메뉴 건너뛰기




Volumn 58, Issue 3, 2007, Pages 226-233

Roles of calmodulin and calmodulin-binding proteins in synaptic vesicle recycling during regulated exocytosis at submicromolar Ca2+ concentrations

Author keywords

Calcium; Calmodulin; CaMKII; Exocytosis; Myosin V; Recycling; SNARE mechanism

Indexed keywords

CALCIUM CHANNEL; CALCIUM ION; CALMODULIN; CALMODULIN BINDING PROTEIN; MYOSIN V; SNARE PROTEIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNAPTOTAGMIN; SYNTAXIN 1A;

EID: 34447252763     PISSN: 01680102     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neures.2007.03.005     Document Type: Article
Times cited : (18)

References (52)
  • 1
    • 0037138403 scopus 로고    scopus 로고
    • Calmodulin signaling via the IQ motif
    • Bähler M., and Rhoads A. Calmodulin signaling via the IQ motif. FEBS Lett. 513 (2002) 107-113
    • (2002) FEBS Lett. , vol.513 , pp. 107-113
    • Bähler, M.1    Rhoads, A.2
  • 2
    • 16344378248 scopus 로고    scopus 로고
    • Chronic antidepressants reduce depolarization-evoked glutamate release and protein interactions favoring formation of SNARE complex in hippocampus
    • Bonanno G., Giambelli R., Raiteri L., Tiraboschi E., Zappettini S., Musazzi L., Raiteri M., Racagni G., and Popoli M. Chronic antidepressants reduce depolarization-evoked glutamate release and protein interactions favoring formation of SNARE complex in hippocampus. J. Neurosci. 25 (2005) 3270-3279
    • (2005) J. Neurosci. , vol.25 , pp. 3270-3279
    • Bonanno, G.1    Giambelli, R.2    Raiteri, L.3    Tiraboschi, E.4    Zappettini, S.5    Musazzi, L.6    Raiteri, M.7    Racagni, G.8    Popoli, M.9
  • 3
    • 20544466059 scopus 로고    scopus 로고
    • 2+-sensor proteins: from Alzheimer's disease to cancer
    • 2+-sensor proteins: from Alzheimer's disease to cancer. Trends Pharmacol. Sci. 26 (2005) 345-351
    • (2005) Trends Pharmacol. Sci. , vol.26 , pp. 345-351
    • Braunewell, K.-H.1
  • 5
    • 0042160096 scopus 로고    scopus 로고
    • Calcium and calmodulin in membrane fusion
    • Burgoyne R.D., and Clague M.J. Calcium and calmodulin in membrane fusion. Biochim. Biophys. Acta 1641 (2003) 137-143
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 137-143
    • Burgoyne, R.D.1    Clague, M.J.2
  • 6
    • 0037378045 scopus 로고    scopus 로고
    • Secretory granule exocytosis
    • Burgoyne R.D., and Morgan A. Secretory granule exocytosis. Physiol. Rev. 83 (2003) 581-632
    • (2003) Physiol. Rev. , vol.83 , pp. 581-632
    • Burgoyne, R.D.1    Morgan, A.2
  • 8
    • 16244404961 scopus 로고    scopus 로고
    • 2+ buffers and synaptic efficacy
    • 2+ buffers and synaptic efficacy. Cell Calicum 37 (2005) 489-495
    • (2005) Cell Calicum , vol.37 , pp. 489-495
    • Burnashev, N.1    Rozov, A.2
  • 10
    • 0032420558 scopus 로고    scopus 로고
    • 2+ channels and their role in neurotransmitter release
    • 2+ channels and their role in neurotransmitter release. Cell Calcium 24 (1998) 307-323
    • (1998) Cell Calcium , vol.24 , pp. 307-323
    • Catterall, W.A.1
  • 12
    • 0033230605 scopus 로고    scopus 로고
    • Disruption of Rab3-calmodulin interaction, but not other effector interaction, prevents Rab3 inhibition of exocytosis
    • Coppola T., Perret-Menou V., Luthi S., Farnsworth C.C., Glomset J.A., and Regazzi R. Disruption of Rab3-calmodulin interaction, but not other effector interaction, prevents Rab3 inhibition of exocytosis. EMBO J. 18 (1999) 5885-5891
    • (1999) EMBO J. , vol.18 , pp. 5885-5891
    • Coppola, T.1    Perret-Menou, V.2    Luthi, S.3    Farnsworth, C.C.4    Glomset, J.A.5    Regazzi, R.6
  • 14
    • 0042744682 scopus 로고    scopus 로고
    • What is the role of SNARE proteins in membrane fusion?
    • Duman J.G., and Forte J.G. What is the role of SNARE proteins in membrane fusion?. Am. J. Physiol. Cell Physiol. 285 (2003) C237-C249
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285
    • Duman, J.G.1    Forte, J.G.2
  • 15
    • 0043162027 scopus 로고    scopus 로고
    • Long coiled-coil proteins and membrane traffic
    • Gillingham A.K., and Munro S. Long coiled-coil proteins and membrane traffic. Biochim. Biophys. Acta 1641 (2003) 71-85
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 71-85
    • Gillingham, A.K.1    Munro, S.2
  • 17
    • 0041327729 scopus 로고    scopus 로고
    • Myosin VI: two distinct roles in endocytosis
    • Hasson T. Myosin VI: two distinct roles in endocytosis. J. Cell Sci. 116 (2003) 3453-3461
    • (2003) J. Cell Sci. , vol.116 , pp. 3453-3461
    • Hasson, T.1
  • 18
    • 0035997377 scopus 로고    scopus 로고
    • Neuronal Ca/calmodulin-dependent protein kinase II: the role of structure and autoregulation in cellular function
    • Hudmon A., and Schulman H. Neuronal Ca/calmodulin-dependent protein kinase II: the role of structure and autoregulation in cellular function. Annu. Rev. Biochem. 71 (2002) 473-510
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 473-510
    • Hudmon, A.1    Schulman, H.2
  • 21
    • 0141960930 scopus 로고    scopus 로고
    • 2+ sensor for neurotransmitter release
    • 2+ sensor for neurotransmitter release. Trends Neurosci. 26 (2003) 413-422
    • (2003) Trends Neurosci. , vol.26 , pp. 413-422
    • Koh, T.-W.1    Bellen, H.J.2
  • 22
    • 0028135465 scopus 로고
    • Essential role of myosin light chain kinase in the mechanism for MgATP-dependent priming of exocytosis in adrenal chromaffin cells
    • Kumakura K., Sasaki K., Sakurai T., Ohara-Imaizumi M., Misonou H., Nakamura S., Matsuda Y., and Nonomura Y. Essential role of myosin light chain kinase in the mechanism for MgATP-dependent priming of exocytosis in adrenal chromaffin cells. J. Neurosci. 14 (1994) 7695-7703
    • (1994) J. Neurosci. , vol.14 , pp. 7695-7703
    • Kumakura, K.1    Sasaki, K.2    Sakurai, T.3    Ohara-Imaizumi, M.4    Misonou, H.5    Nakamura, S.6    Matsuda, Y.7    Nonomura, Y.8
  • 23
    • 14544276353 scopus 로고    scopus 로고
    • Regulation of synaptic vesicle recycling by calcineurin in different vesicle pools
    • Kumashiro S., Lu Y.F., Tomizawa K., Matsushita M., Wei F.Y., and Matsui H. Regulation of synaptic vesicle recycling by calcineurin in different vesicle pools. Neurosci Res. 51 (2005) 435-443
    • (2005) Neurosci Res. , vol.51 , pp. 435-443
    • Kumashiro, S.1    Lu, Y.F.2    Tomizawa, K.3    Matsushita, M.4    Wei, F.Y.5    Matsui, H.6
  • 24
    • 0037672843 scopus 로고    scopus 로고
    • The molecular machinery of synaptic vesicle exocytosis
    • Li L., and Chin L.S. The molecular machinery of synaptic vesicle exocytosis. Cell. Mol. Life Sci. 60 (2003) 942-960
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 942-960
    • Li, L.1    Chin, L.S.2
  • 25
    • 5444240793 scopus 로고    scopus 로고
    • Myosin Va is required for normal photoreceptor synaptic activity
    • Libby R.T., Lillo C., Kitamoto J., Williams D.S., and Steel K.P. Myosin Va is required for normal photoreceptor synaptic activity. J. Cell Sci. 117 (2004) 4509-4515
    • (2004) J. Cell Sci. , vol.117 , pp. 4509-4515
    • Libby, R.T.1    Lillo, C.2    Kitamoto, J.3    Williams, D.S.4    Steel, K.P.5
  • 26
    • 0036513485 scopus 로고    scopus 로고
    • The molecular basis of CaMKII function in synaptic and behavioural memory
    • Lisman J., Schulman H., and Cline H. The molecular basis of CaMKII function in synaptic and behavioural memory. Nat. Rev. Neurosci. 3 (2002) 175-190
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 175-190
    • Lisman, J.1    Schulman, H.2    Cline, H.3
  • 32
    • 0030610085 scopus 로고    scopus 로고
    • 2+/calmodulin causes rab3A to dissociate from synaptic membrane
    • 2+/calmodulin causes rab3A to dissociate from synaptic membrane. J. Biol. Chem. 272 (1997) 20857-20865
    • (1997) J. Biol. Chem. , vol.272 , pp. 20857-20865
    • Park, J.B.1    Farnsworth, C.C.2    Glomset, J.A.3
  • 33
    • 0030921711 scopus 로고    scopus 로고
    • 2+-dependent interaction with the synaptobrevin-synaptophysin complex
    • 2+-dependent interaction with the synaptobrevin-synaptophysin complex. J. Cell Biol. 137 (1997) 1589-1601
    • (1997) J. Cell Biol. , vol.137 , pp. 1589-1601
    • Prekeris, R.1    Terrian, D.M.2
  • 34
    • 33746915109 scopus 로고    scopus 로고
    • N- to C-terminal SNARE complex assembly promotes rapid membrane fusion
    • Pobbati A.V., Stein A., and Fasshauer D. N- to C-terminal SNARE complex assembly promotes rapid membrane fusion. Science 313 (2006) 673-676
    • (2006) Science , vol.313 , pp. 673-676
    • Pobbati, A.V.1    Stein, A.2    Fasshauer, D.3
  • 37
    • 0037174660 scopus 로고    scopus 로고
    • Emerging roles of presynaptic protein in Ca-triggered exocytosis
    • Rettig J., and Neher E. Emerging roles of presynaptic protein in Ca-triggered exocytosis. Science 298 (2002) 781-785
    • (2002) Science , vol.298 , pp. 781-785
    • Rettig, J.1    Neher, E.2
  • 38
    • 0030945196 scopus 로고    scopus 로고
    • Sequence motifs for calmodulin recognition
    • Rhoads A.R., and Friedberg F. Sequence motifs for calmodulin recognition. FASEB J. 11 (1997) 331-340
    • (1997) FASEB J. , vol.11 , pp. 331-340
    • Rhoads, A.R.1    Friedberg, F.2
  • 39
    • 0035913332 scopus 로고    scopus 로고
    • An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming
    • Richmond J.E., Weimer R.M., and Jorgensen E.M. An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming. Nature (Lond.) 412 (2001) 338-341
    • (2001) Nature (Lond.) , vol.412 , pp. 338-341
    • Richmond, J.E.1    Weimer, R.M.2    Jorgensen, E.M.3
  • 40
    • 0036673069 scopus 로고    scopus 로고
    • SNAREs and Munc18 in synaptic vesicle fusion
    • Rizo J., and Südhof T.C. SNAREs and Munc18 in synaptic vesicle fusion. Nat. Rev. Neurosci. 3 (2002) 641-653
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 641-653
    • Rizo, J.1    Südhof, T.C.2
  • 41
    • 0035924595 scopus 로고    scopus 로고
    • Calmodulin mediates rapid recruitment of fast-releasing synaptic vesicles at a calyx-type synapse
    • Sakaba T., and Neher E. Calmodulin mediates rapid recruitment of fast-releasing synaptic vesicles at a calyx-type synapse. Neuron 32 (2001) 1119-1131
    • (2001) Neuron , vol.32 , pp. 1119-1131
    • Sakaba, T.1    Neher, E.2
  • 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
  • 44
    • 0037040890 scopus 로고    scopus 로고
    • Synaptotagmins: why so many?
    • Südhof T.C. Synaptotagmins: why so many?. J. Biol. Chem. 277 (2002) 7629-7632
    • (2002) J. Biol. Chem. , vol.277 , pp. 7629-7632
    • Südhof, T.C.1
  • 45
    • 2942556680 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • Südhof T.C. The synaptic vesicle cycle. Annu. Rev. Neurosci. 27 (2004) 109-147
    • (2004) Annu. Rev. Neurosci. , vol.27 , pp. 109-147
    • Südhof, T.C.1
  • 46
    • 1642277786 scopus 로고    scopus 로고
    • Immunohistochemical localization of myosin Va in the adult rat brain
    • Tilelli C.Q., Martins A.R., Larson R.E., and Garcia-Cairasco N. Immunohistochemical localization of myosin Va in the adult rat brain. Neuroscience 121 (2003) 573-586
    • (2003) Neuroscience , vol.121 , pp. 573-586
    • Tilelli, C.Q.1    Martins, A.R.2    Larson, R.E.3    Garcia-Cairasco, N.4
  • 48
    • 26244444203 scopus 로고    scopus 로고
    • Myosin Va is required for neurotransmitter release during basal synaptic transmission and synaptic plasticity
    • Trinchese F., Rao M., Peterhoff C., Kumar A., Liu S., Nixon R., and Arancio O. Myosin Va is required for neurotransmitter release during basal synaptic transmission and synaptic plasticity. Mol. Biol. Cell 14 (2003) 179a
    • (2003) Mol. Biol. Cell , vol.14
    • Trinchese, F.1    Rao, M.2    Peterhoff, C.3    Kumar, A.4    Liu, S.5    Nixon, R.6    Arancio, O.7
  • 49
    • 0037155602 scopus 로고    scopus 로고
    • Neuronal calcium sensor 1 and activity-dependent facilitation of P/Q-type calcium currents at presynaptic nerve terminals
    • Tsujimoto T., Jeromin A., Saitoh N., Roder J.C., and Takahashi T. Neuronal calcium sensor 1 and activity-dependent facilitation of P/Q-type calcium currents at presynaptic nerve terminals. Science 295 (2002) 2276-2279
    • (2002) Science , vol.295 , pp. 2276-2279
    • Tsujimoto, T.1    Jeromin, A.2    Saitoh, N.3    Roder, J.C.4    Takahashi, T.5
  • 50
    • 0037459061 scopus 로고    scopus 로고
    • The molecular motor toolbox for intracellular transport
    • Vale R.D. The molecular motor toolbox for intracellular transport. Cell 112 (2003) 467-480
    • (2003) Cell , vol.112 , pp. 467-480
    • Vale, R.D.1
  • 51
    • 33846785411 scopus 로고    scopus 로고
    • 2+ channels determines fast neurotransmitter release
    • 2+ channels determines fast neurotransmitter release. Neuron 53 (2007) 563-575
    • (2007) Neuron , vol.53 , pp. 563-575
    • Wadel, K.1    Neher, E.2    Sakaba, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.