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Volumn 52, Issue 3, 2006, Pages 485-496

The TRPM7 Ion Channel Functions in Cholinergic Synaptic Vesicles and Affects Transmitter Release

Author keywords

CELLBIO; MOLNEURO

Indexed keywords

ACETYLCHOLINE; ION CHANNEL; SYNAPSIN I; SYNAPTOTAGMIN; TRANSIENT RECEPTOR POTENTIAL CHANNEL; TRPM7 ION CHANNEL; UNCLASSIFIED DRUG;

EID: 33750515856     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuron.2006.09.033     Document Type: Article
Times cited : (168)

References (50)
  • 1
    • 0015468228 scopus 로고
    • Autonomic neuromuscular transmission
    • Bennett M.R. Autonomic neuromuscular transmission. Monogr. Physiol. Soc. 30 (1972) 1-271
    • (1972) Monogr. Physiol. Soc. , vol.30 , pp. 1-271
    • Bennett, M.R.1
  • 3
    • 0020679244 scopus 로고
    • Morphological studies of synapses and varicosities in dissociated cell cultures of sympathetic neurons
    • Buckley K.M., and Landis S.C. Morphological studies of synapses and varicosities in dissociated cell cultures of sympathetic neurons. J. Neurocytol. 12 (1983) 67-92
    • (1983) J. Neurocytol. , vol.12 , pp. 67-92
    • Buckley, K.M.1    Landis, S.C.2
  • 4
    • 0036542593 scopus 로고    scopus 로고
    • Splitting the quantum: regulation of quantal release during vesicle fusion
    • Burgoyne R.D., and Barclay J.W. Splitting the quantum: regulation of quantal release during vesicle fusion. Trends Neurosci. 25 (2002) 176-178
    • (2002) Trends Neurosci. , vol.25 , pp. 176-178
    • Burgoyne, R.D.1    Barclay, J.W.2
  • 5
    • 0142138839 scopus 로고    scopus 로고
    • Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells
    • Buxton P., Zhang X.M., Walsh B., Sriratana A., Schenberg I., Manickam E., and Rowe T. Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells. Biochem. J. 375 (2003) 433-440
    • (2003) Biochem. J. , vol.375 , pp. 433-440
    • Buxton, P.1    Zhang, X.M.2    Walsh, B.3    Sriratana, A.4    Schenberg, I.5    Manickam, E.6    Rowe, T.7
  • 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
  • 7
  • 8
    • 0035071322 scopus 로고    scopus 로고
    • Phosphorylation of snapin by PKA modulates its interaction with the SNARE complex
    • Chheda M.G., Ashery U., Thakur P., Rettig J., and Sheng Z.H. Phosphorylation of snapin by PKA modulates its interaction with the SNARE complex. Nat. Cell Biol. 3 (2001) 331-338
    • (2001) Nat. Cell Biol. , vol.3 , pp. 331-338
    • Chheda, M.G.1    Ashery, U.2    Thakur, P.3    Rettig, J.4    Sheng, Z.H.5
  • 9
    • 0035195395 scopus 로고    scopus 로고
    • Synapsin dispersion and reclustering during synaptic activity
    • Chi P., Greengard P., and Ryan T.A. Synapsin dispersion and reclustering during synaptic activity. Nat. Neurosci. 4 (2001) 1187-1193
    • (2001) Nat. Neurosci. , vol.4 , pp. 1187-1193
    • Chi, P.1    Greengard, P.2    Ryan, T.A.3
  • 10
    • 0347504835 scopus 로고    scopus 로고
    • TRP channels as cellular sensors
    • Clapham D.E. TRP channels as cellular sensors. Nature 426 (2003) 517-524
    • (2003) Nature , vol.426 , pp. 517-524
    • Clapham, D.E.1
  • 11
    • 77049173124 scopus 로고
    • Quantal components of the end-plate potential
    • Del Castillo J., and Katz B. Quantal components of the end-plate potential. J. Physiol. 124 (1954) 560-573
    • (1954) J. Physiol. , vol.124 , pp. 560-573
    • Del Castillo, J.1    Katz, B.2
  • 13
    • 0031034162 scopus 로고    scopus 로고
    • GIRK1 immunoreactivity is present predominantly in dendrites, dendritic spines, and somata in the CA1 region of the hippocampus
    • Drake C.T., Bausch S.B., Milner T.A., and Chavkin C. GIRK1 immunoreactivity is present predominantly in dendrites, dendritic spines, and somata in the CA1 region of the hippocampus. Proc. Natl. Acad. Sci. USA 94 (1997) 1007-1012
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1007-1012
    • Drake, C.T.1    Bausch, S.B.2    Milner, T.A.3    Chavkin, C.4
  • 15
    • 0020007085 scopus 로고
    • 31P-NMR analysis of synaptic vesicles. Status of ATP and internal pH
    • Fuldner H.H., and Stadler H. 31P-NMR analysis of synaptic vesicles. Status of ATP and internal pH. Eur. J. Biochem. 121 (1982) 519-524
    • (1982) Eur. J. Biochem. , vol.121 , pp. 519-524
    • Fuldner, H.H.1    Stadler, H.2
  • 17
    • 0028708598 scopus 로고
    • Synapsin I, an actin-binding protein regulating synaptic vesicle traffic in the nerve terminal
    • Greengard P., Benfenati F., and Valtorta F. Synapsin I, an actin-binding protein regulating synaptic vesicle traffic in the nerve terminal. Adv. Second Messenger Phosphoprotein Res. 29 (1994) 31-45
    • (1994) Adv. Second Messenger Phosphoprotein Res. , vol.29 , pp. 31-45
    • Greengard, P.1    Benfenati, F.2    Valtorta, F.3
  • 18
    • 0034625410 scopus 로고    scopus 로고
    • A pleckstrin homology domain specific for phosphatidylinositol 4, 5-bisphosphate (PtdIns-4,5-P2) and fused to green fluorescent protein identifies plasma membrane PtdIns-4,5-P2 as being important in exocytosis
    • Holz R.W., Hlubek M.D., Sorensen S.D., Fisher S.K., Balla T., Ozaki S., Prestwich G.D., Stuenkel E.L., and Bittner M.A. A pleckstrin homology domain specific for phosphatidylinositol 4, 5-bisphosphate (PtdIns-4,5-P2) and fused to green fluorescent protein identifies plasma membrane PtdIns-4,5-P2 as being important in exocytosis. J. Biol. Chem. 275 (2000) 17878-17885
    • (2000) J. Biol. Chem. , vol.275 , pp. 17878-17885
    • Holz, R.W.1    Hlubek, M.D.2    Sorensen, S.D.3    Fisher, S.K.4    Balla, T.5    Ozaki, S.6    Prestwich, G.D.7    Stuenkel, E.L.8    Bittner, M.A.9
  • 19
    • 0033366466 scopus 로고    scopus 로고
    • Snapin: a SNARE-associated protein implicated in synaptic transmission
    • Ilardi J.M., Mochida S., and Sheng Z.H. Snapin: a SNARE-associated protein implicated in synaptic transmission. Nat. Neurosci. 2 (1999) 119-124
    • (1999) Nat. Neurosci. , vol.2 , pp. 119-124
    • Ilardi, J.M.1    Mochida, S.2    Sheng, Z.H.3
  • 20
    • 0034753208 scopus 로고    scopus 로고
    • Neurotransmitter release mechanisms in sympathetic neurons: past, present, and future perspectives
    • Jackson V.M., and Cunnane T.C. Neurotransmitter release mechanisms in sympathetic neurons: past, present, and future perspectives. Neurochem. Res. 26 (2001) 875-889
    • (2001) Neurochem. Res. , vol.26 , pp. 875-889
    • Jackson, V.M.1    Cunnane, T.C.2
  • 22
    • 23744484892 scopus 로고    scopus 로고
    • Potentiation of TRPM7 inward currents by protons
    • 10.1085/jgp.200409185 Published online July 11, 2005
    • Jiang J., Li M., and Yue L. Potentiation of TRPM7 inward currents by protons. J. Gen. Physiol. 126 (2005) 137-150 10.1085/jgp.200409185 Published online July 11, 2005
    • (2005) J. Gen. Physiol. , vol.126 , pp. 137-150
    • Jiang, J.1    Li, M.2    Yue, L.3
  • 23
    • 0030028238 scopus 로고    scopus 로고
    • Ion channels from synaptic vesicle membrane fragments reconstituted into lipid bilayers
    • Kelly M.L., and Woodbury D.J. Ion channels from synaptic vesicle membrane fragments reconstituted into lipid bilayers. Biophys. J. 70 (1996) 2593-2599
    • (1996) Biophys. J. , vol.70 , pp. 2593-2599
    • Kelly, M.L.1    Woodbury, D.J.2
  • 24
    • 18744363612 scopus 로고    scopus 로고
    • Identification and characterization of the single channel function of human mucolipin-1 implicated in mucolipidosis type IV, a disorder affecting the lysosomal pathway
    • LaPlante J.M., Falardeau J., Sun M., Kanazirska M., Brown E.M., Slaugenhaupt S.A., and Vassilev P.M. Identification and characterization of the single channel function of human mucolipin-1 implicated in mucolipidosis type IV, a disorder affecting the lysosomal pathway. FEBS Lett. 532 (2002) 183-187
    • (2002) FEBS Lett. , vol.532 , pp. 183-187
    • LaPlante, J.M.1    Falardeau, J.2    Sun, M.3    Kanazirska, M.4    Brown, E.M.5    Slaugenhaupt, S.A.6    Vassilev, P.M.7
  • 25
    • 0034104240 scopus 로고    scopus 로고
    • Nerve growth factor collaborates with myocyte-derived factors to promote development of presynaptic sites in cultured sympathetic neurons
    • Lockhart S.T., Mead J.N., Pisano J.M., Slonimsky J.D., and Birren S.J. Nerve growth factor collaborates with myocyte-derived factors to promote development of presynaptic sites in cultured sympathetic neurons. J. Neurobiol. 42 (2000) 460-476
    • (2000) J. Neurobiol. , vol.42 , pp. 460-476
    • Lockhart, S.T.1    Mead, J.N.2    Pisano, J.M.3    Slonimsky, J.D.4    Birren, S.J.5
  • 26
    • 4344620485 scopus 로고    scopus 로고
    • Culturing mammalian sympathoadrenal derivatives
    • Banker G., and Goslin K. (Eds), Bradford Book, Cambridge, MA
    • Mahanthappa N.K., and Patterson P.H. Culturing mammalian sympathoadrenal derivatives. In: Banker G., and Goslin K. (Eds). Culturing Nerve Cells. Second Edition (2002), Bradford Book, Cambridge, MA 289-308
    • (2002) Culturing Nerve Cells. Second Edition , pp. 289-308
    • Mahanthappa, N.K.1    Patterson, P.H.2
  • 27
    • 0035939659 scopus 로고    scopus 로고
    • Regulation of presynaptic phosphatidylinositol 4,5-biphosphate by neuronal activity
    • Micheva K.D., Holz R.W., and Smith S.J. Regulation of presynaptic phosphatidylinositol 4,5-biphosphate by neuronal activity. J. Cell Biol. 154 (2001) 355-368
    • (2001) J. Cell Biol. , vol.154 , pp. 355-368
    • Micheva, K.D.1    Holz, R.W.2    Smith, S.J.3
  • 28
    • 0027971025 scopus 로고
    • Analysis of the mechanism for acetylcholine release at the synapse formed between rat sympathetic neurons in culture
    • Mochida S., Nonomura Y., and Kobayashi H. Analysis of the mechanism for acetylcholine release at the synapse formed between rat sympathetic neurons in culture. Microsc. Res. Tech. 29 (1994) 94-102
    • (1994) Microsc. Res. Tech. , vol.29 , pp. 94-102
    • Mochida, S.1    Nonomura, Y.2    Kobayashi, H.3
  • 30
    • 0344431635 scopus 로고    scopus 로고
    • Subtype-selective reconstitution of synaptic transmission in sympathetic ganglion neurons by expression of exogenous calcium channels
    • Mochida S., Westenbroek R.E., Yokoyama C.T., Itoh K., and Catterall W.A. Subtype-selective reconstitution of synaptic transmission in sympathetic ganglion neurons by expression of exogenous calcium channels. Proc. Natl. Acad. Sci. USA 100 (2003) 2813-2818
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2813-2818
    • Mochida, S.1    Westenbroek, R.E.2    Yokoyama, C.T.3    Itoh, K.4    Catterall, W.A.5
  • 31
    • 2942614748 scopus 로고    scopus 로고
    • Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity
    • Morenilla-Palao C., Planells-Cases R., Garcia-Sanz N., and Ferrer-Montiel A. Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity. J. Biol. Chem. 279 (2004) 25665-25672
    • (2004) J. Biol. Chem. , vol.279 , pp. 25665-25672
    • Morenilla-Palao, C.1    Planells-Cases, R.2    Garcia-Sanz, N.3    Ferrer-Montiel, A.4
  • 32
    • 0027516245 scopus 로고
    • The secretory granule matrix: a fast-acting smart polymer
    • Nanavati C., and Fernandez J.M. The secretory granule matrix: a fast-acting smart polymer. Science 259 (1993) 963-965
    • (1993) Science , vol.259 , pp. 963-965
    • Nanavati, C.1    Fernandez, J.M.2
  • 33
    • 0034934074 scopus 로고    scopus 로고
    • A TRP homolog in Saccharomyces cerevisiae forms an intracellular Ca(2+)-permeable channel in the yeast vacuolar membrane
    • Palmer C.P., Zhou X.L., Lin J., Loukin S.H., Kung C., and Saimi Y. A TRP homolog in Saccharomyces cerevisiae forms an intracellular Ca(2+)-permeable channel in the yeast vacuolar membrane. Proc. Natl. Acad. Sci. USA 98 (2001) 7801-7805
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7801-7805
    • Palmer, C.P.1    Zhou, X.L.2    Lin, J.3    Loukin, S.H.4    Kung, C.5    Saimi, Y.6
  • 34
    • 2442542273 scopus 로고    scopus 로고
    • Postfusional control of quantal current shape
    • Pawlu C., DiAntonio A., and Heckmann M. Postfusional control of quantal current shape. Neuron 42 (2004) 607-618
    • (2004) Neuron , vol.42 , pp. 607-618
    • Pawlu, C.1    DiAntonio, A.2    Heckmann, M.3
  • 35
    • 0001956792 scopus 로고    scopus 로고
    • Isolation of synaptosomes, growth cones and their subcellular components
    • Turner A.J., and Bachelard H.S. (Eds), IRL Press, Oxford, New York, Tokyo
    • Phelan P., and Gordon-Weeks P.R. Isolation of synaptosomes, growth cones and their subcellular components. In: Turner A.J., and Bachelard H.S. (Eds). Neurochemistry, A Practical Approach, Second Edition (1997), IRL Press, Oxford, New York, Tokyo 27-33
    • (1997) Neurochemistry, A Practical Approach, Second Edition , pp. 27-33
    • Phelan, P.1    Gordon-Weeks, P.R.2
  • 36
    • 0031035397 scopus 로고    scopus 로고
    • Pre- and postfusion regulation of transmitter release
    • Rahamimoff R., and Fernandez J.M. Pre- and postfusion regulation of transmitter release. Neuron 18 (1997) 17-27
    • (1997) Neuron , vol.18 , pp. 17-27
    • Rahamimoff, R.1    Fernandez, J.M.2
  • 40
    • 0036092076 scopus 로고    scopus 로고
    • The TRPM7 channel is inactivated by PIP(2) hydrolysis
    • Runnels L.W., Yue L., and Clapham D.E. The TRPM7 channel is inactivated by PIP(2) hydrolysis. Nat. Cell Biol. 4 (2002) 329-336
    • (2002) Nat. Cell Biol. , vol.4 , pp. 329-336
    • Runnels, L.W.1    Yue, L.2    Clapham, D.E.3
  • 43
    • 0037040890 scopus 로고    scopus 로고
    • Synaptotagmins: why so many?
    • 10.1074/jbc.R100052200 Published online December 5, 2001
    • Sudhof T.C. Synaptotagmins: why so many?. J. Biol. Chem. 277 (2002) 7629-7632 10.1074/jbc.R100052200 Published online December 5, 2001
    • (2002) J. Biol. Chem. , vol.277 , pp. 7629-7632
    • Sudhof, T.C.1
  • 44
    • 2942556680 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • Sudhof T.C. The synaptic vesicle cycle. Annu. Rev. Neurosci. 27 (2004) 509-547
    • (2004) Annu. Rev. Neurosci. , vol.27 , pp. 509-547
    • Sudhof, T.C.1
  • 45
    • 3242747322 scopus 로고    scopus 로고
    • Effects of PKA-mediated phosphorylation of Snapin on synaptic transmission in cultured hippocampal neurons
    • Thakur P., Stevens D.R., Sheng Z.H., and Rettig J. Effects of PKA-mediated phosphorylation of Snapin on synaptic transmission in cultured hippocampal neurons. J. Neurosci. 24 (2004) 6476-6481
    • (2004) J. Neurosci. , vol.24 , pp. 6476-6481
    • Thakur, P.1    Stevens, D.R.2    Sheng, Z.H.3    Rettig, J.4
  • 46
    • 0036720536 scopus 로고    scopus 로고
    • Ion channels in secretory granules of the pancreas and their role in exocytosis and release of secretory proteins
    • Thevenod F. Ion channels in secretory granules of the pancreas and their role in exocytosis and release of secretory proteins. Am. J. Physiol. Cell Physiol. 283 (2002) C651-C672
    • (2002) Am. J. Physiol. Cell Physiol. , vol.283
    • Thevenod, F.1
  • 47
    • 0024356254 scopus 로고
    • Intracellular ion exchange between cytoplasmic potassium and granule histamine, an integrated link in the histamine release machinery of mast cells
    • Uvnas B., Aborg C.H., Lyssarides L., and Danielsson L.G. Intracellular ion exchange between cytoplasmic potassium and granule histamine, an integrated link in the histamine release machinery of mast cells. Acta Physiol. Scand. 136 (1989) 309-320
    • (1989) Acta Physiol. Scand. , vol.136 , pp. 309-320
    • Uvnas, B.1    Aborg, C.H.2    Lyssarides, L.3    Danielsson, L.G.4
  • 48
    • 2942750191 scopus 로고    scopus 로고
    • Reinvestigation of the role of snapin in neurotransmitter release
    • 10.1074/jbc.M404079200 Published online April 14, 2004
    • Vites O., Rhee J.S., Schwarz M., Rosenmund C., and Jahn R. Reinvestigation of the role of snapin in neurotransmitter release. J. Biol. Chem. 279 (2004) 26251-26256 10.1074/jbc.M404079200 Published online April 14, 2004
    • (2004) J. Biol. Chem. , vol.279 , pp. 26251-26256
    • Vites, O.1    Rhee, J.S.2    Schwarz, M.3    Rosenmund, C.4    Jahn, R.5
  • 49
    • 0029067937 scopus 로고
    • The non-specific ion channel in Torpedo ocellata fused synaptic vesicles
    • Yakir N., and Rahamimoff R. The non-specific ion channel in Torpedo ocellata fused synaptic vesicles. J. Physiol. 485 (1995) 683-697
    • (1995) J. Physiol. , vol.485 , pp. 683-697
    • Yakir, N.1    Rahamimoff, R.2
  • 50
    • 0029082282 scopus 로고
    • Amperometric detection of stimulus-induced quantal release of catecholamines from cultured superior cervical ganglion neurons
    • Zhou Z., and Misler S. Amperometric detection of stimulus-induced quantal release of catecholamines from cultured superior cervical ganglion neurons. Proc. Natl. Acad. Sci. USA 92 (1995) 6938-6942
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6938-6942
    • Zhou, Z.1    Misler, S.2


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