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Transmembrane domain length of viral K+ channels is a signal for mitochondria targeting.

Balss, Jörg and Papatheodorou, Panagiotis and Mehmel, Mario and Baumeister, Dirk and Hertel, Brigitte and Delaroque, Nicolas and Chatelain, Franck C. and Minor, Daniel L. and Van Etten, James L. and Rassow, Joachim and Moroni, Anna and Thiel, Gerhard (2008):
Transmembrane domain length of viral K+ channels is a signal for mitochondria targeting.
In: Proceedings of the National Academy of Sciences of the United States of America, pp. 12313-8, 105, (34), ISSN 1091-6490,
[Article]

Abstract

K(+) channels operate in the plasma membrane and in membranes of organelles including mitochondria. The mechanisms and topogenic information for their differential synthesis and targeting is unknown. This article describes 2 similar viral K(+) channels that are differentially sorted; one protein (Kesv) is imported by the Tom complex into the mitochondria, the other (Kcv) to the plasma membrane. By creating chimeras we discovered that mitochondrial sorting of Kesv depends on a hierarchical combination of N- and C-terminal signals. Crucial is the length of the second transmembrane domain; extending its C terminus by > or = 2 hydrophobic amino acids redirects Kesv from the mitochondrial to the plasma membrane. Activity of Kesv in the plasma membrane is detected electrically or by yeast rescue assays only after this shift in sorting. Hence only minor structural alterations in a transmembrane domain are sufficient to switch sorting of a K(+) channel between the plasma membrane and mitochondria.

Item Type: Article
Erschienen: 2008
Creators: Balss, Jörg and Papatheodorou, Panagiotis and Mehmel, Mario and Baumeister, Dirk and Hertel, Brigitte and Delaroque, Nicolas and Chatelain, Franck C. and Minor, Daniel L. and Van Etten, James L. and Rassow, Joachim and Moroni, Anna and Thiel, Gerhard
Title: Transmembrane domain length of viral K+ channels is a signal for mitochondria targeting.
Language: English
Abstract:

K(+) channels operate in the plasma membrane and in membranes of organelles including mitochondria. The mechanisms and topogenic information for their differential synthesis and targeting is unknown. This article describes 2 similar viral K(+) channels that are differentially sorted; one protein (Kesv) is imported by the Tom complex into the mitochondria, the other (Kcv) to the plasma membrane. By creating chimeras we discovered that mitochondrial sorting of Kesv depends on a hierarchical combination of N- and C-terminal signals. Crucial is the length of the second transmembrane domain; extending its C terminus by > or = 2 hydrophobic amino acids redirects Kesv from the mitochondrial to the plasma membrane. Activity of Kesv in the plasma membrane is detected electrically or by yeast rescue assays only after this shift in sorting. Hence only minor structural alterations in a transmembrane domain are sufficient to switch sorting of a K(+) channel between the plasma membrane and mitochondria.

Journal or Publication Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 105
Number: 34
Divisions: 10 Department of Biology > Plant Membrane Biophysics
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10 Department of Biology
Date Deposited: 22 Jun 2011 07:12
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