Am J Physiol Cell Physiol Ad Instruments
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol (November 27, 2002). doi:10.1152/ajpcell.00479.2002
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
284/4/C910    most recent
00479.2002v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
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
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Konstas, A.-A.
Right arrow Articles by Tucker, S. J
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Konstas, A.-A.
Right arrow Articles by Tucker, S. J

Articles in PresS, published online ahead of print November 27, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00479.2002
Submitted on October 15, 2002
Accepted on November 26, 2002

IDENTIFICATION OF DOMAINS WHICH CONTROL THE HETEROMERIC ASSEMBLY OF Kir5.1/Kir4.0 POTASSIUM CHANNELS

Angelos-Aristeidis Konstas1, Christoph Korbmacher2, and Stephen J Tucker1*

1 University Laboratory of Physiology, Oxford University, Oxford, United Kingdom
2 University Laboratory of Physiology, Oxford University, Oxford, United Kingdom; Institut fur Zellulare und Molekulare Physiologie, Universitat Erlangen-Nurnberg, Erlangen, Germany

* To whom correspondence should be addressed. E-mail: stephen.tucker{at}physiol.ox.ac.uk.

Heteromultimerisation between different inwardly-rectifying (Kir) potassium channel subunits is an important mechanism for the generation of functional diversity. However, little is known about the mechanisms which control this process and which prevent promiscuous interactions in cells which express many different Kir subunits. In this study we have examined the heteromeric assembly of Kir5.1 with other Kir subunits and shown that this subunit exhibits a highly selective interaction with members of the Kir4.0 subfamily and does not physically associate with other Kir subunits such as Kir1.1, Kir2.1 and Kir6.2. Furthermore, we have identified regions within the Kir4.1 subunit which appear to govern the specificity of this interaction. These results help us to understand the mechanisms which control Kir subunit recognition and assembly, and how cells can express many different Kir channels whilst maintaining distinct subpopulations of homo- and heteromeric channels within the cell.




This article has been cited by other articles:


Home page
 Am. J. Physiol. Renal Physiol.Home page
A. Sindic, C. Huang, A.-P. Chen, Y. Ding, W. A. Miller-Little, D. Che, M. F. Romero, and R. T. Miller
MUPP1 complexes renal K+ channels to alter cell surface expression and whole cell currents
Am J Physiol Renal Physiol, July 1, 2009; 297(1): F36 - F45.
[Abstract] [Full Text] [PDF]

Home page
 Physiol. Rev.Home page
S. C. Hebert, G. Desir, G. Giebisch, and W. Wang
Molecular Diversity and Regulation of Renal Potassium Channels
Physiol Rev, January 1, 2005; 85(1): 319 - 371.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
D. H. Malinowska, A. M. Sherry, K. P. Tewari, and J. Cuppoletti
Gastric parietal cell secretory membrane contains PKA- and acid-activated Kir2.1 K+ channels
Am J Physiol Cell Physiol, March 1, 2004; 286(3): C495 - C506.
[Abstract] [Full Text]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Visit Other APS Journals Online
Copyright © 1976 by the American Physiological Society.