J Physiol Physiology in Press
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


J Physiol Volume 586, Number 7, 1803-1810, April 1, 2008 DOI: 10.1113/jphysiol.2007.149187
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
586/7/1803    most recent
jphysiol.2007.149187v1
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Google Scholar
Right arrow Articles by Haitin, Y.
Right arrow Articles by Attali, B.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Haitin, Y.
Right arrow Articles by Attali, B.
Related Collections
Right arrow Review articles
Right arrow Neuroscience

SYMPOSIUM REPORT

The C-terminus of Kv7 channels: a multifunctional module

Yoni Haitin1 and Bernard Attali1

1 Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv 69978, Israel

Kv7 channels (KCNQ) represent a family of voltage-gated K+ channels which plays a prominent role in brain and cardiac excitability. Their physiological importance is underscored by the existence of mutations in human Kv7 genes, leading to severe cardiovascular and neurological disorders such as the cardiac long QT syndrome and neonatal epilepsy. Kv7 channels exhibit some structural and functional features that are distinct from other Kv channels. Notably, the Kv7 C-terminus is long compared to other K+ channels and is endowed with characteristic structural domains, including coiled-coils, amphipatic {alpha} helices containing calmodulin-binding motifs and basic amino acid clusters. Here we provide a brief overview of current insights and as yet unsettled issues about the structural and functional attributes of the C-terminus of Kv7 channels. Recent data indicate that the proximal half of the Kv7 C-terminus associates with one calmodulin constitutively bound to each subunit. Epilepsy and long QT mutations located in this proximal region impair calmodulin binding and can affect channel gating, folding and trafficking. The distal half of the Kv7 C-terminus directs tetramerization, employing tandem coiled-coils. Together, the data indicate that the Kv7 C-terminal domain is a multimodular structure playing a crucial role in channel gating, assembly and trafficking as well as in scaffolding the channel complex with signalling proteins.

(Received 2 December 2007; accepted after revision 24 January 2008; first published online 24 January 2008)
Corresponding author B. Attali: Department of Physiology and Pharmacology, Sackler Medical School, Tel Aviv University, Tel Aviv 69978, Israel.  Email: battali{at}post.tau.ac.il


This report was presented at a symposium on Kv7 (KCNQ) potassium channels that are mutated in human diseases, held at a joint meeting of The Slovak Physiological Society, The Physiological Society and The Federation of European Physiological Societies in Bratislava, Slovakia on 14 September 2007. It was commissioned by the Editorial Board and reflects the views of the authors.




This article has been cited by other articles:


Home page
Am. J. Physiol. Cell Physiol.Home page
F. Schuetz, S. Kumar, P. Poronnik, and D. J. Adams
Regulation of the voltage-gated K+ channels KCNQ2/3 and KCNQ3/5 by serum- and glucocorticoid-regulated kinase-1
Am J Physiol Cell Physiol, July 1, 2008; 295(1): C73 - C80.
[Abstract] [Full Text] [PDF]


Home page
J. Physiol.Home page
D. A. Brown
Kv7 (KCNQ) potassium channels that are mutated in human diseases
J. Physiol., April 1, 2008; 586(7): 1781 - 1783.
[Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2008 The Physiological Society.