AJP - Renal Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Renal Physiol 290: F14-F19, 2006; doi:10.1152/ajprenal.00093.2005
0363-6127/06 $8.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
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 ISI Web of Science (10)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wang, W.-H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wang, W.-H.

INVITED REVIEW

Regulation of ROMK (Kir1.1) channels: new mechanisms and aspects

Wen-Hui Wang

Department of Pharmacology, New York Medical College, Valhalla, New York

This brief review attempts to provide an overview regarding recent developments in the regulation of ROMK channels. Studies performed in ROMK null mice suggest that ROMK cannot only form hometetramers such as the small-conductance (30-pS) K channels but also construct heterotetramers such as the 70-pS K channel in the thick ascending limb (TAL). The expression of ROMK channels in the plasma membrane is regulated by protein tyrosine kinase (PTK), serum and glucorticoid-induced kinase (SGK), and with-no-lysine-kinase 4. PTK is involved in mediating the effect of low K intake on ROMK channel activity. Increases in superoxide anions induced by low dietary K intake are responsible for the stimulation of PTK expression and tyrosine phosphorylation of ROMK channels. Finally, a recent study indicated that ROMK channels can be monoubiquitinated and monoubiquitination regulates the surface expression of ROMK channels.


Address for reprint requests and other correspondence: W. Hui Wang, Dept. of Pharmacology, New York Medical College, Valhalla, NY 10595 (e-mail: wenhui_wang{at}nym.edu)




This article has been cited by other articles:


Home page
 Am. J. Physiol. Renal Physiol.Home page
C. Huang, A. Sindic, C. E. Hill, K. M. Hujer, K. W. Chan, M. Sassen, Z. Wu, Y. Kurachi, S. Nielsen, M. F. Romero, et al.
Interaction of the Ca2+-sensing receptor with the inwardly rectifying potassium channels Kir4.1 and Kir4.2 results in inhibition of channel function
Am J Physiol Renal Physiol, March 1, 2007; 292(3): F1073 - F1081.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Regul. Integr. Comp. Physiol.Home page
G. Nishimoto, G. Sasaki, E. Yaoita, M. Nameta, H. Li, K. Furuse, H. Fujinaka, Y. Yoshida, A. Mitsudome, and T. Yamamoto
Molecular characterization of water-selective AQP (EbAQP4) in hagfish: insight into ancestral origin of AQP4
Am J Physiol Regulatory Integrative Comp Physiol, January 1, 2007; 292(1): R644 - R651.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Renal Physiol.Home page
J. L. Pluznick and S. C. Sansom
BK channels in the kidney: role in K+ secretion and localization of molecular components
Am J Physiol Renal Physiol, September 1, 2006; 291(3): F517 - F529.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online
Copyright © 2006 by the American Physiological Society.