메뉴 건너뛰기




Volumn 21, Issue 1, 1998, Pages 123-136

Munc13-1 is a presynaptic phorbol ester receptor that enhances neurotransmitter release

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; CAENORHABDITIS ELEGANS; DRUG RECEPTOR BINDING; ENDOCYTOSIS; LIGAND BINDING; NEUROMUSCULAR SYNAPSE; NEUROTRANSMITTER RELEASE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRESYNAPTIC MEMBRANE; PRIORITY JOURNAL; RAT; SECOND MESSENGER; SYNAPSE VESICLE; SYNAPTIC TRANSMISSION; TARGET CELL;

EID: 18544399674     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(00)80520-6     Document Type: Article
Times cited : (352)

References (51)
  • 1
    • 0026475394 scopus 로고
    • The caenorhabditis elegans unc-13 gene product is aphospholipid-dependent high-affinity phorbol ester receptor
    • Ahmed, S., Maruyama, I.N., Kozma, R., Lee, J., and Brenner, S. (1992). The Caenorhabditis elegans unc-13 gene product is aphospholipid-dependent high-affinity phorbol ester receptor. Biochem. J. 287, 995-999.
    • (1992) Biochem. J. , vol.287 , pp. 995-999
    • Ahmed, S.1    Maruyama, I.N.2    Kozma, R.3    Lee, J.4    Brenner, S.5
  • 2
    • 0028800496 scopus 로고
    • Overexpression of synaptophysin enhances neurotransmitter secretion at Xenopus neuromuscular synapses
    • Alder, J., Kanki, H., Valtorta, F., Greengard, P., and Poo, M.-M. (1995). Overexpression of synaptophysin enhances neurotransmitter secretion at Xenopus neuromuscular synapses. J. Neurosci. 15, 511-519.
    • (1995) J. Neurosci. , vol.15 , pp. 511-519
    • Alder, J.1    Kanki, H.2    Valtorta, F.3    Greengard, P.4    Poo, M.-M.5
  • 3
    • 0029814713 scopus 로고    scopus 로고
    • Mammalian unc-13 homologues as possible regulators of neurotransmitter release
    • Betz, A., Telemenakis, I., Hofmann, K., and Brose, N. (1996). Mammalian unc-13 homologues as possible regulators of neurotransmitter release. Biochem. Soc. Trans. 24, 661-666.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 661-666
    • Betz, A.1    Telemenakis, I.2    Hofmann, K.3    Brose, N.4
  • 4
    • 0031027591 scopus 로고    scopus 로고
    • Direct interaction of the rat unc-13 homologue Munc13-1 with the N-terminus of syntaxin
    • Betz, A., Okamoto, M., Benseler, F., and Brose, N. (1997). Direct interaction of the rat unc-13 homologue Munc13-1 with the N-terminus of syntaxin. J. Biol. Chem. 272, 2520-2526.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2520-2526
    • Betz, A.1    Okamoto, M.2    Benseler, F.3    Brose, N.4
  • 5
    • 0027490681 scopus 로고
    • Protein chemical characterization and immunocytochemical localization of the NMDA receptor subunit NMDA R1
    • Brose, N., Gasic, G.P., Vetter, D.E., Sullivan, J.M., and Heinemann, S.F. (1993). Protein chemical characterization and immunocytochemical localization of the NMDA receptor subunit NMDA R1. J. Biol. Chem. 268, 22663-22678.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22663-22678
    • Brose, N.1    Gasic, G.P.2    Vetter, D.E.3    Sullivan, J.M.4    Heinemann, S.F.5
  • 8
    • 0030065380 scopus 로고    scopus 로고
    • Presynaptic facilitation revisited: State and time dependence
    • Byrne, J.H., and Kandel, E.R. (1996). Presynaptic facilitation revisited: state and time dependence. J. Neurosci. 15, 425-435.
    • (1996) J. Neurosci. , vol.15 , pp. 425-435
    • Byrne, J.H.1    Kandel, E.R.2
  • 9
    • 0022997628 scopus 로고
    • Vesicle-containing dendrites in the nucleus raphedorsalis of the cat. A serial section electron microscopic analysis
    • Chazal, G., and Ohara, P.T. (1986). Vesicle-containing dendrites in the nucleus raphedorsalis of the cat. A serial section electron microscopic analysis. J. Neurocytol. 15, 777-787.
    • (1986) J. Neurocytol. , vol.15 , pp. 777-787
    • Chazal, G.1    Ohara, P.T.2
  • 10
    • 0023392945 scopus 로고
    • High efficiency transformation of mammalian cells by plasmid DNA
    • Chen, C., and Okayama, H. (1987). High efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell Biol. 7, 2745-2752.
    • (1987) Mol. Cell Biol. , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 13
    • 0026347085 scopus 로고
    • Transmitter release: Target of regulation by protein kinase C?
    • Dekker, L.V., De Graan, P.N.E., and Gispen, W.H. (1991). Transmitter release: target of regulation by protein kinase C? Progr. Brain Res. 89, 209-226.
    • (1991) Progr. Brain Res. , vol.89 , pp. 209-226
    • Dekker, L.V.1    De Graan, P.N.E.2    Gispen, W.H.3
  • 14
    • 0027967774 scopus 로고
    • Export of protein from the endoplasmatic reticulum is regulated by a diacylglycerol/ phorbol ester binding protein
    • Fabbri, M., Bannykh, S., and Balch, W.E. (1994). Export of protein from the endoplasmatic reticulum is regulated by a diacylglycerol/ phorbol ester binding protein. J. Biol. Chem. 269, 26848-26857.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26848-26857
    • Fabbri, M.1    Bannykh, S.2    Balch, W.E.3
  • 15
    • 0030176052 scopus 로고    scopus 로고
    • Protein kinase C enhances exocytosis from chromaffin cells by increasing the size of the readily releaseable pool of secretory granules
    • Gillis, K.D., Mößner, R., and Neher, E. (1996). Protein kinase C enhances exocytosis from chromaffin cells by increasing the size of the readily releaseable pool of secretory granules. Neuron 16, 1209-1220.
    • (1996) Neuron , vol.16 , pp. 1209-1220
    • Gillis, K.D.1    Mößner, R.2    Neher, E.3
  • 16
    • 0028588560 scopus 로고
    • Inhibitors of protein kinase C
    • Gordge, P.C., and Ryves, W.J. (1994). Inhibitors of protein kinase C. Cell. Signal. 6, 871-882.
    • (1994) Cell. Signal. , vol.6 , pp. 871-882
    • Gordge, P.C.1    Ryves, W.J.2
  • 17
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathion-S-transferase
    • Guan, K.L., and Dixon, J.E. (1991). Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathion-S-transferase. Anal. Biochem. 193, 262-267.
    • (1991) Anal. Biochem. , vol.193 , pp. 262-267
    • Guan, K.L.1    Dixon, J.E.2
  • 18
    • 0030846539 scopus 로고    scopus 로고
    • Neurotransmitter release - Four years of SNARE complexes
    • Hanson, P.I., Heuser, J.E., and Jahn, R. (1997a). Neurotransmitter release - four years of SNARE complexes. Curr. Opin. Neurobiol. 7, 310-315.
    • (1997) Curr. Opin. Neurobiol. , vol.7 , pp. 310-315
    • Hanson, P.I.1    Heuser, J.E.2    Jahn, R.3
  • 19
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson, P.I., Roth, R., Morisaki, H., Jahn, R., and Heuser, J.E. (1997b). Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90, 523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 20
    • 0030796026 scopus 로고    scopus 로고
    • SNAREs and NSF in targeted membrane fusion
    • Hay, J.C., and Scheller, R.H. (1997). SNAREs and NSF in targeted membrane fusion. Curr. Opin. Cell Biol. 9, 505-512.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 505-512
    • Hay, J.C.1    Scheller, R.H.2
  • 21
    • 0028447767 scopus 로고
    • Solution structure of acysteine rich domain of rat protein kinase C
    • Hommel, U., Zurini, M., and Luyten, M. (1994). Solution structure of acysteine rich domain of rat protein kinase C. Nat. Struct. Biol. 1, 383-387.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 383-387
    • Hommel, U.1    Zurini, M.2    Luyten, M.3
  • 22
    • 0025910348 scopus 로고
    • Additional genes which result in an elevation of acetylcholine levels by mutations in Caenorhabditis elegans
    • Hosono, R., and Kamiya, Y. (1991). Additional genes which result in an elevation of acetylcholine levels by mutations in Caenorhabditis elegans. Neurosci. Lett. 128, 243-244.
    • (1991) Neurosci. Lett. , vol.128 , pp. 243-244
    • Hosono, R.1    Kamiya, Y.2
  • 23
    • 0023616451 scopus 로고
    • Mutations affecting acetylcholine levels in the nematode Caenorhabditis elegans
    • Hosono, R., Sassa, T., and Kuno, S. (1987). Mutations affecting acetylcholine levels in the nematode Caenorhabditis elegans. J. Neurochem. 49, 1820-1823.
    • (1987) J. Neurochem. , vol.49 , pp. 1820-1823
    • Hosono, R.1    Sassa, T.2    Kuno, S.3
  • 25
    • 0028914673 scopus 로고
    • Characterization of the cysteine-rich region of the Caenorhabditis elegans protein Unc13 as a high affinity phorbol ester receptor
    • Kazanietz, M.G., Lewin, N.E., Bruns, J.D., and Blumberg, P.M. (1995). Characterization of the cysteine-rich region of the Caenorhabditis elegans protein Unc13 as a high affinity phorbol ester receptor. J. Biol. Chem. 270, 10777-10783.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10777-10783
    • Kazanietz, M.G.1    Lewin, N.E.2    Bruns, J.D.3    Blumberg, P.M.4
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0026053020 scopus 로고
    • A phorbol ester/diacylglycerol-binding protein encoded by the unc-73 gene of Caenorhabditis elegans
    • Maruyama, I.N., and Brenner, S. (1991). A phorbol ester/diacylglycerol-binding protein encoded by the unc-73 gene of Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA 88, 5729-5733.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5729-5733
    • Maruyama, I.N.1    Brenner, S.2
  • 28
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function, and regulation
    • Newton, A.C. (1995). Protein kinase C: structure, function, and regulation. J. Biol. Chem. 270, 28495-28498.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28495-28498
    • Newton, A.C.1
  • 29
    • 0030987070 scopus 로고    scopus 로고
    • Regulation of protein kinase C
    • Newton, A.C. (1997). Regulation of protein kinase C. Curr. Opin. Cell. Biol. 9, 161-167.
    • (1997) Curr. Opin. Cell. Biol. , vol.9 , pp. 161-167
    • Newton, A.C.1
  • 32
    • 0022360604 scopus 로고
    • The fine structural organization of tyrosinehydroxylase immunoreactive neurons in rat arcuate nucleus
    • Piotte, M., Beaudet, A., Joh, T.H., and Brawer, J.R. (1985). The fine structural organization of tyrosinehydroxylase immunoreactive neurons in rat arcuate nucleus. J. Comp. Neurol. 239, 44-53.
    • (1985) J. Comp. Neurol. , vol.239 , pp. 44-53
    • Piotte, M.1    Beaudet, A.2    Joh, T.H.3    Brawer, J.R.4
  • 33
    • 0029053739 scopus 로고
    • Regulation of substantia nigra dopamine neurons
    • Pucak, M.L., and Grace, A.A. (1994). Regulation of substantia nigra dopamine neurons. Grit. Rev. Neurobiol. 9, 67-89.
    • (1994) Grit. Rev. Neurobiol. , vol.9 , pp. 67-89
    • Pucak, M.L.1    Grace, A.A.2
  • 34
    • 0028021161 scopus 로고
    • The regulatory region of protein kinase Cγ
    • Quest, A.F.G., and Bell, R.M. (1994). The regulatory region of protein kinase Cγ. J. Biol. Chem. 269, 20000-20012.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20000-20012
    • Quest, A.F.G.1    Bell, R.M.2
  • 35
    • 0028086467 scopus 로고
    • A phorbol ester binding domain in protein kinase Cγ
    • Quest, A.F.G., Bardes, E.S.G., and Bell, R.M. (1994). A phorbol ester binding domain in protein kinase Cγ. J. Biol. Chem. 269, 2961-2970.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2961-2970
    • Quest, A.F.G.1    Bardes, E.S.G.2    Bell, R.M.3
  • 36
    • 0015535748 scopus 로고
    • Delayed release of transmitter at the frog neuromuscular junction
    • Rahamimoff, R., and Yaari, Y. (1973). Delayed release of transmitter at the frog neuromuscular junction. J. Physiol. 228, 241-257.
    • (1973) J. Physiol. , vol.228 , pp. 241-257
    • Rahamimoff, R.1    Yaari, Y.2
  • 37
    • 0030997788 scopus 로고    scopus 로고
    • Opposing effects of phorbol esters on transmitter release and calcium currents at frog motor nerve endings
    • Redman, R.S., Searl, T.J., Hirsh, J.K., and Silinsky, E.M. (1997). Opposing effects of phorbol esters on transmitter release and calcium currents at frog motor nerve endings. J. Physiol. (Lond.) 501, 41-48.
    • (1997) J. Physiol. (Lond.) , vol.501 , pp. 41-48
    • Redman, R.S.1    Searl, T.J.2    Hirsh, J.K.3    Silinsky, E.M.4
  • 39
    • 0029067151 scopus 로고
    • S-100 protein expression in subpopulations of neurons of rat brain
    • Rickmann, M., and Wolff, J.R. (1995). S-100 protein expression in subpopulations of neurons of rat brain. Neuroscience 67, 977-991.
    • (1995) Neuroscience , vol.67 , pp. 977-991
    • Rickmann, M.1    Wolff, J.R.2
  • 40
    • 0028352113 scopus 로고
    • Xenopus embryos regulate the nuclear localization of XMyoD
    • Rupp, R.A., Snider, L., and Weintraub, H. (1994). Xenopus embryos regulate the nuclear localization of XMyoD. Genes Dev. 8, 1311-1323.
    • (1994) Genes Dev. , vol.8 , pp. 1311-1323
    • Rupp, R.A.1    Snider, L.2    Weintraub, H.3
  • 41
    • 0031466995 scopus 로고    scopus 로고
    • Direct visualization of the translocation of the γ-subspecies of protein kinase C in living cells using fusion proteins with green fluorescent protein
    • Sakai, N., Sasaki, K., Ikegaki, N., Shirai, Y., Ono, Y., and Saito, N. (1997). Direct visualization of the translocation of the γ-subspecies of protein kinase C in living cells using fusion proteins with green fluorescent protein. J. Cell. Biol. 739, 1465-1476.
    • (1997) J. Cell. Biol. , vol.739 , pp. 1465-1476
    • Sakai, N.1    Sasaki, K.2    Ikegaki, N.3    Shirai, Y.4    Ono, Y.5    Saito, N.6
  • 42
    • 0028316929 scopus 로고
    • Synapsin IIa accelerates functional development of neuromuscular synapses
    • Schaeffer, E., Alder, J., Greengard, P., and Poo, M.-m. (1994). Synapsin IIa accelerates functional development of neuromuscular synapses. Proc. Natl. Acad. Sci. USA 91, 3882-3886.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3882-3886
    • Schaeffer, E.1    Alder, J.2    Greengard, P.3    Poo, M.-M.4
  • 43
    • 0027218134 scopus 로고
    • Improved in vitro rheological system for studying the effect of fluid shear stress on cultured cells
    • Schnittler, H.-J., Franke, R.P., Akbay, U., Mrowietz, C., and Drenkhahn, D. (1993). Improved in vitro rheological system for studying the effect of fluid shear stress on cultured cells. Am. J. Physiol. 265, C289-C298.
    • (1993) Am. J. Physiol. , vol.265
    • Schnittler, H.-J.1    Franke, R.P.2    Akbay, U.3    Mrowietz, C.4    Drenkhahn, D.5
  • 44
    • 0024791835 scopus 로고
    • A phorbol diester-induced enhancement of synaptic transmission in olfactory cortex
    • Scholfield, C.N., and Smith, A.J. (1989). A phorbol diester-induced enhancement of synaptic transmission in olfactory cortex. Br. J. Pharmacol. 98, 1344-1350.
    • (1989) Br. J. Pharmacol. , vol.98 , pp. 1344-1350
    • Scholfield, C.N.1    Smith, A.J.2
  • 45
    • 0021967116 scopus 로고
    • Highly lipophilic phorbol esters as inhibitors of specific [3H]phorbol 12,13-dibutyrate binding
    • Sharkey, N.A., and Blumberg, P.M. (1985). Highly lipophilic phorbol esters as inhibitors of specific [3H]phorbol 12,13-dibutyrate binding. Cancer Res. 45, 19-24.
    • (1985) Cancer Res. , vol.45 , pp. 19-24
    • Sharkey, N.A.1    Blumberg, P.M.2
  • 46
    • 1842394775 scopus 로고
    • Competitive inhibition by diacylglyerol of specific phorbol ester binding
    • Sharkey, N.A., Leach, K.L., and Blumberg, P.M. (1984). Competitive inhibition by diacylglyerol of specific phorbol ester binding. Proc. Natl. Acad. Sci. USA 81, 607-610.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 607-610
    • Sharkey, N.A.1    Leach, K.L.2    Blumberg, P.M.3
  • 47
    • 0030463279 scopus 로고    scopus 로고
    • Molecular machinery mediating vesicle budding, docking and fusion
    • Söllner, T.H., and Rothman, J.E. (1996). Molecular machinery mediating vesicle budding, docking and fusion. Experientia 52, 1021-1025.
    • (1996) Experientia , vol.52 , pp. 1021-1025
    • Söllner, T.H.1    Rothman, J.E.2
  • 48
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof, T.C. (1995). The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature 375, 645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 49
    • 0030222771 scopus 로고    scopus 로고
    • 2-domain proteins that regulate membrane traffic
    • 2-domain proteins that regulate membrane traffic. Neuron 17, 379-388.
    • (1996) Neuron , vol.17 , pp. 379-388
    • Südhof, T.C.1    Rizo, J.2
  • 50
    • 0002868327 scopus 로고
    • Culturing spinal neurons and muscle cells from Xenopus embryos
    • G. Banker and K. Goslin, eds. (Cambridge, MA: MIT Press)
    • Tabti, N., and Poo, M.-M. (1991). Culturing spinal neurons and muscle cells from Xenopus embryos. In Culturing Nerve Cells, G. Banker and K. Goslin, eds. (Cambridge, MA: MIT Press), pp. 137-154.
    • (1991) Culturing Nerve Cells , pp. 137-154
    • Tabti, N.1    Poo, M.-M.2
  • 51
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., and Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.