The yeast CLC chloride channel is proteolytically processed by the furin-like protease Kex2p in the first extracellular loop |
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Authors: | Wächter Andrea Schwappach Blanche |
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Affiliation: | Zentrum für Molekulare Biologie (ZMBH), Universit?t Heidelberg, Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany. |
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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. |
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Keywords: | CLC chloride channel Intracellular ion channel Proteolytic processing Furin |
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