007},
  volume={24 1},
  pages={41-52}
}
Despite being synthesized in the cytosol without a leader sequence, the soluble 253-residue mammalian protein CLIC4 (Chloride Intracellular Channel 4, or p64H1), a structural homologue of Omega-type glutathione-S-transferase, autoinserts into membranes to form an integral membrane protein with ion channel activity. A predicted transmembrane domain (TMD) near the N-terminus of CLIC4 could mediate membrane insertion, and contribute to oligomeric pores, with minimal reorganization of the soluble… CONTINUE READING
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