메뉴 건너뛰기




Volumn 116, Issue 2, 2011, Pages 177-191

The role of myosin v in exocytosis and synaptic plasticity

Author keywords

amino 3 hydroxy 5 methylisoxazole 4 propionate receptor; acetylcholine receptor; large dense core vesicle; long term potentiation; myosin V; secretory granule; synaptic plasticity

Indexed keywords

AMPA RECEPTOR; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALCIUM ION; CALPAIN; MYOSIN V; NEUROPEPTIDE; NICOTINIC RECEPTOR;

EID: 78650709124     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2010.07110.x     Document Type: Review
Times cited : (66)

References (141)
  • 4
    • 0027208145 scopus 로고
    • Induction of LTP in the hippocampus needs synaptic activation of glutamate metabotropic receptors
    • Bashir Z. I., Bortolotto Z. A., Davies C. H., et al. (1993) Induction of LTP in the hippocampus needs synaptic activation of glutamate metabotropic receptors. Nature 363, 347-350.
    • (1993) Nature , vol.363 , pp. 347-350
    • Bashir, Z.I.1    Bortolotto, Z.A.2    Davies, C.H.3
  • 5
    • 67449168385 scopus 로고    scopus 로고
    • Expression of the dominant-negative tail of myosin Va enhances exocytosis of large dense core vesicles in neurons
    • Bittins C. M., Eichler T. W., and, Gerdes H. H., (2009) Expression of the dominant-negative tail of myosin Va enhances exocytosis of large dense core vesicles in neurons. Cell. Mol. Neurobiol. 29, 597-608.
    • (2009) Cell. Mol. Neurobiol. , vol.29 , pp. 597-608
    • Bittins, C.M.1    Eichler, T.W.2    Gerdes, H.H.3
  • 6
    • 77952097761 scopus 로고    scopus 로고
    • Dominant-negative myosin Va impairs retrograde but not anterograde axonal transport of large dense core vesicles
    • Bittins C. M., Eichler T. W., Hammer J. A. 3rd, and, Gerdes H. H., (2010) Dominant-negative myosin Va impairs retrograde but not anterograde axonal transport of large dense core vesicles. Cell. Mol. Neurobiol. 30, 369-379.
    • (2010) Cell. Mol. Neurobiol. , vol.30 , pp. 369-379
    • Bittins, C.M.1    Eichler, T.W.2    Hammer III, J.A.3    Gerdes, H.H.4
  • 7
    • 56549084442 scopus 로고    scopus 로고
    • Local protein synthesis, actin dynamics, and LTP consolidation
    • Bramham C. R., (2008) Local protein synthesis, actin dynamics, and LTP consolidation. Curr. Opin. Neurobiol. 18, 524-531.
    • (2008) Curr. Opin. Neurobiol. , vol.18 , pp. 524-531
    • Bramham, C.R.1
  • 8
    • 24144483438 scopus 로고    scopus 로고
    • BDNF function in adult synaptic plasticity: The synaptic consolidation hypothesis
    • Bramham C. R., and, Messaoudi E., (2005) BDNF function in adult synaptic plasticity: the synaptic consolidation hypothesis. Prog. Neurobiol. 76, 99-125.
    • (2005) Prog. Neurobiol. , vol.76 , pp. 99-125
    • Bramham, C.R.1    Messaoudi, E.2
  • 9
    • 0141918783 scopus 로고    scopus 로고
    • AMPA receptor trafficking at excitatory synapses
    • Bredt D. S., and, Nicoll R. A., (2003) AMPA receptor trafficking at excitatory synapses. Neuron 40, 361-379.
    • (2003) Neuron , vol.40 , pp. 361-379
    • Bredt, D.S.1    Nicoll, R.A.2
  • 10
    • 0032872611 scopus 로고    scopus 로고
    • Myosin Va movements in normal and dilute-lethal axons provide support for a dual filament motor complex
    • Bridgman P. C., (1999) Myosin Va movements in normal and dilute-lethal axons provide support for a dual filament motor complex. J. Cell Biol. 146, 1045-1060.
    • (1999) J. Cell Biol. , vol.146 , pp. 1045-1060
    • Bridgman, P.C.1
  • 11
    • 23844463751 scopus 로고    scopus 로고
    • Differential vesicular targeting and time course of synaptic secretion of the mammalian neurotrophins
    • Brigadski T., Hartmann M., and, Lessmann V., (2005) Differential vesicular targeting and time course of synaptic secretion of the mammalian neurotrophins. J. Neurosci. 25, 7601-7614.
    • (2005) J. Neurosci. , vol.25 , pp. 7601-7614
    • Brigadski, T.1    Hartmann, M.2    Lessmann, V.3
  • 12
  • 13
    • 0842290746 scopus 로고    scopus 로고
    • Short-range axonal/dendritic transport by myosin-V: A model for vesicle delivery to the synapse
    • Brown J. R., Stafford P., and, Langford G. M., (2004) Short-range axonal/dendritic transport by myosin-V: a model for vesicle delivery to the synapse. J. Neurobiol. 58, 175-188.
    • (2004) J. Neurobiol. , vol.58 , pp. 175-188
    • Brown, J.R.1    Stafford, P.2    Langford, G.M.3
  • 14
    • 0037378045 scopus 로고    scopus 로고
    • Secretory granule exocytosis
    • Burgoyne R. D., and, Morgan A., (2003) Secretory granule exocytosis. Physiol. Rev. 83, 581-632.
    • (2003) Physiol. Rev. , vol.83 , pp. 581-632
    • Burgoyne, R.D.1    Morgan, A.2
  • 15
  • 16
    • 0025013459 scopus 로고
    • Development of hippocampal long-term potentiation is reduced by recently introduced calpain inhibitors
    • del Cerro S., Larson J., Oliver M. W., and, Lynch G., (1990) Development of hippocampal long-term potentiation is reduced by recently introduced calpain inhibitors. Brain Res. 530, 91-95.
    • (1990) Brain Res. , vol.530 , pp. 91-95
    • Del Cerro, S.1    Larson, J.2    Oliver, M.W.3    Lynch, G.4
  • 17
    • 33644693055 scopus 로고    scopus 로고
    • Organellar proteomics: Analysis of pancreatic zymogen granule membranes
    • Chen X., Walker A. K., Strahler J. R., et al. (2006) Organellar proteomics: analysis of pancreatic zymogen granule membranes. Mol. Cell Proteomics 5, 306-312.
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 306-312
    • Chen, X.1    Walker, A.K.2    Strahler, J.R.3
  • 18
    • 0027588878 scopus 로고
    • Ca(2+)-dependent phosphorylation of the tail domain of myosin-V, a calmodulin-binding myosin in vertebrate brain
    • Coelho M. V., and, Larson R. E., (1993) Ca(2+)-dependent phosphorylation of the tail domain of myosin-V, a calmodulin-binding myosin in vertebrate brain. Braz. J. Med. Biol. Res. 26, 465-472.
    • (1993) Braz. J. Med. Biol. Res. , vol.26 , pp. 465-472
    • Coelho, M.V.1    Larson, R.E.2
  • 19
    • 2942607447 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II and synaptic plasticity
    • Colbran R. J., and, Brown A. M., (2004) Calcium/calmodulin-dependent protein kinase II and synaptic plasticity. Curr. Opin. Neurobiol. 14, 318-327.
    • (2004) Curr. Opin. Neurobiol. , vol.14 , pp. 318-327
    • Colbran, R.J.1    Brown, A.M.2
  • 21
    • 0032985891 scopus 로고    scopus 로고
    • Brain myosin-V, a calmodulin-carrying myosin, binds to calmodulin-dependent protein kinase II and activates its kinase activity
    • Costa M. C., Mani F., Santoro W. Jr, Espreafico E. M., and, Larson R. E., (1999) Brain myosin-V, a calmodulin-carrying myosin, binds to calmodulin-dependent protein kinase II and activates its kinase activity. J. Biol. Chem. 274, 15811-15819.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15811-15819
    • Costa, M.C.1    Mani, F.2    Santoro, Jr.W.3    Espreafico, E.M.4    Larson, R.E.5
  • 22
    • 35648983506 scopus 로고    scopus 로고
    • Increased motion and travel, rather than stable docking, characterize the last moments before secretory granule fusion
    • Degtyar V. E., Allersma M. W., Axelrod D., and, Holz R. W., (2007) Increased motion and travel, rather than stable docking, characterize the last moments before secretory granule fusion. Proc. Natl Acad. Sci. USA 104, 15929-15934.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 15929-15934
    • Degtyar, V.E.1    Allersma, M.W.2    Axelrod, D.3    Holz, R.W.4
  • 25
    • 10744220744 scopus 로고    scopus 로고
    • Rab27A and its effector MyRIP link secretory granules to F-actin and control their motion towards release sites
    • Desnos C., Schonn J. S., Huet S., et al. (2003) Rab27A and its effector MyRIP link secretory granules to F-actin and control their motion towards release sites. J. Cell Biol. 163, 559-570.
    • (2003) J. Cell Biol. , vol.163 , pp. 559-570
    • Desnos, C.1    Schonn, J.S.2    Huet, S.3
  • 26
    • 34547986066 scopus 로고    scopus 로고
    • 'Should i stay or should i go?': Myosin v function in organelle trafficking
    • Desnos C., Huet S., and, Darchen F., (2007a) 'Should I stay or should I go?': myosin V function in organelle trafficking. Biol. Cell 99, 411-423.
    • (2007) Biol. Cell , vol.99 , pp. 411-423
    • Desnos, C.1    Huet, S.2    Darchen, F.3
  • 30
    • 0041659182 scopus 로고    scopus 로고
    • Actin remodeling to facilitate membrane fusion
    • Eitzen G., (2003) Actin remodeling to facilitate membrane fusion. Biochim. Biophys. Acta 1641, 175-181.
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 175-181
    • Eitzen, G.1
  • 32
    • 0004184280 scopus 로고    scopus 로고
    • McGraw-Hill, New York, Chicago, San Francisco.
    • Engel A. G., and, Franzini-Armstrong C., (2004) Myology. McGraw-Hill, New York, Chicago, San Francisco.
    • (2004) Myology
    • Engel, A.G.1    Franzini-Armstrong, C.2
  • 34
    • 0026642525 scopus 로고
    • Biochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: A novel calmodulin-binding myosin
    • Espindola F. S., Espreafico E. M., Coelho M. V., Martins A. R., Costa F. R., Mooseker M. S., and, Larson R. E., (1992) Biochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: a novel calmodulin-binding myosin. J. Cell Biol. 118, 359-368.
    • (1992) J. Cell Biol. , vol.118 , pp. 359-368
    • Espindola, F.S.1    Espreafico, E.M.2    Coelho, M.V.3    Martins, A.R.4    Costa, F.R.5    Mooseker, M.S.6    Larson, R.E.7
  • 35
    • 0027068050 scopus 로고
    • Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains
    • Espreafico E. M., Cheney R. E., Matteoli M., Nascimento A. A., De Camilli P. V., Larson R. E., and, Mooseker M. S., (1992) Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains. J. Cell Biol. 119, 1541-1557.
    • (1992) J. Cell Biol. , vol.119 , pp. 1541-1557
    • Espreafico, E.M.1    Cheney, R.E.2    Matteoli, M.3    Nascimento, A.A.4    De Camilli, P.V.5    Larson, R.E.6    Mooseker, M.S.7
  • 36
    • 2342570318 scopus 로고    scopus 로고
    • Rab11-family interacting protein 2 and myosin Vb are required for CXCR2 recycling and receptor-mediated chemotaxis
    • Fan G. H., Lapierre L. A., Goldenring J. R., Sai J., and, Richmond A., (2004) Rab11-family interacting protein 2 and myosin Vb are required for CXCR2 recycling and receptor-mediated chemotaxis. Mol. Biol. Cell 15, 2456-2469.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2456-2469
    • Fan, G.H.1    Lapierre, L.A.2    Goldenring, J.R.3    Sai, J.4    Richmond, A.5
  • 37
    • 39549119763 scopus 로고    scopus 로고
    • Activity-induced synaptic capture and exocytosis of the neuronal serine protease neurotrypsin
    • Frischknecht R., Fejtova A., Viesti M., Stephan A., and, Sonderegger P., (2008) Activity-induced synaptic capture and exocytosis of the neuronal serine protease neurotrypsin. J. Neurosci. 28, 1568-1579.
    • (2008) J. Neurosci. , vol.28 , pp. 1568-1579
    • Frischknecht, R.1    Fejtova, A.2    Viesti, M.3    Stephan, A.4    Sonderegger, P.5
  • 39
    • 73349135323 scopus 로고    scopus 로고
    • BDNF signaling in the formation, maturation and plasticity of glutamatergic and GABAergic synapses
    • Gottmann K., Mittmann T., and, Lessmann V., (2009) BDNF signaling in the formation, maturation and plasticity of glutamatergic and GABAergic synapses. Exp. Brain Res. 199, 203-234.
    • (2009) Exp. Brain Res. , vol.199 , pp. 203-234
    • Gottmann, K.1    Mittmann, T.2    Lessmann, V.3
  • 41
    • 0037184989 scopus 로고    scopus 로고
    • Rab11 family interacting protein 2 associates with Myosin Vb and regulates plasma membrane recycling
    • Hales C. M., Vaerman J. P., and, Goldenring J. R., (2002) Rab11 family interacting protein 2 associates with Myosin Vb and regulates plasma membrane recycling. J. Biol. Chem. 277, 50415-50421.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50415-50421
    • Hales, C.M.1    Vaerman, J.P.2    Goldenring, J.R.3
  • 42
    • 0033680967 scopus 로고    scopus 로고
    • Long-term depression of the cerebellar climbing fiber - Purkinje neuron synapse
    • Hansel C., and, Linden D. J., (2000) Long-term depression of the cerebellar climbing fiber - Purkinje neuron synapse. Neuron 26, 473-482.
    • (2000) Neuron , vol.26 , pp. 473-482
    • Hansel, C.1    Linden, D.J.2
  • 43
    • 0031864392 scopus 로고    scopus 로고
    • BDNF-GFP containing secretory granules are localized in the vicinity of synaptic junctions of cultured cortical neurons
    • Haubensak W., Narz F., Heumann R., and, Lessmann V., (1998) BDNF-GFP containing secretory granules are localized in the vicinity of synaptic junctions of cultured cortical neurons. J. Cell Sci. 111 (Pt 11), 1483-1493.
    • (1998) J. Cell Sci. , vol.111 , Issue.PART 11 , pp. 1483-1493
    • Haubensak, W.1    Narz, F.2    Heumann, R.3    Lessmann, V.4
  • 44
    • 58149474389 scopus 로고    scopus 로고
    • Endosomal trafficking of AMPA-type glutamate receptors
    • Hirling H., (2009) Endosomal trafficking of AMPA-type glutamate receptors. Neuroscience 158, 36-44.
    • (2009) Neuroscience , vol.158 , pp. 36-44
    • Hirling, H.1
  • 45
    • 0024603065 scopus 로고
    • MgATP-independent and MgATP-dependent exocytosis. Evidence that MgATP primes adrenal chromaffin cells to undergo exocytosis
    • Holz R. W., Bittner M. A., Peppers S. C., Senter R. A., and, Eberhard D. A., (1989) MgATP-independent and MgATP-dependent exocytosis. Evidence that MgATP primes adrenal chromaffin cells to undergo exocytosis. J. Biol. Chem. 264, 5412-5419.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5412-5419
    • Holz, R.W.1    Bittner, M.A.2    Peppers, S.C.3    Senter, R.A.4    Eberhard, D.A.5
  • 47
    • 26944465715 scopus 로고    scopus 로고
    • Myosin 5a controls insulin granule recruitment during late-phase secretion
    • Ivarsson R., Jing X., Waselle L., Regazzi R., and, Renstrom E., (2005) Myosin 5a controls insulin granule recruitment during late-phase secretion. Traffic 6, 1027-1035.
    • (2005) Traffic , vol.6 , pp. 1027-1035
    • Ivarsson, R.1    Jing, X.2    Waselle, L.3    Regazzi, R.4    Renstrom, E.5
  • 48
    • 73949084166 scopus 로고    scopus 로고
    • Myosin Vc is a molecular motor that functions in secretory granule trafficking
    • Jacobs D. T., Weigert R., Grode K. D., Donaldson J. G., and, Cheney R. E., (2009) Myosin Vc is a molecular motor that functions in secretory granule trafficking. Mol. Biol. Cell 20, 4471-4488.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4471-4488
    • Jacobs, D.T.1    Weigert, R.2    Grode, K.D.3    Donaldson, J.G.4    Cheney, R.E.5
  • 49
    • 0019861021 scopus 로고
    • Dilute (d) coat colour mutation of DBA/2J mice is associated with the site of integration of an ecotropic MuLV genome
    • Jenkins N. A., Copeland N. G., Taylor B. A., and, Lee B. K., (1981) Dilute (d) coat colour mutation of DBA/2J mice is associated with the site of integration of an ecotropic MuLV genome. Nature 293, 370-374.
    • (1981) Nature , vol.293 , pp. 370-374
    • Jenkins, N.A.1    Copeland, N.G.2    Taylor, B.A.3    Lee, B.K.4
  • 51
    • 0032550222 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors are sorted from immature secretory granules via adaptor protein AP-1, clathrin, and syntaxin 6-positive vesicles
    • Klumperman J., Kuliawat R., Griffith J. M., Geuze H. J., and, Arvan P., (1998) Mannose 6-phosphate receptors are sorted from immature secretory granules via adaptor protein AP-1, clathrin, and syntaxin 6-positive vesicles. J. Cell Biol. 141, 359-371.
    • (1998) J. Cell Biol. , vol.141 , pp. 359-371
    • Klumperman, J.1    Kuliawat, R.2    Griffith, J.M.3    Geuze, H.J.4    Arvan, P.5
  • 52
    • 76449102375 scopus 로고    scopus 로고
    • Versatile roles for myosin Va in dense core vesicle biogenesis and function
    • Kögel T., Bittins C. M., Rudolf R., and, Gerdes H. H., (2010a) Versatile roles for myosin Va in dense core vesicle biogenesis and function. Biochem. Soc. Trans. 38, 199-204.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 199-204
    • Kögel, T.1    Bittins, C.M.2    Rudolf, R.3    Gerdes, H.H.4
  • 54
    • 1642286846 scopus 로고    scopus 로고
    • Myosin V: Regulation by calcium, calmodulin, and the tail domain
    • Krementsov D. N., Krementsova E. B., and, Trybus K. M., (2004) Myosin V: regulation by calcium, calmodulin, and the tail domain. J. Cell Biol. 164, 877-886.
    • (2004) J. Cell Biol. , vol.164 , pp. 877-886
    • Krementsov, D.N.1    Krementsova, E.B.2    Trybus, K.M.3
  • 55
    • 0344034703 scopus 로고    scopus 로고
    • Myosin Va and microtubule-based motors are required for fast axonal retrograde transport of tetanus toxin in motor neurons
    • Lalli G., Gschmeissner S., and, Schiavo G., (2003) Myosin Va and microtubule-based motors are required for fast axonal retrograde transport of tetanus toxin in motor neurons. J. Cell Sci. 116, 4639-4650.
    • (2003) J. Cell Sci. , vol.116 , pp. 4639-4650
    • Lalli, G.1    Gschmeissner, S.2    Schiavo, G.3
  • 57
    • 0035158088 scopus 로고    scopus 로고
    • Myosin vb is associated with plasma membrane recycling systems
    • Lapierre L. A., Kumar R., Hales C. M., et al. (2001) Myosin vb is associated with plasma membrane recycling systems. Mol. Biol. Cell 12, 1843-1857.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1843-1857
    • Lapierre, L.A.1    Kumar, R.2    Hales, C.M.3
  • 58
    • 70450277100 scopus 로고    scopus 로고
    • Myosin-Va restrains the trafficking of Na+/K+-ATPase-containing vesicles in alveolar epithelial cells
    • Lecuona E., Minin A., Trejo H. E., et al. (2009) Myosin-Va restrains the trafficking of Na+/K+-ATPase-containing vesicles in alveolar epithelial cells. J. Cell Sci. 122, 3915-3922.
    • (2009) J. Cell Sci. , vol.122 , pp. 3915-3922
    • Lecuona, E.1    Minin, A.2    Trejo, H.E.3
  • 59
    • 0035976524 scopus 로고    scopus 로고
    • Regulation of cell survival by secreted proneurotrophins
    • Lee R., Kermani P., Teng K. K., and, Hempstead B. L., (2001) Regulation of cell survival by secreted proneurotrophins. Science 294, 1945-1948.
    • (2001) Science , vol.294 , pp. 1945-1948
    • Lee, R.1    Kermani, P.2    Teng, K.K.3    Hempstead, B.L.4
  • 60
    • 0033460318 scopus 로고    scopus 로고
    • Activity-dependent neurotransmitter release kinetics: Correlation with changes in morphological distributions of small and large vesicles in central nerve terminals
    • Leenders A. G., Scholten G., Wiegant V. M., Da Silva F. H., and, Ghijsen W. E., (1999) Activity-dependent neurotransmitter release kinetics: correlation with changes in morphological distributions of small and large vesicles in central nerve terminals. Eur. J. Neurosci. 11, 4269-4277.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 4269-4277
    • Leenders, A.G.1    Scholten, G.2    Wiegant, V.M.3    Da Silva, F.H.4    Ghijsen, W.E.5
  • 61
    • 67349173666 scopus 로고    scopus 로고
    • Myosin-dependent targeting of transmembrane proteins to neuronal dendrites
    • Lewis T. L. Jr, Mao T., Svoboda K., and, Arnold D. B., (2009) Myosin-dependent targeting of transmembrane proteins to neuronal dendrites. Nat. Neurosci. 12, 568-576.
    • (2009) Nat. Neurosci. , vol.12 , pp. 568-576
    • Lewis, Jr.T.L.1    Mao, T.2    Svoboda, K.3    Arnold, D.B.4
  • 62
    • 38849084743 scopus 로고    scopus 로고
    • The tail that wags the dog: The globular tail domain defines the function of myosin V/XI
    • Li J. F., and, Nebenfuhr A., (2008) The tail that wags the dog: the globular tail domain defines the function of myosin V/XI. Traffic 9, 290-298.
    • (2008) Traffic , vol.9 , pp. 290-298
    • Li, J.F.1    Nebenfuhr, A.2
  • 63
    • 1242317813 scopus 로고    scopus 로고
    • Ca2+-induced activation of ATPase activity of myosin Va is accompanied with a large conformational change
    • Li X. D., Mabuchi K., Ikebe R., and, Ikebe M., (2004) Ca2+-induced activation of ATPase activity of myosin Va is accompanied with a large conformational change. Biochem. Biophys. Res. Commun. 315, 538-545.
    • (2004) Biochem. Biophys. Res. Commun. , vol.315 , pp. 538-545
    • Li, X.D.1    Mabuchi, K.2    Ikebe, R.3    Ikebe, M.4
  • 64
    • 34249100238 scopus 로고    scopus 로고
    • Myosin V, Rab11, and dRip11 direct apical secretion and cellular morphogenesis in developing Drosophila photoreceptors
    • Li B. X., Satoh A. K., and, Ready D. F., (2007) Myosin V, Rab11, and dRip11 direct apical secretion and cellular morphogenesis in developing Drosophila photoreceptors. J. Cell Biol. 177, 659-669.
    • (2007) J. Cell Biol. , vol.177 , pp. 659-669
    • Li, B.X.1    Satoh, A.K.2    Ready, D.F.3
  • 65
    • 33645644972 scopus 로고    scopus 로고
    • Involvement of myosin Vb in glutamate receptor trafficking
    • Lisé M. F., Wong T. P., Trinh A., et al. (2006) Involvement of myosin Vb in glutamate receptor trafficking. J. Biol. Chem. 281, 3669-3678.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3669-3678
    • Lisé, M.F.1    Wong, T.P.2    Trinh, A.3
  • 66
    • 34447625042 scopus 로고    scopus 로고
    • The sequence of events that underlie quantal transmission at central glutamatergic synapses
    • Lisman J. E., Raghavachari S., and, Tsien R. W., (2007) The sequence of events that underlie quantal transmission at central glutamatergic synapses. Nat. Rev. Neurosci. 8, 597-609.
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 597-609
    • Lisman, J.E.1    Raghavachari, S.2    Tsien, R.W.3
  • 67
    • 33751309948 scopus 로고    scopus 로고
    • Activity-dependent release of tissue plasminogen activator from the dendritic spines of hippocampal neurons revealed by live-cell imaging
    • Lochner J. E., Honigman L. S., Grant W. F., Gessford S. K., Hansen A. B., Silverman M. A., and, Scalettar B. A., (2006) Activity-dependent release of tissue plasminogen activator from the dendritic spines of hippocampal neurons revealed by live-cell imaging. J. Neurobiol. 66, 564-577.
    • (2006) J. Neurobiol. , vol.66 , pp. 564-577
    • Lochner, J.E.1    Honigman, L.S.2    Grant, W.F.3    Gessford, S.K.4    Hansen, A.B.5    Silverman, M.A.6    Scalettar, B.A.7
  • 68
    • 33845894135 scopus 로고    scopus 로고
    • Regulation of myosin v processivity by calcium at the single molecule level
    • Lu H., Krementsova E. B., and, Trybus K. M., (2006) Regulation of myosin V processivity by calcium at the single molecule level. J. Biol. Chem. 281, 31987-31994.
    • (2006) J. Biol. Chem. , vol.281 , pp. 31987-31994
    • Lu, H.1    Krementsova, E.B.2    Trybus, K.M.3
  • 69
    • 0026310518 scopus 로고
    • The role of postsynaptic calcium in the induction of long-term potentiation
    • Malenka R. C., (1991) The role of postsynaptic calcium in the induction of long-term potentiation. Mol. Neurobiol. 5, 289-295.
    • (1991) Mol. Neurobiol. , vol.5 , pp. 289-295
    • Malenka, R.C.1
  • 70
    • 52749089928 scopus 로고    scopus 로고
    • The class v myosin motor, myosin 5c, localizes to mature secretory vesicles and facilitates exocytosis in lacrimal acini
    • Marchelletta R. R., Jacobs D. T., Schechter J. E., Cheney R. E., and, Hamm-Alvarez S. F., (2008) The class V myosin motor, myosin 5c, localizes to mature secretory vesicles and facilitates exocytosis in lacrimal acini. Am. J. Physiol. Cell Physiol. 295, C13-C28.
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295
    • Marchelletta, R.R.1    Jacobs, D.T.2    Schechter, J.E.3    Cheney, R.E.4    Hamm-Alvarez, S.F.5
  • 72
    • 57549096273 scopus 로고
    • Novel myosin heavy chain encoded by murine dilute coat colour locus
    • Mercer J., Seperack P., Strobel M., Copeland N., and, Jenkins N. A., (1990) Novel myosin heavy chain encoded by murine dilute coat colour locus. Nature 352, 547.
    • (1990) Nature , vol.352 , pp. 547
    • Mercer, J.1    Seperack, P.2    Strobel, M.3    Copeland, N.4    Jenkins, N.A.5
  • 73
    • 53849134828 scopus 로고    scopus 로고
    • Rapid recycling of beta-adrenergic receptors is dependent on the actin cytoskeleton and myosin Vb
    • Millman E. E., Zhang H., Zhang H., Godines V., Bean A. J., Knoll B. J., and, Moore R. H., (2008) Rapid recycling of beta-adrenergic receptors is dependent on the actin cytoskeleton and myosin Vb. Traffic 9, 1958-1971.
    • (2008) Traffic , vol.9 , pp. 1958-1971
    • Millman, E.E.1    Zhang, H.2    Zhang, H.3    Godines, V.4    Bean, A.J.5    Knoll, B.J.6    Moore, R.H.7
  • 74
    • 0033636896 scopus 로고    scopus 로고
    • Local calcium release in dendritic spines required for long-term synaptic depression
    • Miyata M., Finch E. A., Khiroug L., et al. (2000) Local calcium release in dendritic spines required for long-term synaptic depression. Neuron 28, 233-244.
    • (2000) Neuron , vol.28 , pp. 233-244
    • Miyata, M.1    Finch, E.A.2    Khiroug, L.3
  • 75
    • 52949112224 scopus 로고    scopus 로고
    • MYO5B mutations cause microvillus inclusion disease and disrupt epithelial cell polarity
    • Müller T., Hess M. W., Schiefermeier N., et al. (2008) MYO5B mutations cause microvillus inclusion disease and disrupt epithelial cell polarity. Nat. Genet. 40, 1163-1165.
    • (2008) Nat. Genet. , vol.40 , pp. 1163-1165
    • Müller, T.1    Hess, M.W.2    Schiefermeier, N.3
  • 76
  • 77
    • 33846197918 scopus 로고    scopus 로고
    • A Role of myosin Vb and Rab11-FIP2 in the aquaporin-2 shuttle
    • Nedvetsky P. I., Stefan E., Frische S., et al. (2007) A Role of myosin Vb and Rab11-FIP2 in the aquaporin-2 shuttle. Traffic 8, 110-123.
    • (2007) Traffic , vol.8 , pp. 110-123
    • Nedvetsky, P.I.1    Stefan, E.2    Frische, S.3
  • 78
    • 3042678496 scopus 로고    scopus 로고
    • Phosphorylation reactions in activity-dependent synapse modification at the neuromuscular junction during development
    • Nelson P. G., Lanuza M. A., Jia M., Li M. X., and, Tomas J., (2003) Phosphorylation reactions in activity-dependent synapse modification at the neuromuscular junction during development. J. Neurocytol. 32, 803-816.
    • (2003) J. Neurocytol. , vol.32 , pp. 803-816
    • Nelson, P.G.1    Lanuza, M.A.2    Jia, M.3    Li, M.X.4    Tomas, J.5
  • 79
    • 0034814742 scopus 로고    scopus 로고
    • Globular tail of myosin-V is bound to vamp/synaptobrevin
    • Ohyama A., Komiya Y., and, Igarashi M., (2001) Globular tail of myosin-V is bound to vamp/synaptobrevin. Biochem. Biophys. Res. Commun. 280, 988-991.
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 988-991
    • Ohyama, A.1    Komiya, Y.2    Igarashi, M.3
  • 80
    • 7044267351 scopus 로고    scopus 로고
    • Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity
    • Okamoto K., Nagai T., Miyawaki A., and, Hayashi Y., (2004) Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity. Nat. Neurosci. 7, 1104-1112.
    • (2004) Nat. Neurosci. , vol.7 , pp. 1104-1112
    • Okamoto, K.1    Nagai, T.2    Miyawaki, A.3    Hayashi, Y.4
  • 81
  • 82
    • 33845396840 scopus 로고    scopus 로고
    • Plasticity-induced growth of dendritic spines by exocytic trafficking from recycling endosomes
    • Park M., Salgado J. M., Ostroff L., Helton T. D., Robinson C. G., Harris K. M., and, Ehlers M. D., (2006) Plasticity-induced growth of dendritic spines by exocytic trafficking from recycling endosomes. Neuron 52, 817-830.
    • (2006) Neuron , vol.52 , pp. 817-830
    • Park, M.1    Salgado, J.M.2    Ostroff, L.3    Helton, T.D.4    Robinson, C.G.5    Harris, K.M.6    Ehlers, M.D.7
  • 83
    • 68649124073 scopus 로고    scopus 로고
    • Semaphorin function in neural plasticity and disease
    • Pasterkamp R. J., and, Giger R. J., (2009) Semaphorin function in neural plasticity and disease. Curr. Opin. Neurobiol. 19, 263-274.
    • (2009) Curr. Opin. Neurobiol. , vol.19 , pp. 263-274
    • Pasterkamp, R.J.1    Giger, R.J.2
  • 84
    • 0030914460 scopus 로고    scopus 로고
    • Griscelli disease maps to chromosome 15q21 and is associated with mutations in the myosin-Va gene
    • Pastural E., Barrat F. J., Dufourcq-Lagelouse R., et al. (1997) Griscelli disease maps to chromosome 15q21 and is associated with mutations in the myosin-Va gene. Nat. Genet. 16, 289-292.
    • (1997) Nat. Genet. , vol.16 , pp. 289-292
    • Pastural, E.1    Barrat, F.J.2    Dufourcq-Lagelouse, R.3
  • 85
    • 77954420032 scopus 로고    scopus 로고
    • Evidence that myosin activity opposes microtubule-based axonal transport of mitochondria
    • Pathak D., Sepp K. J., and, Hollenbeck P. J., (2010) Evidence that myosin activity opposes microtubule-based axonal transport of mitochondria. J. Neurosci. 30, 8984-8992.
    • (2010) J. Neurosci. , vol.30 , pp. 8984-8992
    • Pathak, D.1    Sepp, K.J.2    Hollenbeck, P.J.3
  • 86
    • 0023866466 scopus 로고
    • The ultrastructural localization of calcium-activated protease "calpain" in rat brain
    • Perlmutter L. S., Siman R., Gall C., Seubert P., Baudry M., and, Lynch G., (1988) The ultrastructural localization of calcium-activated protease "calpain" in rat brain. Synapse 2, 79-88.
    • (1988) Synapse , vol.2 , pp. 79-88
    • Perlmutter, L.S.1    Siman, R.2    Gall, C.3    Seubert, P.4    Baudry, M.5    Lynch, G.6
  • 87
    • 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 J. A. 3rd, and, Wenthold R. J., (2001) Glutamate receptor targeting in the postsynaptic spine involves mechanisms that are independent of myosin Va. Eur. J. Neurosci. 13, 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
  • 88
    • 0030921711 scopus 로고    scopus 로고
    • Brain myosin v is a synaptic vesicle-associated motor protein: Evidence for a Ca2+-dependent interaction with the synaptobrevin-synaptophysin complex
    • Prekeris R., and, Terrian D. M., (1997) Brain myosin V is a synaptic vesicle-associated motor protein: evidence for a Ca2+-dependent interaction with the synaptobrevin-synaptophysin complex. J. Cell Biol. 137, 1589-1601.
    • (1997) J. Cell Biol. , vol.137 , pp. 1589-1601
    • Prekeris, R.1    Terrian, D.M.2
  • 89
    • 51649105426 scopus 로고    scopus 로고
    • Myosin-Vb functions as a dynamic tether for peripheral endocytic compartments during transferrin trafficking
    • Provance D. W. Jr, Addison E. J., Wood P. R., Chen D. Z., Silan C. M., and, Mercer J. A., (2008) Myosin-Vb functions as a dynamic tether for peripheral endocytic compartments during transferrin trafficking. BMC Cell Biol. 9, 44.
    • (2008) BMC Cell Biol. , vol.9 , pp. 44
    • Provance, Jr.D.W.1    Addison, E.J.2    Wood, P.R.3    Chen, D.Z.4    Silan, C.M.5    Mercer, J.A.6
  • 90
    • 33644847375 scopus 로고    scopus 로고
    • 2+: Molecular determinants and functional consequences
    • 2+: molecular determinants and functional consequences. Physiol. Rev. 86, 369-408.
    • (2006) Physiol. Rev. , vol.86 , pp. 369-408
    • Rizzuto, R.1    Pozzan, T.2
  • 93
    • 0036500526 scopus 로고    scopus 로고
    • Human myosin-Vc is a novel class v myosin expressed in epithelial cells
    • Rodriguez O. C., and, Cheney R. E., (2002) Human myosin-Vc is a novel class V myosin expressed in epithelial cells. J. Cell Sci. 115, 991-1004.
    • (2002) J. Cell Sci. , vol.115 , pp. 991-1004
    • Rodriguez, O.C.1    Cheney, R.E.2
  • 94
    • 0033588979 scopus 로고    scopus 로고
    • Regulation of melanosome movement in the cell cycle by reversible association with myosin v
    • Rogers S. L., Karcher R. L., Roland J. T., Minin A. A., Steffen W., and, Gelfand V. I., (1999) Regulation of melanosome movement in the cell cycle by reversible association with myosin V. J. Cell Biol. 146, 1265-1276.
    • (1999) J. Cell Biol. , vol.146 , pp. 1265-1276
    • Rogers, S.L.1    Karcher, R.L.2    Roland, J.T.3    Minin, A.A.4    Steffen, W.5    Gelfand, V.I.6
  • 95
    • 59449108592 scopus 로고    scopus 로고
    • Alternative splicing in class v myosins determines association with Rab10
    • Roland J. T., Lapierre L. A., and, Goldenring J. R., (2009) Alternative splicing in class V myosins determines association with Rab10. J. Biol. Chem. 284, 1213-1223.
    • (2009) J. Biol. Chem. , vol.284 , pp. 1213-1223
    • Roland, J.T.1    Lapierre, L.A.2    Goldenring, J.R.3
  • 97
    • 0037387771 scopus 로고    scopus 로고
    • Myosins II and v in chromaffin cells: Myosin v is a chromaffin vesicle molecular motor involved in secretion
    • Rose S. D., Lejen T., Casaletti L., Larson R. E., Pene T. D., and, Trifaro J. M., (2003) Myosins II and V in chromaffin cells: myosin V is a chromaffin vesicle molecular motor involved in secretion. J. Neurochem. 85, 287-298.
    • (2003) J. Neurochem. , vol.85 , pp. 287-298
    • Rose, S.D.1    Lejen, T.2    Casaletti, L.3    Larson, R.E.4    Pene, T.D.5    Trifaro, J.M.6
  • 98
    • 39149138988 scopus 로고    scopus 로고
    • Cargo transport: Molecular motors navigate a complex cytoskeleton
    • Ross J. L., Ali M. Y., and, Warshaw D. M., (2008) Cargo transport: molecular motors navigate a complex cytoskeleton. Curr. Opin. Cell Biol. 20, 41-47.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 41-47
    • Ross, J.L.1    Ali, M.Y.2    Warshaw, D.M.3
  • 99
    • 0034762729 scopus 로고    scopus 로고
    • Dynamics of immature secretory granules: Role of cytoskeletal elements during transport, cortical restriction, and F-actin-dependent tethering
    • Rudolf R., Salm T., Rustom A., and, Gerdes H. H., (2001) Dynamics of immature secretory granules: role of cytoskeletal elements during transport, cortical restriction, and F-actin-dependent tethering. Mol. Biol. Cell 12, 1353-1365.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1353-1365
    • Rudolf, R.1    Salm, T.2    Rustom, A.3    Gerdes, H.H.4
  • 101
    • 0033879511 scopus 로고    scopus 로고
    • An allelic variant of Griscelli disease: Presentation with severe hypotonia, mental-motor retardation, and hypopigmentation consistent with Elejalde syndrome (neuroectodermal melanolysosomal disorder)
    • Sanal O., Yel L., Kucukali T., Gilbert-Barnes E., Tardieu M., Texcan I., Ersoy F., Metin A., and, de Saint Basile G., (2000) An allelic variant of Griscelli disease: presentation with severe hypotonia, mental-motor retardation, and hypopigmentation consistent with Elejalde syndrome (neuroectodermal melanolysosomal disorder). J. Neurol. 247, 570-572.
    • (2000) J. Neurol. , vol.247 , pp. 570-572
    • Sanal, O.1    Yel, L.2    Kucukali, T.3    Gilbert-Barnes, E.4    Tardieu, M.5    Texcan, I.6    Ersoy, F.7    Metin, A.8    De Saint Basile, G.9
  • 102
    • 75849123055 scopus 로고    scopus 로고
    • Differential vesicular distribution and trafficking of MMP-2, MMP-9, and their inhibitors in astrocytes
    • Sbai O., Ould-Yahoui A., Ferhat L., et al. (2010) Differential vesicular distribution and trafficking of MMP-2, MMP-9, and their inhibitors in astrocytes. Glia 58, 344-366.
    • (2010) Glia , vol.58 , pp. 344-366
    • Sbai, O.1    Ould-Yahoui, A.2    Ferhat, L.3
  • 103
    • 0035071224 scopus 로고    scopus 로고
    • Hippocampal synaptic transmission and plasticity are preserved in myosin Va mutant mice
    • Schnell E., and, Nicoll R. A., (2001) Hippocampal synaptic transmission and plasticity are preserved in myosin Va mutant mice. J. Neurophysiol. 85, 1498-1501.
    • (2001) J. Neurophysiol. , vol.85 , pp. 1498-1501
    • Schnell, E.1    Nicoll, R.A.2
  • 104
    • 0030050741 scopus 로고    scopus 로고
    • Cellular processing of the neurotrophin precursors of NT3 and BDNF by the mammalian proprotein convertases
    • Seidah N. G., Benjannet S., Pareek S., Chretien M., and, Murphy R. A., (1996) Cellular processing of the neurotrophin precursors of NT3 and BDNF by the mammalian proprotein convertases. FEBS Lett. 379, 247-250.
    • (1996) FEBS Lett. , vol.379 , pp. 247-250
    • Seidah, N.G.1    Benjannet, S.2    Pareek, S.3    Chretien, M.4    Murphy, R.A.5
  • 106
    • 0029048850 scopus 로고
    • Exocytosis in peptidergic nerve terminals exhibits two calcium-sensitive phases during pulsatile calcium entry
    • Seward E. P., Chernevskaya N. I., and, Nowycky M. C., (1995) Exocytosis in peptidergic nerve terminals exhibits two calcium-sensitive phases during pulsatile calcium entry. J. Neurosci. 15, 3390-3399.
    • (1995) J. Neurosci. , vol.15 , pp. 3390-3399
    • Seward, E.P.1    Chernevskaya, N.I.2    Nowycky, M.C.3
  • 107
    • 33745521118 scopus 로고    scopus 로고
    • Activity-dependent synaptic capture of transiting peptidergic vesicles
    • Shakiryanova D., Tully A., and, Levitan E. S., (2006) Activity-dependent synaptic capture of transiting peptidergic vesicles. Nat. Neurosci. 9, 896-900.
    • (2006) Nat. Neurosci. , vol.9 , pp. 896-900
    • Shakiryanova, D.1    Tully, A.2    Levitan, E.S.3
  • 108
    • 38149016966 scopus 로고    scopus 로고
    • The cell biology of synaptic plasticity: AMPA receptor trafficking
    • Shepherd J. D., and, Huganir R. L., (2007) The cell biology of synaptic plasticity: AMPA receptor trafficking. Annu. Rev. Cell Dev. Biol. 23, 613-643.
    • (2007) Annu. Rev. Cell Dev. Biol. , vol.23 , pp. 613-643
    • Shepherd, J.D.1    Huganir, R.L.2
  • 109
    • 16244419347 scopus 로고    scopus 로고
    • Mechanisms of transport and exocytosis of dense-core granules containing tissue plasminogen activator in developing hippocampal neurons
    • Silverman M. A., Johnson S., Gurkins D., Farmer M., Lochner J. E., Rosa P., and, Scalettar B. A., (2005) Mechanisms of transport and exocytosis of dense-core granules containing tissue plasminogen activator in developing hippocampal neurons. J. Neurosci. 25, 3095-3106.
    • (2005) J. Neurosci. , vol.25 , pp. 3095-3106
    • Silverman, M.A.1    Johnson, S.2    Gurkins, D.3    Farmer, M.4    Lochner, J.E.5    Rosa, P.6    Scalettar, B.A.7
  • 110
    • 0035830935 scopus 로고    scopus 로고
    • Cellular signaling through multifunctional Ca2+/calmodulin-dependent protein kinase II
    • Soderling T. R., Chang B., and, Brickey D., (2001) Cellular signaling through multifunctional Ca2+/calmodulin-dependent protein kinase II. J. Biol. Chem. 276, 3719-3722.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3719-3722
    • Soderling, T.R.1    Chang, B.2    Brickey, D.3
  • 111
    • 3442879896 scopus 로고    scopus 로고
    • Formation, stabilisation and fusion of the readily releasable pool of secretory vesicles
    • Sorensen J. B., (2004) Formation, stabilisation and fusion of the readily releasable pool of secretory vesicles. Pflugers Arch. 448, 347-362.
    • (2004) Pflugers Arch. , vol.448 , pp. 347-362
    • Sorensen, J.B.1
  • 112
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffic
    • Stenmark H., (2009) Rab GTPases as coordinators of vesicle traffic. Nat. Rev. Mol. Cell Biol. 10, 513-525.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 113
    • 34548171427 scopus 로고    scopus 로고
    • Myosin Vb is required for trafficking of the cystic fibrosis transmembrane conductance regulator in Rab11a-specific apical recycling endosomes in polarized human airway epithelial cells
    • Swiatecka-Urban A., Talebian L., Kanno E., et al. (2007) Myosin Vb is required for trafficking of the cystic fibrosis transmembrane conductance regulator in Rab11a-specific apical recycling endosomes in polarized human airway epithelial cells. J. Biol. Chem. 282, 23725-23736.
    • (2007) J. Biol. Chem. , vol.282 , pp. 23725-23736
    • Swiatecka-Urban, A.1    Talebian, L.2    Kanno, E.3
  • 115
  • 116
    • 33750805030 scopus 로고    scopus 로고
    • Molecular anatomy of a trafficking organelle
    • Takamori S., Holt M., Stenius K., et al. (2006) Molecular anatomy of a trafficking organelle. Cell 127, 831-846.
    • (2006) Cell , vol.127 , pp. 831-846
    • Takamori, S.1    Holt, M.2    Stenius, K.3
  • 117
    • 20044370999 scopus 로고    scopus 로고
    • ProBDNF induces neuronal apoptosis via activation of a receptor complex of p75NTR and sortilin
    • Teng H. K., Teng K. K., Lee R., et al. (2005) ProBDNF induces neuronal apoptosis via activation of a receptor complex of p75NTR and sortilin. J. Neurosci. 25, 5455-5463.
    • (2005) J. Neurosci. , vol.25 , pp. 5455-5463
    • Teng, H.K.1    Teng, K.K.2    Lee, R.3
  • 118
  • 121
    • 43049183000 scopus 로고    scopus 로고
    • Myosin v from head to tail
    • Trybus K. M., (2008) Myosin V from head to tail. Cell. Mol. Life Sci. 65, 1378-1389.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1378-1389
    • Trybus, K.M.1
  • 122
    • 66149115113 scopus 로고    scopus 로고
    • The recycling and transcytotic pathways for IgG transport by FcRn are distinct and display an inherent polarity
    • Tzaban S., Massol R. H., Yen E., et al. (2009) The recycling and transcytotic pathways for IgG transport by FcRn are distinct and display an inherent polarity. J. Cell Biol. 185, 673-684.
    • (2009) J. Cell Biol. , vol.185 , pp. 673-684
    • Tzaban, S.1    Massol, R.H.2    Yen, E.3
  • 123
    • 0027370762 scopus 로고
    • Rab11, a small GTPase associated with both constitutive and regulated secretory pathways in PC12 cells
    • Urbe S., Huber L. A., Zerial M., Tooze S. A., and, Parton R. G., (1993) Rab11, a small GTPase associated with both constitutive and regulated secretory pathways in PC12 cells. FEBS Lett. 334, 175-182.
    • (1993) FEBS Lett. , vol.334 , pp. 175-182
    • Urbe, S.1    Huber, L.A.2    Zerial, M.3    Tooze, S.A.4    Parton, R.G.5
  • 124
    • 19644364331 scopus 로고    scopus 로고
    • Myosin Va transports dense core secretory vesicles in pancreatic MIN6 beta-cells
    • Varadi A., Tsuboi T., and, Rutter G. A., (2005) Myosin Va transports dense core secretory vesicles in pancreatic MIN6 beta-cells. Mol. Biol. Cell 16, 2670-2680.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2670-2680
    • Varadi, A.1    Tsuboi, T.2    Rutter, G.A.3
  • 125
    • 0037112197 scopus 로고    scopus 로고
    • Rab11a and myosin Vb regulate recycling of the M4 muscarinic acetylcholine receptor
    • Volpicelli L. A., Lah J. J., Fang G., Goldenring J. R., and, Levey A. I., (2002) Rab11a and myosin Vb regulate recycling of the M4 muscarinic acetylcholine receptor. J. Neurosci. 22, 9776-9784.
    • (2002) J. Neurosci. , vol.22 , pp. 9776-9784
    • Volpicelli, L.A.1    Lah, J.J.2    Fang, G.3    Goldenring, J.R.4    Levey, A.I.5
  • 128
    • 54549123514 scopus 로고    scopus 로고
    • Myosin Vb mobilizes recycling endosomes and AMPA receptors for postsynaptic plasticity
    • Wang Z., Edwards J. G., Riley N., et al. (2008) Myosin Vb mobilizes recycling endosomes and AMPA receptors for postsynaptic plasticity. Cell 135, 535-548.
    • (2008) Cell , vol.135 , pp. 535-548
    • Wang, Z.1    Edwards, J.G.2    Riley, N.3
  • 130
    • 26244449813 scopus 로고    scopus 로고
    • Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A
    • Watanabe M., Nomura K., Ohyama A., et al. (2005) Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A. Mol. Biol. Cell 16, 4519-4530.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4519-4530
    • Watanabe, M.1    Nomura, K.2    Ohyama, A.3
  • 131
    • 33745750458 scopus 로고    scopus 로고
    • Vesicular trafficking of semaphorin 3A is activity-dependent and differs between axons and dendrites
    • de Wit J., Toonen R. F., Verhaagen J., and, Verhage M., (2006) Vesicular trafficking of semaphorin 3A is activity-dependent and differs between axons and dendrites. Traffic 7, 1060-1077.
    • (2006) Traffic , vol.7 , pp. 1060-1077
    • De Wit, J.1    Toonen, R.F.2    Verhaagen, J.3    Verhage, M.4
  • 132
    • 0030964893 scopus 로고    scopus 로고
    • Myosin v associates with melanosomes in mouse melanocytes: Evidence that myosin v is an organelle motor
    • Wu X., Bowers B., Wei Q., Kocher B., and, Hammer J. A. 3rd, (1997) Myosin V associates with melanosomes in mouse melanocytes: evidence that myosin V is an organelle motor. J. Cell Sci. 110 (Pt 7), 847-859.
    • (1997) J. Cell Sci. , vol.110 , Issue.PART 7 , pp. 847-859
    • Wu, X.1    Bowers, B.2    Wei, Q.3    Kocher, B.4    Hammer III, J.A.5
  • 133
    • 0032576622 scopus 로고    scopus 로고
    • Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin v function in vivo
    • Wu X., Bowers B., Rao K., Wei Q., and, Hammer J. A. 3rd, (1998) Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function In vivo. J. Cell Biol. 143, 1899-1918.
    • (1998) J. Cell Biol. , vol.143 , pp. 1899-1918
    • Wu, X.1    Bowers, B.2    Rao, K.3    Wei, Q.4    Hammer III, J.A.5
  • 134
    • 1542334478 scopus 로고    scopus 로고
    • Nerve growth factor, brain-derived neurotrophic factor, and neurotrophin-3 are sorted to dense-core vesicles and released via the regulated pathway in primary rat cortical neurons
    • Wu Y. J., Kruttgen A., Moller J. C., Shine D., Chan J. R., Shooter E. M., and, Cosgaya J. M., (2004) Nerve growth factor, brain-derived neurotrophic factor, and neurotrophin-3 are sorted to dense-core vesicles and released via the regulated pathway in primary rat cortical neurons. J. Neurosci. Res. 75, 825-834.
    • (2004) J. Neurosci. Res. , vol.75 , pp. 825-834
    • Wu, Y.J.1    Kruttgen, A.2    Moller, J.C.3    Shine, D.4    Chan, J.R.5    Shooter, E.M.6    Cosgaya, J.M.7
  • 135
    • 0030785497 scopus 로고    scopus 로고
    • Acetylcholine receptors in innervated muscles of dystrophic mdx mice degrade as after denervation
    • Xu R., and, Salpeter M. M., (1997) Acetylcholine receptors in innervated muscles of dystrophic mdx mice degrade as after denervation. J. Neurosci. 17, 8194-8200.
    • (1997) J. Neurosci. , vol.17 , pp. 8194-8200
    • Xu, R.1    Salpeter, M.M.2
  • 136
    • 78049376215 scopus 로고    scopus 로고
    • Time lapse in vivo visualization of developmental stabilization of synaptic receptors at Neuromuscular Junctions
    • Yampolsky P., Pacifici P. G., Lomb L., Giese G., Rudolf R., Röder I. V., and, Witzemann V., (2010) Time lapse in vivo visualization of developmental stabilization of synaptic receptors at Neuromuscular Junctions. J. Biol. Chem. 285, 34589-34596.
    • (2010) J. Biol. Chem. , vol.285 , pp. 34589-34596
    • Yampolsky, P.1    Pacifici, P.G.2    Lomb, L.3    Giese, G.4    Rudolf, R.5    Röder, I.V.6    Witzemann, V.7
  • 137
  • 138
    • 33751428390 scopus 로고    scopus 로고
    • Myosin-Va facilitates the accumulation of mRNA/protein complex in dendritic spines
    • Yoshimura A., Fujii R., Watanabe Y., Okabe S., Fukui K., and, Takumi T., (2006) Myosin-Va facilitates the accumulation of mRNA/protein complex in dendritic spines. Curr. Biol. 16, 2345-2351.
    • (2006) Curr. Biol. , vol.16 , pp. 2345-2351
    • Yoshimura, A.1    Fujii, R.2    Watanabe, Y.3    Okabe, S.4    Fukui, K.5    Takumi, T.6
  • 139
    • 34447499043 scopus 로고    scopus 로고
    • Myosin 5a is an insulin-stimulated Akt2 (protein kinase Bbeta) substrate modulating GLUT4 vesicle translocation
    • Yoshizaki T., Imamura T., Babendure J. L., Lu J. C., Sonoda N., and, Olefsky J. M., (2007) Myosin 5a is an insulin-stimulated Akt2 (protein kinase Bbeta) substrate modulating GLUT4 vesicle translocation. Mol. Cell. Biol. 27, 5172-5183.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 5172-5183
    • Yoshizaki, T.1    Imamura, T.2    Babendure, J.L.3    Lu, J.C.4    Sonoda, N.5    Olefsky, J.M.6
  • 140
    • 69249211018 scopus 로고    scopus 로고
    • CAMP signal transduction in the heart: Understanding spatial control for the development of novel therapeutic strategies
    • Zaccolo M., (2009) cAMP signal transduction in the heart: understanding spatial control for the development of novel therapeutic strategies. Br. J. Pharmacol. 158, 50-60.
    • (2009) Br. J. Pharmacol. , vol.158 , pp. 50-60
    • Zaccolo, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.