Referenced in: none

Automatically associated channels: ClC4

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

Authors: Andrea Wächter, Blanche Schwappach

Journal, date & volume: FEBS Lett., 2005 Feb 14 , 579, 1149-53

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/15710404

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.