|
|
||||||||
Viewpoint |
Department of Physiology and Biophysics, Mount Sinai School of Medicine of NYU, New York, NY 10029
SUMMARY
Ma et al. have reported that different G protein-regulated inwardly rectifying K+ (GIRK) channels composed of combinations of Kir3.1-Kir3.2-Kir3.3-Kir3.4 are localized to different subcellular compartments. Kir3.3 seems to target Kir3.1-containing channels to lysosomes, whereas Kir3.1-containing channels also consisting of Kir3.2 or Kir3.4 are successfully expressed at the cell surface. The new results suggest a mechanism whereby the surface expression of heterotetramers is controlled and thus channel density can be properly maintained. Mirshahi and Logothetis discuss the results and their implications for channel trafficking, but caution that we are far from understanding the whole regulatory process and that, indeed, other mechanisms participate in maintaining channel density.
This article has been cited by other articles:
![]() |
S. R. Pondugula, N. N. Raveendran, Z. Ergonul, Y. Deng, J. Chen, J. D. Sanneman, L. G. Palmer, and D. C. Marcus Glucocorticoid regulation of genes in the amiloride-sensitive sodium transport pathway by semicircular canal duct epithelium of neonatal rat Physiol Genomics, January 12, 2006; 24(2): 114 - 123. [Abstract] [Full Text] [PDF] |
||||
![]() |
T. Mirshahi and D. E. Logothetis Molecular Determinants Responsible for Differential Cellular Distribution of G Protein-gated Inwardly Rectifying K+ Channels J. Biol. Chem., March 19, 2004; 279(12): 11890 - 11897. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| ASPET Journals | Pharmacological Reviews | Drug Metabolism and Disposition |
| Molecular Interventions | Molecular Pharmacology | J Pharmacology and Exp Therapeutics |