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Bioinformatics Advance Access published online on April 6, 2006
Bioinformatics, doi:10.1093/bioinformatics/btl137
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© The Author (2006). Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org
Received January 28, 2006
Revised March 22, 2006
Accepted April 4, 2006

Discovery note

Intrinsically disordered C-terminal segments of voltage-activated potassium channels: a possible fishing rod-like mechanism for channel binding to scaffold proteins

Elhanan Magidovich 1, Sarel J. Fleishman 2, and Ofer Yifrach 1 *

1 Department of Life Sciences and the Zlotowski Center for Neurosciences, Ben Gurion University of the Negev, Beer Sheva, Israel
2 Department of Biochemistry, Tel Aviv University, Ramat Aviv, Israel


  Abstract

Membrane-embedded voltage-activated potassium channels (Kv) bind intracellular scaffold proteins, such as the Post Synaptic Density 95 (PSD-95) protein, using a conserved PDZ-binding motif located at the channels' C-terminal tip. This interaction underlies Kv-channel clustering, and is important for the proper assembly and functioning of the synapse. Here we demonstrate that the C-terminal segments of Kv channels adjacent to the PDZ-binding motif are intrinsically disordered. Phylogenetic analysis of the Kv channel family reveals a cluster of channel sequences belonging to three out of the four main channel families, for which an association is demonstrated between the presence of the consensus terminal PDZ-binding motif and the intrinsically disordered nature of the immediately adjacent C-terminal segment. Our observations, combined with a structural analogy to the N-terminal intra-molecular ball-and-chain mechanism for Kv channel inactivation, suggest that the C-terminal disordered segments of these channel families encode an inter-molecular fishing rod-like mechanism for K+ channel binding to scaffold proteins.

Associate Editor: Golan Yona
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Home page
 Proc. Natl. Acad. Sci. USAHome page
E. Magidovich, I. Orr, D. Fass, U. Abdu, and O. Yifrach
Intrinsic disorder in the C-terminal domain of the Shaker voltage-activated K+ channel modulates its interaction with scaffold proteins
PNAS, August 7, 2007; 104(32): 13022 - 13027.
[Abstract] [Full Text] [PDF]


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