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
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Amino Acid Sequence
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Cell Membrane / metabolism
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Chloride Channels / chemistry*
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Chloride Channels / genetics
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Chloride Channels / metabolism*
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Furin / metabolism
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Molecular Sequence Data
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Mutation / genetics
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Proprotein Convertases / metabolism*
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Protein Processing, Post-Translational*
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Saccharomyces cerevisiae / enzymology
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins / chemistry*
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
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Sequence Alignment
Substances
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Chloride Channels
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GEF1 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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Proprotein Convertases
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KEX2 protein, S cerevisiae
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Furin