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 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. 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. Proper sorting and transport of excitatory neurotransmitter receptors and associated proteins is essential for neuronal activity and plasticity. Recent studies have identified several proteins that regulate clustering of neurotransmitter receptors at the synapse (1Kim E. Sheng M. Nat. Rev. Neurosci. 2004; 5: 771-781Crossref PubMed Scopus (1218) Google Scholar). However, it remains unknown what proteins mediate sorting and delivery of receptors from the soma to postsynaptic sites. Molecular motors that regulate cargo trafficking on both actin filaments and microtubules have been implicated in initial transport and delivery to specific subcellular sites (2Bridgman P.C. J. Neurobiol. 2004; 58: 164-174Crossref PubMed Scopus (83) Google Scholar, 3Hirokawa N. Takemura R. Nat. Rev. Neurosci. 2005; 6: 201-214Crossref PubMed Scopus (664) Google Scholar). In particular, class V of unconventional myosins is actin-based motors thought to regulate trafficking of organelles and associated proteins in neuronal cells (2Bridgman P.C. J. Neurobiol. 2004; 58: 164-174Crossref PubMed Scopus (83) Google Scholar, 4Langford G.M. Traffic. 2002; 3: 859-865Crossref PubMed Scopus (177) Google Scholar). Three known members of the myosin V family have been detected in brain extracts. The most studied member, myosin Va, is widely expressed in the brain (5Tilelli C.Q. Martins A.R. Larson R.E. Garcia-Cairasco N. Neuroscience. 2003; 121: 573-586Crossref PubMed Scopus (28) Google Scholar). Dilute mice, which possess mutation in the myosin Va gene, suffer from impaired melanosome transport and severe seizures and die within 2-3 weeks after birth (6Mercer J.A. Seperack P.K. Strobel M.C. Copeland N.G. Jenkins N.A. Nature. 1991; 349: 709-713Crossref PubMed Scopus (457) Google Scholar). These observations suggest that alteration in the transport of important yet unknown cargos contributed to the observed defects in neuronal function. In neurons, myosin Va is enriched at the postsynaptic density (PSD) 4The abbreviations used are: PSD, postsynaptic density; GFP, green fluorescent protein; AMPA, α-amino-3-hydroxy-5-methyl-4-isoxazole propionate; mEPSC, miniature excitatory postsynaptic current; mIPSC, miniature inhibitory postsynaptic current; ER, endoplasmic reticulum; DIV, days in vitro; HEK cells, human embryonic kidney cells; Syn, synaptophysin; BERP, brain-expressed ring finger protein. 4The abbreviations used are: PSD, postsynaptic density; GFP, green fluorescent protein; AMPA, α-amino-3-hydroxy-5-methyl-4-isoxazole propionate; mEPSC, miniature excitatory postsynaptic current; mIPSC, miniature inhibitory postsynaptic current; ER, endoplasmic reticulum; DIV, days in vitro; HEK cells, human embryonic kidney cells; Syn, synaptophysin; BERP, brain-expressed ring finger protein. of excitatory synapses (7Walikonis R.S. Jensen O.N. Mann M. Provance Jr., D.W. Mercer J.A. Kennedy M.B. J. Neurosci. 2000; 20: 4069-4080Crossref PubMed Google Scholar) and associates with the scaffolding guanylate kinase domain-associated protein through interaction with the dynein light chain (8Naisbitt S. Valtschanoff J. Allison D.W. Sala C. Kim E. Craig A.M. Weinberg R.J. Sheng M. J. Neurosci. 2000; 20: 4524-4534Crossref PubMed Google Scholar). The association of guanylate kinase domain-associated protein with the postsynaptic density protein-95 (PSD-95), a protein involved in glutamate receptor clustering, may functionally couple these proteins to myosin Va (1Kim E. Sheng M. Nat. Rev. Neurosci. 2004; 5: 771-781Crossref PubMed Scopus (1218) Google Scholar, 9Kim E. Naisbitt S. Hsueh Y.P. Rao A. Rothschild A. Craig A.M. Sheng M. J. Cell Biol. 1997; 136: 669-678Crossref PubMed Scopus (429) Google Scholar). Myosin Vb and myosin Vc are two additional members of the myosin V family that are also expressed in the brain; however, their exact localization in neurons remains unclear (10Zhao L.P. Koslovsky J.S. Reinhard J. Bahler M. Witt A.E. Provance Jr., D.W. Mercer J.A. Proc. Natl. Acad. Sci. U. S. A. 1996; 93: 10826-10831Crossref PubMed Scopus (76) Google Scholar, 11Rodriguez O.C. Cheney R.E. J. Cell Sci. 2002; 115: 991-1004Crossref PubMed Google Scholar). All of these motors share ∼42% identity and contain a conserved N-terminal motor domain followed by a coiled-coil region and a globular C-terminal tail. The globular tail of class V myosins contains the cargo binding domain (2Bridgman P.C. J. Neurobiol. 2004; 58: 164-174Crossref PubMed Scopus (83) Google Scholar, 12Karcher R.L. Deacon S.W. Gelfand V.I. Trends Cell Biol. 2002; 12: 21-27Abstract Full Text Full Text PDF PubMed Scopus (163) Google Scholar). Expression of truncated forms of various members of the myosin V family lacking the N-terminal motor domain but containing the globular tail domain leads to a dominant-negative phenotype in different cultured cell systems (11Rodriguez O.C. Cheney R.E. J. Cell Sci. 2002; 115: 991-1004Crossref PubMed Google Scholar, 13Hales C.M. Vaerman J.P. Goldenring J.R. J. Biol. Chem. 2002; 277: 50415-50421Abstract Full Text Full Text PDF PubMed Scopus Google Scholar, R. C.M. J. Provance Jr., D.W. Mercer J.A. Bahler M. Goldenring J.R. Biol. 12: PubMed Scopus Google Scholar, Goldenring J.R. J. Neurosci. 2002; PubMed Google Scholar, Goldenring J.R. J. A. Biol. 2004; PubMed Scopus Google Scholar, J.A. Cell PubMed Scopus Google Scholar). important of myosin Va in the of melanosome transport in Rao J. Cell Biol. PubMed Scopus Google Scholar). been used to the of myosin Vb in of several receptors in These the of receptors in cells Goldenring J.R. J. Neurosci. 2002; PubMed Google and receptors in and kidney cells (11Rodriguez O.C. Cheney R.E. J. Cell Sci. 2002; 115: 991-1004Crossref PubMed Google Scholar, 13Hales C.M. Vaerman J.P. Goldenring J.R. J. Biol. Chem. 2002; 277: 50415-50421Abstract Full Text Full Text PDF PubMed Scopus Google Scholar, R. C.M. J. Provance Jr., D.W. Mercer J.A. Bahler M. Goldenring J.R. Biol. 12: PubMed Scopus Google and the receptor in cells Goldenring J.R. J. A. Biol. 2004; PubMed Scopus Google Scholar). of the family of small have of transport by members of the myosin V family G.M. Traffic. 2002; 3: 859-865Crossref PubMed Scopus (177) Google Scholar, J.A. Cell Biol. 2002; PubMed Scopus Google Scholar, M.C. E. Traffic. 2004; 5: PubMed Scopus Google Scholar). In myosin Va associates with through interaction with a receptor containing and E. R. N. R. J.P. R. J. Cell Biol. PubMed Scopus Google Scholar, M. J. Biol. Chem. 2002; 277: Full Text Full Text PDF PubMed Scopus Google Scholar, D.W. Mercer J.A. Traffic. 2002; 3: PubMed Scopus Google Scholar, Rao M.B. Copeland N.G. Jenkins N.A. J.A. J. Cell Sci. PubMed Google Scholar, Rao J.R. Copeland N.G. Jenkins N.A. J.A. Nat. Cell Biol. 2002; PubMed Scopus Google Scholar). of myosin Vb with also been to regulate R. C.M. J. Provance Jr., D.W. Mercer J.A. Bahler M. Goldenring J.R. Biol. 12: PubMed Scopus Google Scholar). In contrast, the association of myosin Vc with is involved in trafficking in cells (11Rodriguez O.C. Cheney R.E. J. Cell Sci. 2002; 115: 991-1004Crossref PubMed Google Scholar). These observations that of members of the myosin V family to a of proteins may the of cargo transported by these these studies of the myosin the identity of cargo transported by these proteins in neurons remains unknown. unclear is various members of the myosin V family share for cargo to specific subcellular In we show that myosin Vb is widely in the brain and that it is expressed in several neuronal In brain myosin Vb associates with the α-amino-3-hydroxy-5-methyl-4-isoxazole glutamate receptor subunit GluR1. Expression of the tail region of myosin Vb reduced surface expression and clustering of GluR1. These observations with a in the frequency of excitatory currents. myosin V lacking required for to we that the effects of myosin Vb on GluR1 to Rab11. these results a novel for myosin Vb in trafficking of a specific subunit of the excitatory neurotransmitter receptors in and Vb expression in detected a protein of the coiled-coil region of myosin were with were for with Vb and the used for and a from mutant myosin Va by with of in The truncated of myosin Vb by with of myosin Vb The truncated of myosin Vb lacking the region by the at the of the myosin Vb tail mutant The of full-length myosin Vb to R. C.M. J. Provance Jr., D.W. Mercer J.A. Bahler M. Goldenring J.R. Biol. 12: PubMed Scopus Google Scholar). myosin Vb lacking the region by to the The of GluR1 and full-length Sci. 2000; PubMed Scopus Google Scholar, A.E. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). The were by Cell and neuronal were from the of were by were on were in with and J.R. J. Neurosci. PubMed Scopus Google Scholar). cells were in essential containing and and cells were cultured in containing and and were to the M. 2004; PubMed Scopus Google Scholar). were at days and and HEK cells, were to were at for in in for synaptic were with containing and after The were used and GluR1 and protein receptor by All were in containing for at at were at in containing the Molecular were on with GluR1 surface were region of GluR1 A. A. 2004; PubMed Scopus Google Scholar). and of neurons and cell used in were a to a and of and surface density the were in by A. Proc. Natl. Acad. Sci. U. S. A. 2004; PubMed Scopus Google Scholar). of cells of were fluorescent were sites of at the The in cells with cells in the changes in accumulation in neuronal and cells, a of cells from at of used to the were and from were in with and myosin Vb cells were in by the of GluR1 cells were in containing and for at by at for at were for at with of Vb proteins of coiled-coil region of myosin Vb and tail of the of of protein were at for were with containing were in with for and by were detected with A. A. 2004; PubMed Scopus Google Scholar) from cells were in containing and were subcellular from were and A. Neuroscience. 2004; PubMed Scopus Google Scholar). of on and small protein synaptic of miniature excitatory postsynaptic and miniature inhibitory postsynaptic were days neurons on were to a with containing and cells with were identified a fluorescent of and used for and by were for were in the at the for miniature postsynaptic to at the for glutamate miniature to and were by the glutamate receptor and the receptor not were at at and in a by Myosin Vb in the in studies that myosin Vb is in the brain; however, its exact subcellular unknown (10Zhao L.P. Koslovsky J.S. Reinhard J. Bahler M. Witt A.E. Provance Jr., D.W. Mercer J.A. Proc. Natl. Acad. Sci. U. S. A. 1996; 93: 10826-10831Crossref PubMed Scopus (76) Google Scholar). myosin Vb is expressed in neurons, we specific the coiled-coil domain of myosin Vb, the region conserved members of the myosin V family (2Bridgman P.C. J. Neurobiol. 2004; 58: 164-174Crossref PubMed Scopus (83) Google Scholar). that the the coiled-coil region of myosin Vb but not myosin Va of detected in from various brain of and Myosin Vb detected in neurons in the and in specific neuronal in the brain and and not myosin Vb also in the of the and neurons in In both neurons in brain and hippocampal neurons in myosin Vb a in the region and and Myosin Vb also in in the and not the subcellular of myosin Vb in neurons, we the localization of myosin Vb to the synaptic and at days in and in In neurons, myosin Vb in the soma and but lacking from synaptic sites and In myosin Vb observed in the However, at myosin Vb also detected in and at sites for and and The of myosin Vb in the region in both developing and neurons that myosin Vb in initial cargo transport from the soma to neuronal the localization of myosin Vb in in neurons that myosin Vb also of cargo delivery at the Expression of a of Myosin Vb the of is that the tail of myosin are for cargo transport (2Bridgman P.C. J. Neurobiol. 2004; 58: 164-174Crossref PubMed Scopus (83) Google Scholar, 12Karcher R.L. Deacon S.W. Gelfand V.I. Trends Cell Biol. 2002; 12: 21-27Abstract Full Text Full Text PDF PubMed Scopus (163) Google Scholar). forms the tail domain of myosin Va myosin Vb in a that with and cargo transport in cells C.M. Vaerman J.P. Goldenring J.R. J. Biol. Chem. 2002; 277: 50415-50421Abstract Full Text Full Text PDF PubMed Scopus Google Scholar, Goldenring J.R. J. Neurosci. 2002; PubMed Google Scholar, Rao J. Cell Biol. PubMed Scopus Google Scholar). their in neuronal protein we hippocampal neurons with containing the tail domain of myosin Va P.C. J. Cell Biol. PubMed Scopus Google Scholar) myosin Vb (10Zhao L.P. Koslovsky J.S. Reinhard J. Bahler M. Witt A.E. Provance Jr., D.W. Mercer J.A. Proc. Natl. Acad. Sci. U. S. A. 1996; 93: 10826-10831Crossref PubMed Scopus (76) Google Scholar). days neurons were and the of several neuronal proteins neurons but not a accumulation of the glutamate receptor subunit GluR1 In contrast, change in the accumulation of several other neurotransmitter receptors including the glutamate receptor and and the receptor and did not the of protein a specific of myosin Vb on GluR1 trafficking from a from the region and with the truncated of myosin Vb did not a of organelles the and endoplasmic (11Rodriguez O.C. Cheney R.E. J. Cell Sci. 2002; 115: 991-1004Crossref PubMed Google Scholar, R. C.M. J. Provance Jr., D.W. Mercer J.A. Bahler M. Goldenring J.R. Biol. 12: PubMed Scopus Google Scholar). the containing GluR1 and myosin Vb mutant did not with the with the that the accumulation of GluR1 with is not to of GluR1 in these GluR1 localization that myosin Vb in a protein containing GluR1. myosin Vb from brain and binding were for that GluR1 with myosin however, the protein detected myosin Vb also detected in GluR1 the myosin Vb and GluR1 in developing hippocampal neurons, we GluR1 localization in and neurons at synaptic and sites GluR1 at GluR1. the of myosin Vb in these In neurons, GluR1 accumulation at synaptic which myosin Vb at the However, at of both proteins were in the soma and the at sites. of from brain the of myosin Vb in the and that are enriched in GluR1 is with the of both myosin Vb and GluR1 in the of However, myosin Vb not to these but also enriched in the and subcellular the for myosin Va Valtschanoff Weinberg R. Sheng M. PubMed Scopus Google Scholar). These results suggest that in the myosin Vb in a containing GluR1 in both synaptic and sites. expression of effects on GluR1 localization in several expression systems including cells, cells, and the cell and not The of to GluR1 localization in these cell a of were with the C-terminal tail full-length myosin Vb to and GluR1 BERP, a known binding of myosin with myosin Vb A.E. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). However, GluR1 from myosin Vb These results that myosin Vb association with GluR1 may expressed in in the involved in sorting of GluR1 in cells and neurons may have contributed to the effects of mutant myosin Vb on GluR1. we enhanced accumulation of GluR1 in neurons mutant myosin Vb results in GluR1 trafficking sorting to the neurons were with truncated forms of myosin Va days neurons were with that the domain of and with a of the of GluR1 in cells with reduced of GluR1 on the surface of neurons In contrast, change in GluR1 surface localization observed in cells These results show that expression of the mutant of myosin Vb in neurons the delivery of GluR1 to the cell the of myosin Vb in receptor we also surface expression of GluR1 results in reduced clustering of GluR1 at the neurons were with full-length myosin Vb the truncated forms of myosin Va and were days and for GluR1 and the synaptic that expression of but not full-length myosin Vb results in a in the of GluR1 The of GluR1 clustering at sites for a in GluR1 accumulation at synapses Expression of however, did not clustering of the receptor subunit the effects on GluR1 clustering were specific to the expression of on the clustering of GluR1 and and the of the changes observed upon expression of mutant myosin Vb, neurons were with days of changes in the frequency of and postsynaptic were with the reduced clustering of expression of reduced frequency the The reduced frequency of excitatory but not inhibitory in the of excitatory synapses to the of Myosin Vb of a of studies that specific proteins regulate trafficking of receptor GluR1 and (1Kim E. Sheng M. Nat. Rev. Neurosci. 2004; 5: 771-781Crossref PubMed Scopus (1218) Google Scholar, 2003; Full Text Full Text PDF PubMed Scopus Google Scholar, S. J.A. R. Full Text Full Text PDF PubMed Scopus Google Scholar, A. Sheng M. 2004; Full Text Full Text PDF PubMed Scopus Google Scholar, M. Sheng M. Nat. Neurosci. PubMed Scopus Google Scholar). myosin Vb the localization of various receptor we hippocampal neurons with GluR1 and did not to the which contains and GluR1 The of of GluR1 in the region with In contrast, and with the of change in in the change in the of observed in neurons and not detected in myosin Vb from both and brain and These results are the of GluR1 are thought to that myosin Vb may regulate the transport of a specific of GluR1 containing Myosin on GluR1 to Recent studies in cells that myosin Vb associates with the protein and that protein is involved myosin cargo transport C.M. Vaerman J.P. Goldenring J.R. J. Biol. Chem. 2002; 277: 50415-50421Abstract Full Text Full Text PDF PubMed Scopus Google Scholar, R. C.M. J. Provance Jr., D.W. Mercer J.A. Bahler M. Goldenring J.R. Biol. 12: PubMed Scopus Google Scholar, Goldenring J.R. J. Neurosci. 2002; PubMed Google Scholar, C.M. R. M.C. R. J. Goldenring J.R. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, J. Proc. Natl. Acad. Sci. U. S. A. 2005; Scopus Google Scholar). In neurons, myosin Vb and show in in the soma and a mechanism for transport of GluR1 in neurons may of myosin Vb to Rab11. with expression of the tail region of myosin Vb in enhanced accumulation of in cells, cells, and in cultured neurons and and In contrast, change in the of including and the protein observed upon expression and and not the of in myosin cargo we of myosin Vb to is required for GluR1 we a mutant of the C-terminal globular tail but lacking which contains the region required for interaction with R. C.M. J. Provance Jr., D.W. Mercer J.A. Bahler M. Goldenring J.R. Biol. 12: PubMed Scopus Google Scholar). is to with actin with Rab11. In neurons, detected in the soma and and not to the of mutant did not the localization of expressed in cells in neurons in change in GluR1 clustering and also expression of the full-length of myosin Vb lacking the region required for interaction with R. C.M. J. Provance Jr., D.W. Mercer J.A. Bahler M. Goldenring J.R. Biol. 12: PubMed Scopus Google Scholar) with GluR1 trafficking R. C.M. J. Provance Jr., D.W. Mercer J.A. Bahler M. Goldenring J.R. Biol. 12: PubMed Scopus Google Scholar). mutant contains the actin binding motor it is to and actin however, it the binding a mutant may with cargo transport that of to myosin truncated of myosin Vb, mutant detected in both the soma and of neurons, and its localization not to the with a in both GluR1 clustering and surface expression and and and These results the that of myosin Vb to is involved in GluR1 to the of in we expressed a of in neurons and its on GluR1 and myosin Vb of in hippocampal neurons enhanced accumulation of GluR1 and myosin Vb that expression of results in a in surface expression of GluR1 that with of GluR1 in in the and its at the with that of receptors M. J.A. 2004; PubMed Scopus Google Scholar). the that both myosin Vb and in the of GluR1 In we have the of myosin V family members in the trafficking of a of neuronal a for myosin Vb in the trafficking of glutamate receptor subunit important for synaptic 2003; Full Text Full Text PDF PubMed Scopus Google Scholar, N. Acad. Sci. 2003; PubMed Scopus Google Scholar). we show that in neurons association with the protein Rab11. synaptic is by receptor a mechanism for the of synaptic mediated by a member of the myosin V family. that myosin Vb is in several neuronal populations in the In neurons, the of myosin Vb in the region that myosin Vb is involved in transport of cargo from a in the myosin Vb from synaptic sites in hippocampal neurons but in in neurons, that myosin Vb may also mediate cargo transport at synaptic sites at of neuronal The of myosin Vb at of neurons, sites myosin Va is also enriched (7Walikonis R.S. Jensen O.N. Mann M. Provance Jr., D.W. Mercer J.A. Kennedy M.B. J. Neurosci. 2000; 20: 4069-4080Crossref PubMed Google Scholar, S. S. M. Neurosci. 1996; PubMed Scopus Google that both motor proteins may of glutamate receptor trafficking at the studies implicated myosin Va in glutamate receptor Myosin Va associates with a containing dynein light chain and the scaffolding protein guanylate kinase domain-associated which associates with (8Naisbitt S. Valtschanoff J. Allison D.W. Sala C. Kim E. Craig A.M. Weinberg R.J. Sheng M. J. Neurosci. 2000; 20: 4524-4534Crossref PubMed Google Scholar, 9Kim E. Naisbitt S. Hsueh Y.P. Rao A. Rothschild A. Craig A.M. Sheng M. J. Cell Biol. 1997; 136: 669-678Crossref PubMed Scopus (429) Google Scholar). In of and through members of the family of proteins a for a protein containing myosin light kinase domain-associated in in glutamate receptor trafficking (1Kim E. Sheng M. Nat. Rev. Neurosci. 2004; 5: 771-781Crossref PubMed Scopus (1218) Google Scholar, R.S. R.J. Nature. 2000; PubMed Scopus Google Scholar). However, in we show that expression of a mutant of myosin Va not GluR1 of change in glutamate receptor clustering and localization been also in myosin Va mutant E. J. PubMed Scopus Google Scholar, R.S. N. J.A. R.J. J. Neurosci. PubMed Google Scholar). these that myosin Va may not essential for glutamate receptor The effects of myosin V on GluR1 trafficking is of the of receptor in cells by a mutant of myosin Vb but not myosin Va R. C.M. J. Provance Jr., D.W. Mercer J.A. Bahler M. Goldenring J.R. Biol. 12: PubMed Scopus Google Scholar). is that to specific various members of the the of cargo transported by these receptor are thought to and in the and to the for Cell Biol. 2004; PubMed Scopus Google Scholar). from is the of mutant myosin Vb on the clustering of the receptor subunit GluR1 but not from myosin Vb that myosin Vb a specific containing GluR1 but not of receptor from hippocampal neurons that of the receptor contains GluR1 R. R. A. J. Neurosci. 1996; PubMed Google Scholar). the of a of GluR1 in cultured hippocampal neurons M. 2005; Full Text Full Text PDF PubMed Scopus Google Scholar). However, that a small of GluR1 is in hippocampal neurons, it to a change in the localization of that changes in receptor localization days after expression of mutant forms of myosin Vb, may have for the observed accumulation of GluR1 in the region and its reduced surface expression. The of GluR1 from the cell surface is with is that myosin Vb from a neuronal containing GluR1. the a of GluR1. it is that we have myosin Vb from a specific neuronal containing of receptors is through interaction of different with a of proteins and members of the family of proteins (1Kim E. Sheng M. Nat. Rev. Neurosci. 2004; 5: 771-781Crossref PubMed Scopus (1218) Google Scholar, 2003; Full Text Full Text PDF PubMed Scopus Google Scholar, N. Acad. Sci. 2003; PubMed Scopus Google Scholar, M. J. Cell Biol. 2005; PubMed Scopus Google Scholar). it is that association with of these molecules may the effects of myosin Vb on specific of however, studies are These observations the of mechanism to transport In a of the protein and a member of the been implicated in the transport of receptors microtubules M. M. N. Nature. 2002; PubMed Scopus Google Scholar). is member of the family that been to regulate transport of a protein containing the subunit of receptor M. N. 2000; PubMed Scopus Google Scholar, M. N. J. Neurosci. 2003; PubMed Google Scholar). these it is that the trafficking of various of glutamate receptors from the soma to the In the it important to and receptor transport cargo myosin Vb and Myosin is unconventional myosin that is enriched at the and been implicated receptor trafficking E. J. Cell Biol. 2005; PubMed Scopus Google Scholar). myosin been to receptor studies are required to myosin and V family members in to regulate of of in suggest that of myosin Vb to is involved in GluR1 expression of a truncated of myosin Vb lacking the N-terminal motor domain but containing the globular tail domain with both and GluR1 However, of the C-terminal region that binding the effects of mutant on both and GluR1. results from expression of full-length myosin Vb lacking required for binding to mutant contains the actin binding motor and it is to and on actin the of mutant to with may with myosin cargo expression of mutant in a in GluR1 clustering and surface expression. expression of a of GluR1 and myosin Vb in the soma and surface expression of GluR1. However, it remains unclear myosin changes in GluR1 localization were to neuronal localization in both neuronal and is that GluR1 is to various populations of transport and that to in we were to in of both GluR1 and myosin Vb from brain these results suggest that interaction of myosin Vb with GluR1 is mediated by a protein through association with Rab11. The of GluR1 in myosin Vb from brain but not from expression to In neurons, proteins may which have been implicated in sorting of glutamate receptors (1Kim E. Sheng M. Nat. Rev. Neurosci. 2004; 5: 771-781Crossref PubMed Scopus (1218) Google Scholar, M. M. N. Nature. 2002; PubMed Scopus Google Scholar, R.J. S. N. R.S. Rev. 2003; PubMed Scopus Google Scholar, N. R.S. C. S. R.J. Nat. 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