Molecular Biology of the Cell Call for Nominations: MBC Editor-in-Chief

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
 QUICK SEARCH:   [advanced]


     


MBC in Press, published online ahead of print January 12, 2005
Mol. Biol. Cell 10.1091/mbc.E04-10-0885

A more recent version of this article appeared on March 1, 2005
This Article
Right arrow Full Text (PDF)
Right arrow Supplemental Material
Right arrow All Versions of this Article:
E04-10-0885v1
16/3/1417    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Glodowski, D. R.
Right arrow Articles by Rongo, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Glodowski, D. R.
Right arrow Articles by Rongo, C.

Submitted on October 8, 2004
Revised on December 10, 2004
Accepted on December 18, 2004

Distinct LIN-10 Domains Are Required for Its Neuronal Function, Its Epithelial Function, and Its Synaptic Localization

Doreen R. Glodowski,* Tricia Wright,* Keri Martinowich,* Howard Chia-Hao Chang, Douglas Beach, and Christopher Rongo{dagger}

The Waksman Institute, Department of Genetics, Rutgers University, Piscataway, NJ 08854

Monitoring Editor: Guido Guidotti

AMPA-type glutamate receptors (AMPARs) mediate excitatory neurotransmission at neuronal synapses, and their regulated localization plays a role in synaptic plasticity. In C. elegans, the PDZ and PTB domain-containing protein LIN-10 is required both for the synaptic localization of the AMPAR subunit GLR-1 and for vulval fate induction in epithelia. Here we examine the role that different LIN-10 domains play in GLR-1 localization. We find that an amino-terminal region of LIN-10 directs LIN-10 protein localization to the Golgi and to synaptic clusters. In addition, mutations in the carboxy-terminal PDZ domains prevent LIN-10 from regulating GLR-1 localization in neurons, but do not prevent LIN-10 from functioning in the vulval epithelia. A mutation in the amino-terminus prevents the protein from functioning in the vulval epithelia, but does not prevent it from functioning to regulate GLR-1 localization in neurons. Finally, we show that human Mint2 can substitute for LIN-10 to facilitate GLR-1 localization in neurons, and that the Mint2 amino-terminus is critical for this function. Taken together, our data suggest that LIN-10 uses distinct modular domains for its functions in neurons and epithelial cells, and that during evolution its vertebrate ortholog, Mint2, has retained the ability to direct AMPAR localization in neurons.


*These authors contributed equally to this work.

{dagger}Corresponding author. E-mail: rongo{at}waksman.rutgers.edu







Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2005 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.