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Volumn 1143, Issue 1, 2007, Pages 46-59

Nonmuscle myosins II-B and Va are components of detergent-resistant membrane skeletons derived from mouse forebrain

Author keywords

Actin cytoskeleton; Lipid raft; Myosin II; Myosin V; Postsynaptic density; Proteomics

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATE; ALPHA ACTININ 2; DETERGENT; GLUTAMATE RECEPTOR; MEMBRANE PROTEIN; MYOSIN IIB; MYOSIN VA; RECEPTOR SUBUNIT; REGULATOR PROTEIN; SPECTRIN; TRITON X 100; TUBULIN; UNCLASSIFIED DRUG;

EID: 33947312696     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.brainres.2007.01.061     Document Type: Article
Times cited : (15)

References (54)
  • 1
    • 0024346185 scopus 로고
    • Binding of myosin I to membrane lipids
    • Adams R.J., and Pollard T.D. Binding of myosin I to membrane lipids. Nature 340 (1989) 565-568
    • (1989) Nature , vol.340 , pp. 565-568
    • Adams, R.J.1    Pollard, T.D.2
  • 4
    • 0023804303 scopus 로고
    • Contributions of mass spectrometry to peptide and protein structure
    • Biemann K. Contributions of mass spectrometry to peptide and protein structure. Biomed. Environ. Mass Spectrom. 16 (1988) 99-111
    • (1988) Biomed. Environ. Mass Spectrom. , vol.16 , pp. 99-111
    • Biemann, K.1
  • 5
    • 0842269066 scopus 로고    scopus 로고
    • Myosin-dependent transport in neurons
    • Bridgman P.C. Myosin-dependent transport in neurons. J. Neurobiol. 58 (2004) 164-174
    • (2004) J. Neurobiol. , vol.58 , pp. 164-174
    • Bridgman, P.C.1
  • 6
    • 0019134836 scopus 로고
    • Isolation and characterization of postsynaptic densities from various brain regions: enrichment of different types of postsynaptic densities
    • Carlin R.K., Grab D.J., Cohen R.S., and Siekevitz P. Isolation and characterization of postsynaptic densities from various brain regions: enrichment of different types of postsynaptic densities. J. Cell Biol. 86 (1980) 831-845
    • (1980) J. Cell Biol. , vol.86 , pp. 831-845
    • Carlin, R.K.1    Grab, D.J.2    Cohen, R.S.3    Siekevitz, P.4
  • 8
    • 0026492629 scopus 로고
    • The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein
    • Cho K.O., Hunt C.A., and Kennedy M.B. The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein. Neuron 9 (1992) 929-942
    • (1992) Neuron , vol.9 , pp. 929-942
    • Cho, K.O.1    Hunt, C.A.2    Kennedy, M.B.3
  • 9
    • 22244473990 scopus 로고    scopus 로고
    • Detergent-resistant membranes in human erythrocytes and their connection to the membrane-skeleton
    • Ciana A., Balduini C., and Minetti G. Detergent-resistant membranes in human erythrocytes and their connection to the membrane-skeleton. J. Biosci. 30 (2005) 317-328
    • (2005) J. Biosci. , vol.30 , pp. 317-328
    • Ciana, A.1    Balduini, C.2    Minetti, G.3
  • 10
    • 33646823604 scopus 로고    scopus 로고
    • Molecular characterization and comparison of the components and multiprotein complexes in the postsynaptic proteome
    • Collins M.O., Husi H., Yu L., Brandon J.M., Anderson C.N., Blackstock W.P., Choudhary J.S., and Grant S.G. Molecular characterization and comparison of the components and multiprotein complexes in the postsynaptic proteome. J. Neurochem. 97 Suppl. 1 (2006) 16-23
    • (2006) J. Neurochem. , vol.97 , Issue.SUPPL. 1 , pp. 16-23
    • Collins, M.O.1    Husi, H.2    Yu, L.3    Brandon, J.M.4    Anderson, C.N.5    Blackstock, W.P.6    Choudhary, J.S.7    Grant, S.G.8
  • 11
    • 0033103971 scopus 로고    scopus 로고
    • Synaptic targeting of the postsynaptic density protein PSD-95 mediated by lipid and protein motifs
    • Craven S.E., El-Husseini A.E., and Bredt D.S. Synaptic targeting of the postsynaptic density protein PSD-95 mediated by lipid and protein motifs. Neuron 22 (1999) 497-509
    • (1999) Neuron , vol.22 , pp. 497-509
    • Craven, S.E.1    El-Husseini, A.E.2    Bredt, D.S.3
  • 12
    • 0033880909 scopus 로고    scopus 로고
    • Spectrin tethers and mesh in the biosynthetic pathway
    • De Matteis M.A., and Morrow J.S. Spectrin tethers and mesh in the biosynthetic pathway. J. Cell Sci. 113 Pt. 13 (2000) 2331-2343
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 13 , pp. 2331-2343
    • De Matteis, M.A.1    Morrow, J.S.2
  • 14
  • 15
    • 0030878573 scopus 로고    scopus 로고
    • Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains
    • Harder T., and Simons K. Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains. Curr. Opin. Cell Biol. 9 (1997) 534-542
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 534-542
    • Harder, T.1    Simons, K.2
  • 16
    • 0028330166 scopus 로고
    • Dendritic spines: cellular specializations imparting both stability and flexibility to synaptic function
    • Harris K.M., and Kater S.B. Dendritic spines: cellular specializations imparting both stability and flexibility to synaptic function. Annu. Rev. Neurosci. 17 (1994) 341-371
    • (1994) Annu. Rev. Neurosci. , vol.17 , pp. 341-371
    • Harris, K.M.1    Kater, S.B.2
  • 17
    • 0037996880 scopus 로고    scopus 로고
    • Lipid rafts in the maintenance of synapses, dendritic spines, and surface AMPA receptor stability
    • Hering H., Lin C.C., and Sheng M. Lipid rafts in the maintenance of synapses, dendritic spines, and surface AMPA receptor stability. J. Neurosci. 23 (2003) 3262-3271
    • (2003) J. Neurosci. , vol.23 , pp. 3262-3271
    • Hering, H.1    Lin, C.C.2    Sheng, M.3
  • 19
    • 0029858301 scopus 로고    scopus 로고
    • PIN: an associated protein inhibitor of neuronal nitric oxide synthase
    • Jaffrey S.R., and Snyder S.H. PIN: an associated protein inhibitor of neuronal nitric oxide synthase. Science 274 (1996) 774-777
    • (1996) Science , vol.274 , pp. 774-777
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 20
    • 0038006754 scopus 로고    scopus 로고
    • Nuclear interaction of the dynein light chain LC8a with the TRPS1 transcription factor suppresses the transcriptional repression activity of TRPS1
    • Kaiser F.J., Tavassoli K., Van den Bemd G.J., Chang G.T., Horsthemke B., Moroy T., and Ludecke H.J. Nuclear interaction of the dynein light chain LC8a with the TRPS1 transcription factor suppresses the transcriptional repression activity of TRPS1. Hum. Mol. Genet. 12 (2003) 1349-1358
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1349-1358
    • Kaiser, F.J.1    Tavassoli, K.2    Van den Bemd, G.J.3    Chang, G.T.4    Horsthemke, B.5    Moroy, T.6    Ludecke, H.J.7
  • 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. Chicken nonmuscle myosin heavy chains: differential expression of two mRNAs and evidence for two different polypeptides. J. Cell Biol. 112 (1991) 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. Signal transduction molecules at the glutamatergic postsynaptic membrane. Brain Res. Brain Res. Rev. 26 (1998) 243-257
    • (1998) Brain Res. Brain Res. Rev. , vol.26 , pp. 243-257
    • Kennedy, M.B.1
  • 23
    • 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. Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science 269 (1995) 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
  • 24
    • 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. Regulation of NMDA receptor activity by F-actin and myosin light chain kinase. J. Neurosci. 21 (2001) 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
  • 25
    • 0028049373 scopus 로고
    • Association of a cellular myosin II with anionic phospholipids and the neuronal plasma membrane
    • Li D., Miller M., and Chantler P.D. Association of a cellular myosin II with anionic phospholipids and the neuronal plasma membrane. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 853-857
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 853-857
    • Li, D.1    Miller, M.2    Chantler, P.D.3
  • 26
    • 5644297038 scopus 로고    scopus 로고
    • Lipid raft proteomics: analysis of in-solution digest of sodium dodecyl sulfate-solubilized lipid raft proteins by liquid chromatography-matrix-assisted laser desorption/ionization tandem mass spectrometry
    • Li N., Shaw A.R., Zhang N., Mak A., and Li L. Lipid raft proteomics: analysis of in-solution digest of sodium dodecyl sulfate-solubilized lipid raft proteins by liquid chromatography-matrix-assisted laser desorption/ionization tandem mass spectrometry. Proteomics 4 (2004) 3156-3166
    • (2004) Proteomics , vol.4 , pp. 3156-3166
    • Li, N.1    Shaw, A.R.2    Zhang, N.3    Mak, A.4    Li, L.5
  • 29
    • 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 Chantler P.D. Myosin II distribution in neurons is consistent with a role in growth cone motility but not synaptic vesicle mobilization. Neuron 8 (1992) 25-44
    • (1992) Neuron , vol.8 , pp. 25-44
    • Miller, M.1    Bower, E.2    Levitt, P.3    Li, D.4    Chantler, P.D.5
  • 30
    • 0024557848 scopus 로고
    • In situ localization of myosin and actin in dendritic spines with the immunogold technique
    • Morales M., and Fifkova E. In situ localization of myosin and actin in dendritic spines with the immunogold technique. J. Comp. Neurol. 279 (1989) 666-674
    • (1989) J. Comp. Neurol. , vol.279 , pp. 666-674
    • Morales, M.1    Fifkova, E.2
  • 31
    • 0028286263 scopus 로고
    • Direct binding of myosin II to phospholipid vesicles via tail regions and phosphorylation of the heavy chains by protein kinase C
    • Murakami N., Elzinga M., Singh S.S., and Chauhan V.P. Direct binding of myosin II to phospholipid vesicles via tail regions and phosphorylation of the heavy chains by protein kinase C. J. Biol. Chem. 269 (1994) 16082-16090
    • (1994) J. Biol. Chem. , vol.269 , pp. 16082-16090
    • Murakami, N.1    Elzinga, M.2    Singh, S.S.3    Chauhan, V.P.4
  • 32
    • 0028825025 scopus 로고
    • Phospholipid binding, phosphorylation by protein kinase C, and filament assembly of the COOH terminal heavy chain fragments of nonmuscle myosin II isoforms MIIA and MIIB
    • Murakami N., Singh S.S., Chauhan V.P., and Elzinga M. Phospholipid binding, phosphorylation by protein kinase C, and filament assembly of the COOH terminal heavy chain fragments of nonmuscle myosin II isoforms MIIA and MIIB. Biochemistry 34 (1995) 16046-16055
    • (1995) Biochemistry , vol.34 , pp. 16046-16055
    • Murakami, N.1    Singh, S.S.2    Chauhan, V.P.3    Elzinga, M.4
  • 33
    • 0030858386 scopus 로고    scopus 로고
    • Characterization of guanylate kinase-associated protein, a postsynaptic density protein at excitatory synapses that interacts directly with postsynaptic density-95/synapse-associated protein 90
    • Naisbitt S., Kim E., Weinberg R.J., Rao A., Yang F.C., Craig A.M., and Sheng M. Characterization of guanylate kinase-associated protein, a postsynaptic density protein at excitatory synapses that interacts directly with postsynaptic density-95/synapse-associated protein 90. J. Neurosci. 17 (1997) 5687-5696
    • (1997) J. Neurosci. , vol.17 , pp. 5687-5696
    • Naisbitt, S.1    Kim, E.2    Weinberg, R.J.3    Rao, A.4    Yang, F.C.5    Craig, A.M.6    Sheng, M.7
  • 34
    • 0034660288 scopus 로고    scopus 로고
    • Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein
    • Naisbitt S., Valtschanoff J., Allison D.W., Sala C., Kim E., Craig A.M., Weinberg R.J., and Sheng M. Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein. J. Neurosci. 20 (2000) 4524-4534
    • (2000) J. Neurosci. , vol.20 , pp. 4524-4534
    • Naisbitt, S.1    Valtschanoff, J.2    Allison, D.W.3    Sala, C.4    Kim, E.5    Craig, A.M.6    Weinberg, R.J.7    Sheng, M.8
  • 35
    • 0037044851 scopus 로고    scopus 로고
    • Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes
    • Nebl T., Pestonjamasp K.N., Leszyk J.D., Crowley J.L., Oh S.W., and Luna E.J. Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes. J. Biol. Chem. 277 (2002) 43399-43409
    • (2002) J. Biol. Chem. , vol.277 , pp. 43399-43409
    • Nebl, T.1    Pestonjamasp, K.N.2    Leszyk, J.D.3    Crowley, J.L.4    Oh, S.W.5    Luna, E.J.6
  • 36
    • 0035015910 scopus 로고    scopus 로고
    • Glutamate receptor targeting in the postsynaptic spine involves mechanisms that are independent of myosin Va
    • Petralia R.S., Wang Y.X., Sans N., Worley P.F., Hammer III J.A., and Wenthold R.J. Glutamate receptor targeting in the postsynaptic spine involves mechanisms that are independent of myosin Va. Eur. J. Neurosci. 13 (2001) 1722-1732
    • (2001) Eur. J. Neurosci. , vol.13 , pp. 1722-1732
    • Petralia, R.S.1    Wang, Y.X.2    Sans, N.3    Worley, P.F.4    Hammer III, J.A.5    Wenthold, R.J.6
  • 37
    • 1642354334 scopus 로고    scopus 로고
    • Lipid rafts: heterogeneity on the high seas
    • Pike L.J. Lipid rafts: heterogeneity on the high seas. Biochem. J. 378 (2004) 281-292
    • (2004) Biochem. J. , vol.378 , pp. 281-292
    • Pike, L.J.1
  • 38
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • Puthalakath H., Huang D.C., O'Reilly L.A., King S.M., and Strasser A. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol. Cell 3 (1999) 287-296
    • (1999) Mol. Cell , vol.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 39
    • 4344717226 scopus 로고    scopus 로고
    • Lateral organization of endocytic machinery in dendritic spines
    • Racz B., Blanpied T.A., Ehlers M.D., and Weinberg R.J. Lateral organization of endocytic machinery in dendritic spines. Nat. Neurosci. 7 (2004) 917-918
    • (2004) Nat. Neurosci. , vol.7 , pp. 917-918
    • Racz, B.1    Blanpied, T.A.2    Ehlers, M.D.3    Weinberg, R.J.4
  • 40
    • 0035879095 scopus 로고    scopus 로고
    • Glycolipid-enriched membrane domains are assembled into membrane patches by associating with the actin cytoskeleton
    • Rodgers W., and Zavzavadjian J. Glycolipid-enriched membrane domains are assembled into membrane patches by associating with the actin cytoskeleton. Exp. Cell Res. 267 (2001) 173-183
    • (2001) Exp. Cell Res. , vol.267 , pp. 173-183
    • Rodgers, W.1    Zavzavadjian, J.2
  • 41
    • 30644456796 scopus 로고    scopus 로고
    • A critical role for Myosin IIb in dendritic spine morphology and synaptic function
    • Ryu J., Liu L., Wong T.P., Wu D.C., Burette A., Weinberg R., Wang Y.T., and Sheng M. A critical role for Myosin IIb in dendritic spine morphology and synaptic function. Neuron 49 (2006) 175-182
    • (2006) Neuron , vol.49 , pp. 175-182
    • Ryu, J.1    Liu, L.2    Wong, T.P.3    Wu, D.C.4    Burette, A.5    Weinberg, R.6    Wang, Y.T.7    Sheng, M.8
  • 42
    • 0035071224 scopus 로고    scopus 로고
    • Hippocampal synaptic transmission and plasticity are preserved in myosin Va mutant mice
    • Schnell E., and Nicoll R.A. Hippocampal synaptic transmission and plasticity are preserved in myosin Va mutant mice. J. Neurophysiol. 85 (2001) 1498-1501
    • (2001) J. Neurophysiol. , vol.85 , pp. 1498-1501
    • Schnell, E.1    Nicoll, R.A.2
  • 43
    • 0033787039 scopus 로고    scopus 로고
    • The molecular motor dynein is involved in targeting swallow and bicoid RNA to the anterior pole of Drosophila oocytes
    • Schnorrer F., Bohmann K., and Nusslein-Volhard C. The molecular motor dynein is involved in targeting swallow and bicoid RNA to the anterior pole of Drosophila oocytes. Nat. Cell Biol. 2 (2000) 185-190
    • (2000) Nat. Cell Biol. , vol.2 , pp. 185-190
    • Schnorrer, F.1    Bohmann, K.2    Nusslein-Volhard, C.3
  • 44
    • 0034677906 scopus 로고    scopus 로고
    • Myosins: a diverse superfamily
    • Sellers J.R. Myosins: a diverse superfamily. Biochim. Biophys. Acta 1496 (2000) 3-22
    • (2000) Biochim. Biophys. Acta , vol.1496 , pp. 3-22
    • Sellers, J.R.1
  • 45
    • 0343192494 scopus 로고    scopus 로고
    • Growth of the NMDA receptor industrial complex
    • Sheng M., and Lee S.H. Growth of the NMDA receptor industrial complex. Nat. Neurosci. 3 (2000) 633-635
    • (2000) Nat. Neurosci. , vol.3 , pp. 633-635
    • Sheng, M.1    Lee, S.H.2
  • 46
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • Sheng M., and Sala C. PDZ domains and the organization of supramolecular complexes. Annu. Rev. Neurosci. 24 (2001) 1-29
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 47
    • 0033756376 scopus 로고    scopus 로고
    • Overview on the structure, composition, function, development, and plasticity of hippocampal dendritic spines
    • Sorra K.E., and Harris K.M. Overview on the structure, composition, function, development, and plasticity of hippocampal dendritic spines. Hippocampus 10 (2000) 501-511
    • (2000) Hippocampus , vol.10 , pp. 501-511
    • Sorra, K.E.1    Harris, K.M.2
  • 49
    • 0242677759 scopus 로고    scopus 로고
    • Myosin V motor proteins: marching stepwise towards a mechanism
    • Vale R.D. Myosin V motor proteins: marching stepwise towards a mechanism. J. Cell Biol. 163 (2003) 445-450
    • (2003) J. Cell Biol. , vol.163 , pp. 445-450
    • Vale, R.D.1
  • 51
    • 0035865546 scopus 로고    scopus 로고
    • Laminar organization of the NMDA receptor complex within the postsynaptic density
    • Valtschanoff J.G., and Weinberg R.J. Laminar organization of the NMDA receptor complex within the postsynaptic density. J. Neurosci. 21 (2001) 1211-1217
    • (2001) J. Neurosci. , vol.21 , pp. 1211-1217
    • Valtschanoff, J.G.1    Weinberg, R.J.2
  • 53
    • 0034303806 scopus 로고    scopus 로고
    • Walking on two heads: the many talents of kinesin
    • Woehlke G., and Schliwa M. Walking on two heads: the many talents of kinesin. Nat. Rev., Mol. Cell Biol. 1 (2000) 50-58
    • (2000) Nat. Rev., Mol. Cell Biol. , vol.1 , pp. 50-58
    • Woehlke, G.1    Schliwa, M.2
  • 54
    • 18544393408 scopus 로고    scopus 로고
    • Homer regulates the association of group 1 metabotropic glutamate receptors with multivalent complexes of homer-related, synaptic proteins
    • Xiao B., Tu J.C., Petralia R.S., Yuan J.P., Doan A., Breder C.D., Ruggiero A., Lanahan A.A., Wenthold R.J., and Worley P.F. Homer regulates the association of group 1 metabotropic glutamate receptors with multivalent complexes of homer-related, synaptic proteins. Neuron 21 (1998) 707-716
    • (1998) Neuron , vol.21 , pp. 707-716
    • Xiao, B.1    Tu, J.C.2    Petralia, R.S.3    Yuan, J.P.4    Doan, A.5    Breder, C.D.6    Ruggiero, A.7    Lanahan, A.A.8    Wenthold, R.J.9    Worley, P.F.10


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