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

Standard

The yeast CLC chloride channel is proteolytically processed by the furin-like protease Kex2p in the first extracellular loop. / Wächter, Andrea; Schwappach, Blanche.

in: FEBS LETT, Jahrgang 579, Nr. 5, 14.02.2005, S. 1149-53.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Wächter, A & Schwappach, B 2005, 'The yeast CLC chloride channel is proteolytically processed by the furin-like protease Kex2p in the first extracellular loop', FEBS LETT, Jg. 579, Nr. 5, S. 1149-53. https://doi.org/10.1016/j.febslet.2005.01.011

APA

Wächter, A., & Schwappach, B. (2005). The yeast CLC chloride channel is proteolytically processed by the furin-like protease Kex2p in the first extracellular loop. FEBS LETT, 579(5), 1149-53. https://doi.org/10.1016/j.febslet.2005.01.011

Vancouver

Wächter A, Schwappach B. The yeast CLC chloride channel is proteolytically processed by the furin-like protease Kex2p in the first extracellular loop. FEBS LETT. 2005 Feb 14;579(5):1149-53. https://doi.org/10.1016/j.febslet.2005.01.011

Bibtex

@article{1bbd5ae6a5d04287b9afaf57594a0650,
title = "The yeast CLC chloride channel is proteolytically processed by the furin-like protease Kex2p in the first extracellular loop",
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.",
keywords = "Amino Acid Sequence, Cell Membrane/metabolism, Chloride Channels/chemistry, Furin/metabolism, Molecular Sequence Data, Mutation/genetics, Proprotein Convertases/metabolism, Protein Processing, Post-Translational, Saccharomyces cerevisiae/enzymology, Saccharomyces cerevisiae Proteins/chemistry, Sequence Alignment",
author = "Andrea W{\"a}chter and Blanche Schwappach",
year = "2005",
month = feb,
day = "14",
doi = "10.1016/j.febslet.2005.01.011",
language = "English",
volume = "579",
pages = "1149--53",
journal = "FEBS LETT",
issn = "0014-5793",
publisher = "Elsevier",
number = "5",

}

RIS

TY - JOUR

T1 - The yeast CLC chloride channel is proteolytically processed by the furin-like protease Kex2p in the first extracellular loop

AU - Wächter, Andrea

AU - Schwappach, Blanche

PY - 2005/2/14

Y1 - 2005/2/14

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Cell Membrane/metabolism

KW - Chloride Channels/chemistry

KW - Furin/metabolism

KW - Molecular Sequence Data

KW - Mutation/genetics

KW - Proprotein Convertases/metabolism

KW - Protein Processing, Post-Translational

KW - Saccharomyces cerevisiae/enzymology

KW - Saccharomyces cerevisiae Proteins/chemistry

KW - Sequence Alignment

U2 - 10.1016/j.febslet.2005.01.011

DO - 10.1016/j.febslet.2005.01.011

M3 - SCORING: Journal article

C2 - 15710404

VL - 579

SP - 1149

EP - 1153

JO - FEBS LETT

JF - FEBS LETT

SN - 0014-5793

IS - 5

ER -