Involvement of Myosin Vb in Glutamate Receptor Trafficking
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 α-amino-3-hydroxy-5-methyl-4-isoxazole propionate-type glutamate recept...
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Veröffentlicht in: | The Journal of biological chemistry 2006-02, Vol.281 (6), p.3669-3678 |
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creator | Lisé, Marie-France Wong, Tak Pan Trinh, Alex Hines, Rochelle M. Liu, Lidong Kang, Rujun Hines, Dustin J. Lu, Jie Goldenring, James R. Wang, Yu Tian El-Husseini, Alaa |
description | 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 α-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. |
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Here we show that myosin Vb is expressed in several neuronal populations and associates with the α-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.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M511725200</identifier><identifier>PMID: 16338934</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Blotting, Western ; Brain - metabolism ; Cell Line ; Chlorocebus aethiops ; Cloning, Molecular ; COS Cells ; DNA, Complementary - metabolism ; Electrophysiology ; Female ; Glutathione Transferase - metabolism ; Hippocampus - embryology ; Image Processing, Computer-Assisted ; Immunohistochemistry ; Microscopy, Fluorescence ; Mutagenesis ; Mutation ; Myosin Type V - chemistry ; Myosins - chemistry ; Neurons - metabolism ; Neurotransmitter Agents - metabolism ; Protein Binding ; Protein Structure, Tertiary ; Protein Transport ; rab GTP-Binding Proteins - metabolism ; Rats ; Rats, Wistar ; Receptors, AMPA - metabolism ; Receptors, Glutamate - chemistry ; Receptors, Glutamate - metabolism ; Subcellular Fractions ; Transfection</subject><ispartof>The Journal of biological chemistry, 2006-02, Vol.281 (6), p.3669-3678</ispartof><rights>2006 © 2006 ASBMB. 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Here we show that myosin Vb is expressed in several neuronal populations and associates with the α-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. 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Wong, Tak Pan ; Trinh, Alex ; Hines, Rochelle M. ; Liu, Lidong ; Kang, Rujun ; Hines, Dustin J. ; Lu, Jie ; Goldenring, James R. ; Wang, Yu Tian ; El-Husseini, Alaa</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c485t-67c9a759283781cccd91492a69a909ed0ec4f1fbfa4657dc38a47a7fd01cf8ab3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Animals</topic><topic>Blotting, Western</topic><topic>Brain - metabolism</topic><topic>Cell Line</topic><topic>Chlorocebus aethiops</topic><topic>Cloning, Molecular</topic><topic>COS Cells</topic><topic>DNA, Complementary - metabolism</topic><topic>Electrophysiology</topic><topic>Female</topic><topic>Glutathione Transferase - metabolism</topic><topic>Hippocampus - embryology</topic><topic>Image Processing, Computer-Assisted</topic><topic>Immunohistochemistry</topic><topic>Microscopy, Fluorescence</topic><topic>Mutagenesis</topic><topic>Mutation</topic><topic>Myosin Type V - chemistry</topic><topic>Myosins - chemistry</topic><topic>Neurons - metabolism</topic><topic>Neurotransmitter Agents - metabolism</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Transport</topic><topic>rab GTP-Binding Proteins - metabolism</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Receptors, AMPA - metabolism</topic><topic>Receptors, Glutamate - chemistry</topic><topic>Receptors, Glutamate - metabolism</topic><topic>Subcellular Fractions</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lisé, Marie-France</creatorcontrib><creatorcontrib>Wong, Tak Pan</creatorcontrib><creatorcontrib>Trinh, Alex</creatorcontrib><creatorcontrib>Hines, Rochelle M.</creatorcontrib><creatorcontrib>Liu, Lidong</creatorcontrib><creatorcontrib>Kang, Rujun</creatorcontrib><creatorcontrib>Hines, Dustin J.</creatorcontrib><creatorcontrib>Lu, Jie</creatorcontrib><creatorcontrib>Goldenring, James R.</creatorcontrib><creatorcontrib>Wang, Yu Tian</creatorcontrib><creatorcontrib>El-Husseini, Alaa</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lisé, Marie-France</au><au>Wong, Tak Pan</au><au>Trinh, Alex</au><au>Hines, Rochelle M.</au><au>Liu, Lidong</au><au>Kang, Rujun</au><au>Hines, Dustin J.</au><au>Lu, Jie</au><au>Goldenring, James R.</au><au>Wang, Yu Tian</au><au>El-Husseini, Alaa</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Involvement of Myosin Vb in Glutamate Receptor Trafficking</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2006-02-10</date><risdate>2006</risdate><volume>281</volume><issue>6</issue><spage>3669</spage><epage>3678</epage><pages>3669-3678</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>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 α-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. 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subjects | Animals Blotting, Western Brain - metabolism Cell Line Chlorocebus aethiops Cloning, Molecular COS Cells DNA, Complementary - metabolism Electrophysiology Female Glutathione Transferase - metabolism Hippocampus - embryology Image Processing, Computer-Assisted Immunohistochemistry Microscopy, Fluorescence Mutagenesis Mutation Myosin Type V - chemistry Myosins - chemistry Neurons - metabolism Neurotransmitter Agents - metabolism Protein Binding Protein Structure, Tertiary Protein Transport rab GTP-Binding Proteins - metabolism Rats Rats, Wistar Receptors, AMPA - metabolism Receptors, Glutamate - chemistry Receptors, Glutamate - metabolism Subcellular Fractions Transfection |
title | Involvement of Myosin Vb in Glutamate Receptor Trafficking |
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