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Volumn 486, Issue 7401, 2012, Pages 122-125

α2δ expression sets presynaptic calcium channel abundance and release probability

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CALCIUM; CHAPERONE; GABAPENTIN; METAL ION DEPENDENT ADHESION SITE; PREGABALIN; UNCLASSIFIED DRUG; VOLTAGE GATED CALCIUM CHANNEL; VON WILLEBRAND FACTOR;

EID: 84861947988     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature11033     Document Type: Article
Times cited : (299)

References (34)
  • 1
    • 0016989744 scopus 로고
    • Presynaptic calcium currents and their relation to synaptic transmission: Voltage clamp study in squid giant synapse and theoretical model for the calcium gate
    • Llinás, R., Steinberg, I. Z. & Walton, K. Presynaptic calcium currents and their relation to synaptic transmission: voltage clamp study in squid giant synapse and theoretical model for the calcium gate. Proc. Natl Acad. Sci. USA 73, 2918-2922 (1976).
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 2918-2922
    • Llinás, R.1    Steinberg, I.Z.2    Walton, K.3
  • 2
    • 52049106127 scopus 로고    scopus 로고
    • Multiple roles of calcium ions in the regulation of neurotransmitter release
    • Neher, E. & Sakaba, T. Multiple roles of calcium ions in the regulation of neurotransmitter release. Neuron 59, 861-872 (2008).
    • (2008) Neuron , vol.59 , pp. 861-872
    • Neher, E.1    Sakaba, T.2
  • 3
    • 76549117726 scopus 로고    scopus 로고
    • The a2d subunits of voltage-gated calcium channels form GPIanchored proteins, a posttranslational modification essential for function
    • Davies, A. et al. The a2d subunits of voltage-gated calcium channels form GPIanchored proteins, a posttranslational modification essential for function. Proc. Natl Acad. Sci. USA 107, 1654-1659 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 1654-1659
    • Davies, A.1
  • 4
    • 33751232667 scopus 로고    scopus 로고
    • Identification of the a2-d-1 subunit of voltage-dependent calcium channels as a molecular target for pain mediating the analgesic actions of pregabalin
    • Field, M. J. et al. Identification of the a2-d-1 subunit of voltage-dependent calcium channels as a molecular target for pain mediating the analgesic actions of pregabalin. Proc. Natl Acad. Sci. USA 103, 17537-17542 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 17537-17542
    • Field, M.J.1
  • 5
    • 0033198905 scopus 로고    scopus 로고
    • Structural requirement of the calciumchannel subunit a2d for gabapentin binding
    • Wang, M., Offord, J., Oxender, D. L.&Su, T. Z. Structural requirement of the calciumchannel subunit a2d for gabapentin binding. Biochem. J. 342, 313-320 (1999).
    • (1999) Biochem. J. , vol.342 , pp. 313-320
    • Wang, M.1    Offord, J.2    Oxender, D.L.3    Su, T.Z.4
  • 6
    • 78149472321 scopus 로고    scopus 로고
    • A genome-wide Drosophila screen for heat nociception identifies a2d3 as an evolutionarily conserved pain gene
    • Neely, G. G. et al. A genome-wide Drosophila screen for heat nociception identifies a2d3 as an evolutionarily conserved pain gene. Cell 143, 628-638 (2010).
    • (2010) Cell , vol.143 , pp. 628-638
    • Neely, G.G.1
  • 7
    • 0034697135 scopus 로고    scopus 로고
    • Functional properties of a new voltage-dependent calcium channel a2d auxiliary subunit gene (CACNA2D2)
    • Gao, B. et al. Functional properties of a new voltage-dependent calcium channel a2d auxiliary subunit gene (CACNA2D2). J. Biol.Chem.275, 12237-12242(2000).
    • (2000) J. Biol.Chem. , vol.275 , pp. 12237-12242
    • Gao, B.1
  • 8
    • 0038045158 scopus 로고    scopus 로고
    • Auxiliary subunits: Essential components of the voltage-gated calcium channel complex
    • Arikkath, J. & Campbell, K. P. Auxiliary subunits: essential components of the voltage-gated calcium channel complex. Curr. Opin. Neurobiol. 13, 298-307 (2003).
    • (2003) Curr. Opin. Neurobiol. , vol.13 , pp. 298-307
    • Arikkath, J.1    Campbell, K.P.2
  • 9
    • 0034518423 scopus 로고    scopus 로고
    • Structureandregulation of voltage-gated Ca21 channels
    • Catterall, W. A. Structureandregulation of voltage-gated Ca21 channels. Annu. Rev. Cell Dev. Biol. 16, 521-555 (2000).
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 521-555
    • Catterall, W.A.1
  • 10
    • 0028985125 scopus 로고
    • Exocytotic Ca21 channels in mammalian central neurons
    • Dunlap, K., Luebke, J. I. & Turner, T. J. Exocytotic Ca21 channels in mammalian central neurons. Trends Neurosci. 18, 89-98 (1995).
    • (1995) Trends Neurosci. , vol.18 , pp. 89-98
    • Dunlap, K.1    Luebke, J.I.2    Turner, T.J.3
  • 11
    • 4043126769 scopus 로고    scopus 로고
    • Presynaptic Ca21 channels compete for channel type-preferring slots in altered neurotransmission arising from Ca21 channelopathy
    • Cao, Y. Q. et al. Presynaptic Ca21 channels compete for channel type-preferring slots in altered neurotransmission arising from Ca21 channelopathy. Neuron 43, 387-400 (2004).
    • (2004) Neuron , vol.43 , pp. 387-400
    • Cao, Y.Q.1
  • 12
    • 64149110842 scopus 로고    scopus 로고
    • Functional properties and modulation of extracellular epitope-tagged CaV2.1 voltage-gated calcium channels
    • Watschinger, K. et al. Functional properties and modulation of extracellular epitope-tagged CaV2.1 voltage-gated calcium channels. Channels 2, 461-473 (2008).
    • (2008) Channels , vol.2 , pp. 461-473
    • Watschinger, K.1
  • 13
    • 0033767401 scopus 로고    scopus 로고
    • A hot spot for the interaction of gating modifier toxins with voltage-dependent ion channels
    • Winterfield, J. R. & Swartz, K. J. A hot spot for the interaction of gating modifier toxins with voltage-dependent ion channels. J. Gen. Physiol. 116, 637-644 (2000).
    • (2000) J. Gen. Physiol. , vol.116 , pp. 637-644
    • Winterfield, J.R.1    Swartz, K.J.2
  • 14
    • 68649099001 scopus 로고    scopus 로고
    • Calcium channel diversity: Multiple roles of calcium channel subunits
    • Dolphin, A. C. Calcium channel diversity: multiple roles of calcium channel subunits. Curr. Opin. Neurobiol. 19, 237-244 (2009).
    • (2009) Curr. Opin. Neurobiol. , vol.19 , pp. 237-244
    • Dolphin, A.C.1
  • 15
    • 0028179146 scopus 로고
    • Calciumchannel b-subunit binds to a conserved motif in the I-II cytoplasmic linker of the a1-subunit
    • Pragnell, M. et al. Calciumchannel b-subunit binds to a conserved motif in the I-II cytoplasmic linker of the a1-subunit. Nature 368, 67-70 (1994).
    • (1994) Nature , vol.368 , pp. 67-70
    • Pragnell, M.1
  • 16
    • 0036542627 scopus 로고    scopus 로고
    • Vesicle pools and short-termsynaptic depression: Lessons from a large synapse
    • Schneggenburger, R., Sakaba, T.& Neher, E. Vesicle pools and short-termsynaptic depression: lessons from a large synapse. Trends Neurosci. 25, 206-212 (2002).
    • (2002) Trends Neurosci. , vol.25 , pp. 206-212
    • Schneggenburger, R.1    Sakaba, T.2    Neher, E.3
  • 17
    • 84856806024 scopus 로고    scopus 로고
    • Optical mapping of release properties in synapses
    • Ariel, P. & Ryan, T. A. Optical mapping of release properties in synapses. Front. Neural Circuits 4, 18 (2010).
    • (2010) Front. Neural Circuits , vol.4 , pp. 18
    • Ariel, P.1    Ryan, T.A.2
  • 18
    • 52049098700 scopus 로고    scopus 로고
    • Calciumchannel regulation and presynaptic plasticity
    • Catterall, W. A. & Few, A. P. Calciumchannel regulation and presynaptic plasticity. Neuron 59, 882-901 (2008).
    • (2008) Neuron , vol.59 , pp. 882-901
    • Catterall, W.A.1    Few, A.P.2
  • 19
    • 73349108496 scopus 로고    scopus 로고
    • Imaging neural activity inworms flies and mice withimprovedGCaMP calcium indicators
    • Tian, L. et al.Imaging neural activity inworms, flies and mice withimprovedGCaMP calcium indicators. Nature Methods 6, 875-881 (2009).
    • (2009) Nature Methods , vol.6 , pp. 875-881
    • Tian, L.1
  • 20
    • 0014154913 scopus 로고
    • Co-operative action a calciumions in transmitter release at the neuromuscular junction
    • Dodge, F. A. Jr & Rahamimoff, R. Co-operative action a calciumions in transmitter release at the neuromuscular junction. J. Physiol. (Lond.) 193, 419-432 (1967).
    • (1967) J. Physiol. (Lond.) , vol.193 , pp. 419-432
    • Dodge Jr., F.A.1    Rahamimoff, R.2
  • 21
    • 47249152762 scopus 로고    scopus 로고
    • Ca21 microdomains near plasmamembrane Ca21 channels: Impact on cell function
    • Parekh, A. B. Ca21 microdomains near plasmamembrane Ca21 channels: impact on cell function. J. Physiol. (Lond.) 586, 3043-3054 (2008).
    • (2008) J. Physiol. (Lond.) , vol.586 , pp. 3043-3054
    • Parekh, A.B.1
  • 22
    • 23844500323 scopus 로고    scopus 로고
    • Themetal-ion-dependent adhesion site in the von Willebrand factor-A domain of a2d subunits is key to trafficking voltage-gated Ca21 channels
    • Cant́, C. et al. Themetal-ion-dependent adhesion site in the Von Willebrand factor-A domain of a2d subunits is key to trafficking voltage-gated Ca21 channels. Proc. Natl Acad. Sci. USA 102, 11230-11235 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 11230-11235
    • Cant́, C.1
  • 23
    • 33846213195 scopus 로고    scopus 로고
    • Complement and the multifaceted functions of VWA and integrin i domains
    • Springer, T. A. Complement and the multifaceted functions of VWA and integrin I domains. Structure 14, 1611-1616 (2006).
    • (2006) Structure , vol.14 , pp. 1611-1616
    • Springer, T.A.1
  • 24
    • 2342454381 scopus 로고    scopus 로고
    • Crystal structure of the von Willebrand factor A domain of human capillary morphogenesis protein 2: An anthrax toxin receptor
    • Lacy, D. B., Wigelsworth, D. J., Scobie, H. M., Young, J. A. & Collier, R. J. Crystal structure of the von Willebrand factor A domain of human capillary morphogenesis protein 2: an anthrax toxin receptor. Proc. Natl Acad. Sci. USA 101, 6367-6372 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 6367-6372
    • Lacy, D.B.1    Wigelsworth, D.J.2    Scobie, H.M.3    Young, J.A.4    Collier, R.J.5
  • 25
    • 0036796740 scopus 로고    scopus 로고
    • Distribution and evolution of von Willebrand/integrin A domains: Widely dispersed domains with roles in cell adhesion and elsewhere
    • Whittaker, C. A. & Hynes, R. O. Distribution and evolution of von Willebrand/integrin A domains: widely dispersed domains with roles in cell adhesion and elsewhere. Mol. Biol. Cell 13, 3369-3387 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3369-3387
    • Whittaker, C.A.1    Hynes, R.O.2
  • 26
    • 33748275476 scopus 로고    scopus 로고
    • The calciumchannel a2d-2 subunit partitions with CaV2.1 into lipid rafts in cerebellum: Implications for localization and function
    • Davies, A. et al. The calciumchannel a2d-2 subunit partitions with CaV2.1 into lipid rafts in cerebellum: implications for localization and function. J. Neurosci. 26, 8748-8757 (2006).
    • (2006) J. Neurosci. , vol.26 , pp. 8748-8757
    • Davies, A.1
  • 27
    • 13844294230 scopus 로고    scopus 로고
    • Gabapentin fails to alter P/Q-type Ca21 channelmediated synaptic transmission in the hippocampus in vitro
    • Brown, J. T. & Randall, A. Gabapentin fails to alter P/Q-type Ca21 channelmediated synaptic transmission in the hippocampus in vitro. Synapse 55, 262-269 (2005).
    • (2005) Synapse , vol.55 , pp. 262-269
    • Brown, J.T.1    Randall, A.2
  • 28
    • 77957193042 scopus 로고    scopus 로고
    • The a2d ligand gabapentin inhibits the Rab11-dependent recycling of the calcium channel subunit a2d-2
    • Tran-Van-Minh, A. & Dolphin, A. C. The a2d ligand gabapentin inhibits the Rab11-dependent recycling of the calcium channel subunit a2d-2. J. Neurosci. 30, 12856-12867 (2010).
    • (2010) J. Neurosci. , vol.30 , pp. 12856-12867
    • Tran-Van-Minh, A.1    Dolphin, A.C.2
  • 29
    • 72449126550 scopus 로고    scopus 로고
    • Presynaptic a2d-3 is required for synaptic morphogenesis independent of its Ca21-channel functions
    • Kurshan, P. T., Oztan, A.& Schwarz, T. L. Presynaptic a2d-3 is required for synaptic morphogenesis independent of its Ca21-channel functions. Nature Neurosci. 12, 1415-1423 (2009).
    • (2009) Nature Neurosci. , vol.12 , pp. 1415-1423
    • Kurshan, P.T.1    Oztan, A.2    Schwarz, T.L.3
  • 30
    • 77956314453 scopus 로고    scopus 로고
    • CDK5 serves as a major control point in neurotransmitter release
    • Kim, S. H. & Ryan, T. A. CDK5 serves as a major control point in neurotransmitter release. Neuron 67, 797-809 (2010).
    • (2010) Neuron , vol.67 , pp. 797-809
    • Kim, S.H.1    Ryan, T.A.2
  • 31
    • 0032500053 scopus 로고    scopus 로고
    • Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins
    • Miesenböck, G., De Angelis, D. A. & Rothman, J. E. Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins. Nature 394, 192-195 (1998).
    • (1998) Nature , vol.394 , pp. 192-195
    • Miesenböck, G.1    De Angelis, D.A.2    Rothman, J.E.3
  • 32
    • 33745494172 scopus 로고    scopus 로고
    • Distinct endocytic pathways control the rate and extent of synaptic vesicle protein recycling
    • Voglmaier, S. M. et al. Distinct endocytic pathways control the rate and extent of synaptic vesicle protein recycling. Neuron 51, 71-84 (2006).
    • (2006) Neuron , vol.51 , pp. 71-84
    • Voglmaier, S.M.1
  • 33
    • 44449109239 scopus 로고    scopus 로고
    • Improving the photostability of brightmonomeric orange and red fluorescent proteins
    • Shaner, N. C. et al. Improving the photostability of brightmonomeric orange and red fluorescent proteins. Nature Methods 5, 545-551 (2008).
    • (2008) Nature Methods , vol.5 , pp. 545-551
    • Shaner, N.C.1
  • 34
    • 4344662040 scopus 로고    scopus 로고
    • PI3K promotes voltage-dependent calcium channel trafficking to the plasma membrane
    • Viard, P. et al. PI3K promotes voltage-dependent calcium channel trafficking to the plasma membrane. Nature Neurosci. 7, 939-946 (2004).
    • (2004) Nature Neurosci. , vol.7 , pp. 939-946
    • Viard, P.1


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