WWW.JNEUROSCI.ORG
-
The Journal of Neuroscience
 QUICK SEARCH:   [advanced]


     
-


HOME
  |  
SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Submit an eLetter
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
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
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Web of Science (21)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wreden, C. C.
Right arrow Articles by Edwards, R. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wreden, C. C.
Right arrow Articles by Edwards, R. H.

 Previous Article  |  Next Article 

The Journal of Neuroscience, February 15, 2003, 23(4):1265

The H+-Coupled Electrogenic Lysosomal Amino Acid Transporter LYAAT1 Localizes to the Axon and Plasma Membrane of Hippocampal Neurons

Christopher C. Wreden1, Juliette Johnson2, Cindy Tran1, Rebecca P. Seal1, David R. Copenhagen2, Richard J. Reimer1, 3, and Robert H. Edwards1

Departments of 1 Neurology and Physiology and 2 Ophthalmology and Physiology, and 3 Graduate Programs in Neuroscience and Cell Biology, University of California San Francisco School of Medicine, San Francisco, California 94143

Recent work has identified a lysosomal protein that transports neutral amino acids (LYAAT1). We now show that LYAAT1 mediates H+ cotransport with a stoichiometry of 1 H+/1 amino acid, consistent with a role in the active efflux of amino acids from lysosomes. In neurons, however, LYAAT1 localizes to axonal processes as well as lysosomes. In axons LYAAT1 fails to colocalize with synaptic markers. Rather, axonal LYAAT1 colocalizes with the exocyst, suggesting a role for membranes expressing LYAAT1 in specifying sites for exocytosis. A protease protection assay and measurements of intracellular pH further indicate abundant expression at the plasma membrane, raising the possibility of physiological roles for LYAAT1 on the cell surface as well as in lysosomes.

Key words: LYAAT1; lysosome; neutral amino acid transport; exocyst; axon; neuronal ceroid lipofuscinosis


Copyright © 2003 Society for Neuroscience  0270-6474/03/2341265-11$05.00/0


This article has been cited by other articles:


Home page
Am. J. Physiol. Renal Physiol.Home page
A. Taranta, S. Petrini, A. Palma, L. Mannucci, M. J. Wilmer, V. De Luca, F. Diomedi-Camassei, S. Corallini, F. Bellomo, L. P. van den Heuvel, et al.
Identification and subcellular localization of a new cystinosin isoform
Am J Physiol Renal Physiol, May 1, 2008; 294(5): F1101 - F1108.
[Abstract] [Full Text] [PDF]


Home page
J Antimicrob ChemotherHome page
C. Lecaroz, M. J. Blanco-Prieto, M. A. Burrell, and C. Gamazo
Intracellular killing of Brucella melitensis in human macrophages with microsphere-encapsulated gentamicin
J. Antimicrob. Chemother., September 1, 2006; 58(3): 549 - 556.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
C. C. Wreden, M. Wlizla, and R. J. Reimer
Varied Mechanisms Underlie the Free Sialic Acid Storage Disorders
J. Biol. Chem., January 14, 2005; 280(2): 1408 - 1416.
[Abstract] [Full Text] [PDF]


Home page
Mol. Pharmacol.Home page
J. H. Gray, L. M. Mangravite, R. P. Owen, T. J. Urban, W. Chan, E. J. Carlson, C. C. Huang, M. Kawamoto, S. J. Johns, D. Stryke, et al.
Functional and Genetic Diversity in the Concentrative Nucleoside Transporter, CNT1, in Human Populations
Mol. Pharmacol., March 1, 2004; 65(3): 512 - 519.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
I. Rubio-Aliaga, M. Boll, D. M. Vogt Weisenhorn, M. Foltz, G. Kottra, and H. Daniel
The Proton/Amino Acid Cotransporter PAT2 Is Expressed in Neurons with a Different Subcellular Localization than Its Paralog PAT1
J. Biol. Chem., January 23, 2004; 279(4): 2754 - 2760.
[Abstract] [Full Text] [PDF]



-
-

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help

-
Copyright 2009 by Society for Neuroscience ONLINE ISSN: 1529-2401
-