메뉴 건너뛰기




Volumn 92, Issue 2, 2005, Pages 349-361

Direct interaction of myosin regulatory light chain with the NMDA receptor

Author keywords

Calmodulin; Cytoskeleton; E F hand; Excitatory synapse; Myosin II; Postsynaptic

Indexed keywords

ADAPTOR PROTEIN; BRAIN EXTRACT; CALMODULIN; CYTOSKELETON PROTEIN; MYOSIN HEAVY CHAIN; MYOSIN II; MYOSIN LIGHT CHAIN; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 1; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 2A; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 2B; POSTSYNAPTIC DENSITY PROTEIN 95; REGULATOR PROTEIN;

EID: 13244268511     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2004.02869.x     Document Type: Article
Times cited : (36)

References (54)
  • 1
    • 0018881743 scopus 로고
    • Regulation and kinetics of the actin-myosin-ATP interaction
    • Adelstein R. S. and Eisenberg E. (1980) Regulation and kinetics of the actin-myosin-ATP interaction. Annu. Rev. Biochem. 49, 921-956.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 921-956
    • Adelstein, R.S.1    Eisenberg, E.2
  • 2
    • 0033553412 scopus 로고    scopus 로고
    • Heterodimeric interactions between chicken ovalbumin upstream promoter-transcription factor family members ARP1 and ear2
    • Avram D., Ishmael J. E., Nevrivy D. J., Peterson V. J., Lee S. H., Dowell P. and Leid M. (1999) Heterodimeric interactions between chicken ovalbumin upstream promoter-transcription factor family members ARP1 and ear2. J. Biol. Chem. 274, 14 331-14 336.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14331-14336
    • Avram, D.1    Ishmael, J.E.2    Nevrivy, D.J.3    Peterson, V.J.4    Lee, S.H.5    Dowell, P.6    Leid, M.7
  • 3
    • 0033005168 scopus 로고    scopus 로고
    • Molecular mechanisms of nonmuscle myosin-II regulation
    • Bresnick A. R. (1999) Molecular mechanisms of nonmuscle myosin-II regulation. Curr. Opin. Cell Biol. 11, 26-33.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 26-33
    • Bresnick, A.R.1
  • 5
    • 0017257022 scopus 로고
    • Homology of myosin DTNB light chain with alkali light chains, troponin C and parvalbumin
    • Collins J. H. (1976) Homology of myosin DTNB light chain with alkali light chains, troponin C and parvalbumin. Nature 259, 699-700.
    • (1976) Nature , vol.259 , pp. 699-700
    • Collins, J.H.1
  • 6
    • 0037144811 scopus 로고    scopus 로고
    • Myosin Ic and myosin IIB serve opposing roles in lamellipodial dynamics of the neuronal growth cone
    • Diefenbach T. J., Latham V. M., Yimlamai D., Liu C. A., Herman I. M. and Jay D. G. (2002) Myosin Ic and myosin IIB serve opposing roles in lamellipodial dynamics of the neuronal growth cone. J. Cell Biol. 158, 1207-1217.
    • (2002) J. Cell Biol. , vol.158 , pp. 1207-1217
    • Diefenbach, T.J.1    Latham, V.M.2    Yimlamai, D.3    Liu, C.A.4    Herman, I.M.5    Jay, D.G.6
  • 7
    • 0031439111 scopus 로고    scopus 로고
    • p300 functions as a coactivator for the peroxisome proliferator-activated receptor alpha
    • Dowell P., Ishmael J. E., Avram D., Peterson V. J., Nevrivy D. J. and Leid M. (1997) p300 functions as a coactivator for the peroxisome proliferator-activated receptor alpha. J. Biol. Chem. 272, 33 435-33 443.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33435-33443
    • Dowell, P.1    Ishmael, J.E.2    Avram, D.3    Peterson, V.J.4    Nevrivy, D.J.5    Leid, M.6
  • 8
    • 0029991047 scopus 로고    scopus 로고
    • Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit
    • Ehlers M. D., Zhang S., Bernhadt J. P. and Huganir R. L. (1996) Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit. Cell 84, 745-755.
    • (1996) Cell , vol.84 , pp. 745-755
    • Ehlers, M.D.1    Zhang, S.2    Bernhadt, J.P.3    Huganir, R.L.4
  • 9
    • 0031972719 scopus 로고    scopus 로고
    • Splice variant-specific interaction of the NMDA receptor subunit NR1 with neuronal intermediate filaments
    • Ehlers M. D., Fung E. T., O'Brien R. J. and Huganir R. L. (1998) Splice variant-specific interaction of the NMDA receptor subunit NR1 with neuronal intermediate filaments. J. Neurosci. 18, 720-730.
    • (1998) J. Neurosci. , vol.18 , pp. 720-730
    • Ehlers, M.D.1    Fung, E.T.2    O'Brien, R.J.3    Huganir, R.L.4
  • 10
  • 11
    • 0026034052 scopus 로고
    • Expression of myosin regulatory light chains in rat brain: Characterization of a novel isoform
    • Feinstein D. L., Durand M. and Milner R. J. (1991) Expression of myosin regulatory light chains in rat brain: characterization of a novel isoform. Brain Res. Mol Brain Res. 10, 97-105.
    • (1991) Brain Res. Mol Brain Res. , vol.10 , pp. 97-105
    • Feinstein, D.L.1    Durand, M.2    Milner, R.J.3
  • 12
    • 0022083950 scopus 로고
    • A possible mechanism of morphometric changes in dendritic spines induced by stimulation
    • Fifkova E. (1985) A possible mechanism of morphometric changes in dendritic spines induced by stimulation. Cell. Mol. Neurobiol. 5, 47-63.
    • (1985) Cell. Mol. Neurobiol. , vol.5 , pp. 47-63
    • Fifkova, E.1
  • 13
    • 0024950039 scopus 로고
    • Calcium-regulated contractile and cytoskeletal proteins in dendritic spines may control synaptic plasticity
    • Fifkova E. and Morales M. (1989) Calcium-regulated contractile and cytoskeletal proteins in dendritic spines may control synaptic plasticity. Ann. N. Y. Acad. Sci. 568, 131-137.
    • (1989) Ann. N. Y. Acad. Sci. , vol.568 , pp. 131-137
    • Fifkova, E.1    Morales, M.2
  • 14
    • 0025130921 scopus 로고
    • Regulation of scallop myosin by mutant regulatory light chains
    • Goodwin E. B., Leinwand L. A. and Szent-Gyorgyi A. G. (1990) Regulation of scallop myosin by mutant regulatory light chains. J. Mol. Biol. 216, 85-93.
    • (1990) J. Mol. Biol. , vol.216 , pp. 85-93
    • Goodwin, E.B.1    Leinwand, L.A.2    Szent-Gyorgyi, A.G.3
  • 15
    • 0002329664 scopus 로고
    • Rat hippocampal neurons in low density culture
    • Banker G. and Goslin K., eds, MIT, Cambridge
    • Goslin K. and Banker G. (1992) Rat hippocampal neurons in low density culture, in Culturing Nerve Cells (Banker G. and Goslin K., eds), pp. 251-282. MIT, Cambridge.
    • (1992) Culturing Nerve Cells , pp. 251-282
    • Goslin, K.1    Banker, G.2
  • 16
    • 0028330166 scopus 로고
    • Dendritic spines: Cellular specializations imparting both stability and flexibility to synaptic function
    • Harris K. M. and Kater S. B. (1994) Dendritic spines: cellular specializations imparting both stability and flexibility to synaptic function. Annu. Rev. Neurosci. 17, 341-371.
    • (1994) Annu. Rev. Neurosci. , vol.17 , pp. 341-371
    • Harris, K.M.1    Kater, S.B.2
  • 18
    • 0035077318 scopus 로고    scopus 로고
    • Isolation of 2000-kDa complexes of N-methyl-D-aspartate receptor and postsynaptic density 95 from mouse brain
    • Husi H. and Grant S. G. (2001) Isolation of 2000-kDa complexes of N-methyl-D-aspartate receptor and postsynaptic density 95 from mouse brain. J. Neurochem. 77, 281-291.
    • (2001) J. Neurochem. , vol.77 , pp. 281-291
    • Husi, H.1    Grant, S.G.2
  • 19
  • 20
    • 0035895901 scopus 로고    scopus 로고
    • Dedicated myosin light chain kinases with diverse cellular functions
    • Kamm K. E. and Stull J. T. (2001) Dedicated myosin light chain kinases with diverse cellular functions. J. Biol. Chem. 276, 4527-4530.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4527-4530
    • Kamm, K.E.1    Stull, J.T.2
  • 21
    • 0026029783 scopus 로고
    • Chicken nonmuscle myosin heavy chains: Differential expression of two mRNAs and evidence for two different polypeptides
    • Kawamoto S. and Adelstein R. S. (1991) Chicken nonmuscle myosin heavy chains: differential expression of two mRNAs and evidence for two different polypeptides. J. Cell Biol. 112, 915-924.
    • (1991) J. Cell Biol. , vol.112 , pp. 915-924
    • Kawamoto, S.1    Adelstein, R.S.2
  • 22
    • 0032077680 scopus 로고    scopus 로고
    • Signal transduction molecules at the glutamatergic postsynaptic membrane
    • Kennedy M. B. (1998) Signal transduction molecules at the glutamatergic postsynaptic membrane. Brain Res. Brain Res. Rev. 26, 243-257.
    • (1998) Brain Res. Brain Res. Rev. , vol.26 , pp. 243-257
    • Kennedy, M.B.1
  • 23
    • 0033749378 scopus 로고    scopus 로고
    • Coevolution of head, neck, and tail domains of myosin heavy chains
    • Korn E. D. (2000) Coevolution of head, neck, and tail domains of myosin heavy chains. Proc. Natl Acad. Sci. USA 97, 12 559-12 564.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12559-12564
    • Korn, E.D.1
  • 24
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau H. C., Schenker L. T., Kennedy M. B. and Seeburg P. H. (1995) Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science 269, 1737-1740.
    • (1995) Science , vol.269 , pp. 1737-1740
    • Kornau, H.C.1    Schenker, L.T.2    Kennedy, M.B.3    Seeburg, P.H.4
  • 26
    • 0028912374 scopus 로고
    • A new version of the two-hybrid assay for detection of protein-protein interactions
    • Le Douarin B., Pierrat B., vom Baur E., Chambon P. and Losson R. (1995) A new version of the two-hybrid assay for detection of protein-protein interactions. Nucl. Acids Res. 23, 876-878.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 876-878
    • Le Douarin, B.1    Pierrat, B.2    Vom Baur, E.3    Chambon, P.4    Losson, R.5
  • 27
    • 0035503064 scopus 로고    scopus 로고
    • Regulation of NMDA receptor activity by F-actin and myosin light chain kinase
    • Lei S., Czerwinska E., Czerwinski W., Walsh M. P. and MacDonald J. F. (2001) Regulation of NMDA receptor activity by F-actin and myosin light chain kinase. J. Neurosci. 21, 8464-8472.
    • (2001) J. Neurosci. , vol.21 , pp. 8464-8472
    • Lei, S.1    Czerwinska, E.2    Czerwinski, W.3    Walsh, M.P.4    MacDonald, J.F.5
  • 28
    • 2242425422 scopus 로고    scopus 로고
    • Regulation of calcium/calmodulin-dependent protein kinase II docking to N-methyl-D-aspartate receptors by calcium/calmodulin and alpha-actinin
    • Leonard A. S., Bayer K. U., Merrill M. A., Lim I. A., Shea M. A., Schulman H. and Hell J. W. (2002) Regulation of calcium/calmodulin-dependent protein kinase II docking to N-methyl-D-aspartate receptors by calcium/calmodulin and alpha-actinin. J. Biol. Chem. 277, 48 441-48 448.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48441-48448
    • Leonard, A.S.1    Bayer, K.U.2    Merrill, M.A.3    Lim, I.A.4    Shea, M.A.5    Schulman, H.6    Hell, J.W.7
  • 29
    • 0029863153 scopus 로고    scopus 로고
    • Myosin drives retrograde F-actin flow in neuronal growth cones
    • Lin C. H., Espreafico E. M., Mooseker M. S. and Forscher P. (1996) Myosin drives retrograde F-actin flow in neuronal growth cones. Neuron 16, 769-782.
    • (1996) Neuron , vol.16 , pp. 769-782
    • Lin, C.H.1    Espreafico, E.M.2    Mooseker, M.S.3    Forscher, P.4
  • 30
    • 0032520827 scopus 로고    scopus 로고
    • Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1
    • Lin J. W., Wyszynski M., Madhavan R., Sealock R., Kim J. U. and Sheng M. (1998) Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1. J. Neurosci. 18, 2017-2027.
    • (1998) J. Neurosci. , vol.18 , pp. 2017-2027
    • Lin, J.W.1    Wyszynski, M.2    Madhavan, R.3    Sealock, R.4    Kim, J.U.5    Sheng, M.6
  • 31
    • 0036441201 scopus 로고    scopus 로고
    • Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity
    • Luo L. (2002) Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity. Annu. Rev. Cell Dev. Biol. 18, 601-635.
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 601-635
    • Luo, L.1
  • 32
    • 0032559349 scopus 로고    scopus 로고
    • Unconventional myosins in cell movement, membrane traffic, and signal transduction
    • Mermall V., Post P. L. and Mooseker M. S. (1998) Unconventional myosins in cell movement, membrane traffic, and signal transduction. Science 279, 527-533.
    • (1998) Science , vol.279 , pp. 527-533
    • Mermall, V.1    Post, P.L.2    Mooseker, M.S.3
  • 33
    • 0026557199 scopus 로고
    • Myosin II distribution in neurons is consistent with a role in growth cone motility but not synaptic vesicle mobilization
    • Miller M., Bower E., Levitt P., Li D. and Chantier P. D. (1992) Myosin II distribution in neurons is consistent with a role in growth cone motility but not synaptic vesicle mobilization. Neuron 8, 25-44.
    • (1992) Neuron , vol.8 , pp. 25-44
    • Miller, M.1    Bower, E.2    Levitt, P.3    Li, D.4    Chantier, P.D.5
  • 34
    • 0024557848 scopus 로고
    • In situ localization of myosin and actin in dendritic spines with the immunogold technique
    • Morales M. and Fifkova E. (1989) In situ localization of myosin and actin in dendritic spines with the immunogold technique. J. Comp. Neurol. 279, 666-674.
    • (1989) J. Comp. Neurol. , vol.279 , pp. 666-674
    • Morales, M.1    Fifkova, E.2
  • 35
    • 0032795907 scopus 로고    scopus 로고
    • Rundown of somatodendritic N-methyl-D-aspartate (NMDA) receptor channels in rat hippocampal neurones: Evidence for a role of the small GTPase RhoA
    • Norenberg W., Hofmann F., Illes P., Aktories K. and Meyer D. K. (1999) Rundown of somatodendritic N-methyl-D-aspartate (NMDA) receptor channels in rat hippocampal neurones: evidence for a role of the small GTPase RhoA. Br. J. Pharmacol. 127, 1060-1063.
    • (1999) Br. J. Pharmacol. , vol.127 , pp. 1060-1063
    • Norenberg, W.1    Hofmann, F.2    Illes, P.3    Aktories, K.4    Meyer, D.K.5
  • 36
    • 0029162555 scopus 로고
    • Cloning of the cDNA encoding human nonmuscle myosin heavy chain-B and analysis of human tissues with isoform-specific antibodies
    • Phillips C. L., Yamakawa K. and Adelstein R. S. (1995) Cloning of the cDNA encoding human nonmuscle myosin heavy chain-B and analysis of human tissues with isoform-specific antibodies. J. Muscle Res. Cell Motil. 16, 379-389.
    • (1995) J. Muscle Res. Cell Motil. , vol.16 , pp. 379-389
    • Phillips, C.L.1    Yamakawa, K.2    Adelstein, R.S.3
  • 37
    • 0030819659 scopus 로고    scopus 로고
    • Activity regulates the synaptic localization of the NMDA receptor in hippocampal neurons
    • Rao A. and Craig A. M. (1997) Activity regulates the synaptic localization of the NMDA receptor in hippocampal neurons. Neuron 19, 801-812.
    • (1997) Neuron , vol.19 , pp. 801-812
    • Rao, A.1    Craig, A.M.2
  • 40
    • 0029586312 scopus 로고
    • Localization of myosin II A and B isoforms in cultured neurons
    • Rochlin M. W., Itoh K., Adelstein R. S. and Bridgman P. C. (1995) Localization of myosin II A and B isoforms in cultured neurons. J. Cell Sci. 108, 3661-3670.
    • (1995) J. Cell Sci. , vol.108 , pp. 3661-3670
    • Rochlin, M.W.1    Itoh, K.2    Adelstein, R.S.3    Bridgman, P.C.4
  • 41
    • 0027258451 scopus 로고
    • Calcium-induced actin depolymerization reduces NMDA channel activity
    • Rosenmund C. and Westbrook G. L. (1993) Calcium-induced actin depolymerization reduces NMDA channel activity. Neuron 10, 805-814.
    • (1993) Neuron , vol.10 , pp. 805-814
    • Rosenmund, C.1    Westbrook, G.L.2
  • 42
    • 4143131141 scopus 로고    scopus 로고
    • Endocytosis and degradative sorting of NMDA receptors by conserved membrane-proximal signals
    • Scott D. B., Michailidis I., Mu Y., Logothetis D. and Ehlers M. D. (2004) Endocytosis and degradative sorting of NMDA receptors by conserved membrane-proximal signals. J. Neurosci. 24, 7096-7109.
    • (2004) J. Neurosci. , vol.24 , pp. 7096-7109
    • Scott, D.B.1    Michailidis, I.2    Mu, Y.3    Logothetis, D.4    Ehlers, M.D.5
  • 43
    • 0035413609 scopus 로고    scopus 로고
    • Structure and regulation of calcium/calmodulin-dependent protein kinases
    • Soderling T. R. and Stall J. T. (2001) Structure and regulation of calcium/calmodulin-dependent protein kinases. Chem. Rev. 101, 2341-2352.
    • (2001) Chem. Rev. , vol.101 , pp. 2341-2352
    • Soderling, T.R.1    Stall, J.T.2
  • 44
    • 0034650714 scopus 로고    scopus 로고
    • Signal transduction by G-proteins, rho-kinase and protein phosphatase to smooth muscle and non-muscle myosin II
    • Somlyo A. P. and Somlyo A. V. (2000) Signal transduction by G-proteins, rho-kinase and protein phosphatase to smooth muscle and non-muscle myosin II. J. Physiol. 522(Part 2), 177-185.
    • (2000) J. Physiol. , vol.522 , Issue.2 PART , pp. 177-185
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 45
    • 0032516819 scopus 로고    scopus 로고
    • Autophosphorylation-dependent targeting of calcium/calmodulin-dependent protein kinase II by the NR2B subunit of the N-methyl-D-aspartate receptor
    • Strack S. and Colbran R. J. (1998) Autophosphorylation-dependent targeting of calcium/calmodulin-dependent protein kinase II by the NR2B subunit of the N-methyl-D-aspartate receptor. J. Biol. Chem. 273, 20 689-20 692.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20689-20692
    • Strack, S.1    Colbran, R.J.2
  • 46
    • 0023279090 scopus 로고
    • Cloning and characterization of mammalian myosin regulatory light chain (RLC) cDNA: The RLC gene is expressed in smooth, sarcomeric, and nonmuscle tissues
    • Taubman M. B., Grant J. W. and Nadal-Ginard B. (1987) Cloning and characterization of mammalian myosin regulatory light chain (RLC) cDNA: the RLC gene is expressed in smooth, sarcomeric, and nonmuscle tissues. J. Cell Biol. 104, 1505-1513.
    • (1987) J. Cell Biol. , vol.104 , pp. 1505-1513
    • Taubman, M.B.1    Grant, J.W.2    Nadal-Ginard, B.3
  • 47
    • 0034986665 scopus 로고    scopus 로고
    • A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux
    • Vissel B., Krupp J. J., Heinemann S. F. and Westbrook G. L. (2001) A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux. Nat. Neurosci. 4, 587-596.
    • (2001) Nat. Neurosci. , vol.4 , pp. 587-596
    • Vissel, B.1    Krupp, J.J.2    Heinemann, S.F.3    Westbrook, G.L.4
  • 48
    • 0028506122 scopus 로고
    • The Merck Frosst Award Lecture 1994. Calmodulin: A versatile calcium mediator protein
    • Vogel H. J. (1994) The Merck Frosst Award Lecture 1994. Calmodulin: a versatile calcium mediator protein. Biochem. Cell Biol. 72, 357-376.
    • (1994) Biochem. Cell Biol. , vol.72 , pp. 357-376
    • Vogel, H.J.1
  • 50
    • 0032527719 scopus 로고    scopus 로고
    • Brain spectrin binding to the NMDA receptor is regulated by phosphorylation, calcium and calmodulin
    • Wechsler A. and Teichberg V. I. (1998) Brain spectrin binding to the NMDA receptor is regulated by phosphorylation, calcium and calmodulin. EMBO J. 17, 3931-3939.
    • (1998) EMBO J. , vol.17 , pp. 3931-3939
    • Wechsler, A.1    Teichberg, V.I.2
  • 53
    • 0031013896 scopus 로고    scopus 로고
    • Competitive binding of alpha-actinin and calmodulin to the NMDA receptor
    • Wyszynski M., Lin J., Rao A., Nigh E., Beggs A. H., Craig A. M. and Sheng M. (1997) Competitive binding of alpha-actinin and calmodulin to the NMDA receptor. Nature 385, 439-442.
    • (1997) Nature , vol.385 , pp. 439-442
    • Wyszynski, M.1    Lin, J.2    Rao, A.3    Nigh, E.4    Beggs, A.H.5    Craig, A.M.6    Sheng, M.7
  • 54
    • 0032142987 scopus 로고    scopus 로고
    • Calmodulin mediates calcium-dependent inactivation of N-methyl-D-aspartate receptors
    • Zhang S., Ehlers M. D., Bernhardt J. P., Su C. T. and Huganir R. L. (1998) Calmodulin mediates calcium-dependent inactivation of N-methyl-D-aspartate receptors. Neuron 21, 443-453.
    • (1998) Neuron , vol.21 , pp. 443-453
    • Zhang, S.1    Ehlers, M.D.2    Bernhardt, J.P.3    Su, C.T.4    Huganir, R.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.