The yeast CLC chloride channel is proteolytically processed by the furin-like protease Kex2p in the first extracellular loop

FEBS Lett. 2005 Feb 14;579(5):1149-53. doi: 10.1016/j.febslet.2005.01.011.

Abstract

CLC chloride channels are a family of channel proteins mediating chloride transport across the plasma membrane and intracellular membranes. The single yeast CLC protein Gef1p is localized to the Golgi and endosomal system. Investigating epitope-tagged variants of Gef1p, we found that the channel is proteolytically processed in the secretory pathway. Proteolytic cleavage occurs in the first extracellular loop of the protein at residues KR136/137 and is carried out by the Kex2p protease. Fragments mimicking the N- and C-terminal products of the cleavage reaction are non-functional when expressed alone. However, functional channels can assemble when the two fragments are co-expressed.

MeSH terms

  • Amino Acid Sequence
  • Cell Membrane / metabolism
  • Chloride Channels / chemistry*
  • Chloride Channels / genetics
  • Chloride Channels / metabolism*
  • Furin / metabolism
  • Molecular Sequence Data
  • Mutation / genetics
  • Proprotein Convertases / metabolism*
  • Protein Processing, Post-Translational*
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Sequence Alignment

Substances

  • Chloride Channels
  • GEF1 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Proprotein Convertases
  • KEX2 protein, S cerevisiae
  • Furin