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

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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.