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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. The yeast CLC chloride channel is proteolytically processed by the furin-like protease Kex2p in the first extracellular loop. Wächter, A., Schwappach, B. FEBS Lett. (2005) [Pubmed]
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