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J. Biol. Chem., Vol. 281, Issue 6, 3669-3678, February 10, 2006

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 281/6/3669    most recent M511725200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lisé, M.-F. Articles by El-Husseini, A. Search for Related Content PubMed PubMed Citation Articles by Lisé, M.-F. Articles by El-Husseini, A. Social Bookmarking                      What's this?

Involvement of Myosin Vb in Glutamate Receptor Trafficking^*

Marie-France Lisé¹, Tak Pan Wong, Alex Trinh, Rochelle M. Hines, Lidong Liu, Rujun Kang, Dustin J. Hines, Jie Lu, James R. Goldenring^¶2, Yu Tian Wang, and Alaa El-Husseini³

From the Departments of Psychiatry and Medicine, Brain Research Centre, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada and ^¶Department of Surgery, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-2733

Myosin V motors mediate cargo transport; however, the identity of neuronal molecules transported by these proteins remains unknown. Here we show that myosin Vb is expressed in several neuronal populations and associates with the -amino-3-hydroxy-5-methyl-4-isoxazole propionate-type glutamate receptor subunit GluR1. In developing hippocampal neurons, expression of the tail domain of myosin Vb, but not myosin Va, enhanced GluR1 accumulation in the soma and reduced its surface expression. These changes were accompanied by reduced GluR1 clustering and diminished frequency of excitatory but not inhibitory synaptic currents. Similar effects were observed upon expression of full-length myosin Vb lacking a C-terminal region required for binding to the small GTPase Rab11. In contrast, mutant myosin Vb did not change the localization of several other neurotransmitter receptors, including the glutamate receptor subunit NR1. These results reveal a novel mechanism for the transport of a specific glutamate receptor subunit in neurons mediated by a member of the myosin V family.

Received for publication, October 31, 2005

^* This work was supported in part by grants from the Canadian Institutes for Health

Research and the Michael Smith Foundation for Health Research (to A. E.-H. and Y. T. W.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains Supplemental Figs. S1-S7 and Appendix 1.

¹ Supported by a University of British Columbia graduate fellowship and the Michael Smith Foundation for Health Research.

² Supported by National Institutes of Health Grant DK48370.

³ Supported by funds from the EJLB foundation. To whom correspondence should be addressed. Tel.: 604-822-7526; E-mail: alaa{at}interchange.ubc.ca.

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