Am J Physiol Cell Physiol AJP: Heart and Circulatory Physiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol 283: C1784-C1794, 2002. First published August 22, 2002; doi:10.1152/ajpcell.00061.2002
0363-6143/02 $5.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
283/6/C1784    most recent
00061.2002v1
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 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 Web of Science (6)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kizhatil, K.
Right arrow Articles by Albritton, L. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kizhatil, K.
Right arrow Articles by Albritton, L. M.
Vol. 283, Issue 6, C1784-C1794, December 2002

System y+ localizes to different membrane subdomains in the basolateral plasma membrane of epithelial cells

Krishnakumar Kizhatil and Lorraine M. Albritton

Department of Molecular Sciences, University of Tennessee Health Sciences Center, Memphis, Tennessee 38163

We report here that the system y+ cationic amino acid transporter ATRC1 localized to clusters within the basolateral membrane of polarized Madin-Darby canine kidney and human embryonic kidney (HEK) cells, suggesting that the transporters are restricted to discrete membrane microdomains in epithelial cells. Based on solubility in nonionic detergents, two populations of ATRC1 molecules existed: approximately half of the total ATRC1 in HEK cells associated with the actin membrane cytoskeleton, whereas another one-fourth resided in detergent-resistant membranes (DRM). In agreement with these findings, cytochalasin D reduced the amount of ATRC1 associated with the actin membrane cytoskeleton. Although some ATRC1 clusters in HEK cells colocalized with caveolin, the majority of ATRC1 did not colocalize with this marker protein for a type of DRM called caveolae. This distribution of ATRC1 is somewhat different from that reported for pulmonary artery endothelial cells in which transporters cluster predominantly in caveolae, suggesting that differences in the proportion of ATRC1 in specific membrane microdomains correlate with differences in the physiological role of the transporter in polarized kidney epithelial vs. vascular endothelial cells.

system y+; membrane microdomains; rafts; F-actin membrane cytoskeleton; retrovirus receptor


This article has been cited by other articles:


Home page
 Am. J. Physiol. Cell Physiol.Home page
R. Martin-Venegas, M. J. Rodriguez-Lagunas, Y. Mercier, P.-A. Geraert, and R. Ferrer
Effect of pH on L- and D-methionine uptake across the apical membrane of Caco-2 cells
Am J Physiol Cell Physiol, March 1, 2009; 296(3): C632 - C638.
[Abstract] [Full Text] [PDF]

Home page
 J. Nutr.Home page
E. I. Closs, A. Simon, N. Vekony, and A. Rotmann
Plasma Membrane Transporters for Arginine
J. Nutr., October 1, 2004; 134(10): 2752S - 2759S.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
Z. Qian, H. Wang, C. Empig, W. F. Anderson, and L. M. Albritton
Complementation of a Binding-Defective Retrovirus by a Host Cell Receptor Mutant
J. Virol., June 1, 2004; 78(11): 5766 - 5772.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online