메뉴 건너뛰기




Volumn 8, Issue 5, 2005, Pages 597-605

Gβγ acts at the C terminus of SNAP-25 to mediate presynaptic inhibition

Author keywords

[No Author keywords available]

Indexed keywords

BOTULINUM TOXIN; GUANINE NUCLEOTIDE BINDING PROTEIN BETA SUBUNIT; SNARE PROTEIN; SYNAPTOBREVIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNAPTOTAGMIN; VOLTAGE GATED CALCIUM CHANNEL; AGENTS INTERACTING WITH TRANSMITTER, HORMONE OR DRUG RECEPTORS; CALCIUM BINDING PROTEIN; CALCIUM CHANNEL; G PROTEIN BETA GAMMA; G-PROTEIN BETA GAMMA; GUANINE NUCLEOTIDE BINDING PROTEIN GAMMA SUBUNIT; MEMBRANE PROTEIN; NERVE PROTEIN; SYNAPTOTAGMIN I; VESICULAR TRANSPORT PROTEIN;

EID: 17844373228     PISSN: 10976256     EISSN: None     Source Type: Journal    
DOI: 10.1038/nn1439     Document Type: Article
Times cited : (147)

References (50)
  • 1
    • 0024582313 scopus 로고
    • G proteins couple α-adrenergic and GABAb receptors to inhibition of peptide secretion from peripheral sensory neurons
    • Holz, G.G., 4th., Kream, R.M., Spiegel, A. & Dunlap, K. G proteins couple α-adrenergic and GABAb receptors to inhibition of peptide secretion from peripheral sensory neurons. J. Neurosci. 9, 657-666 (1989).
    • (1989) J. Neurosci. , vol.9 , pp. 657-666
    • Holz IV, G.G.1    Kream, R.M.2    Spiegel, A.3    Dunlap, K.4
  • 2
    • 0027158113 scopus 로고
    • G protein modulation of voltage-dependent calcium channels and transmitter release
    • Dolphin, A.C. et al. G protein modulation of voltage-dependent calcium channels and transmitter release. Biochem. Soc. Trans. 21, 391-395 (1993).
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 391-395
    • Dolphin, A.C.1
  • 3
    • 0031033757 scopus 로고    scopus 로고
    • Direct binding of G-protein βγ complex to voltage-dependent calcium channels
    • DeWaard, M. et al. Direct binding of G-protein βγ complex to voltage-dependent calcium channels. Nature 385, 446-450 (1997).
    • (1997) Nature , vol.385 , pp. 446-450
    • DeWaard, M.1
  • 5
    • 0034934093 scopus 로고    scopus 로고
    • GTP-binding protein βγ subunits mediate presynaptic calcium current inhibition by GABA(B) receptor
    • Kajikawa, Y., Saitoh, N. & Takahashi, T. GTP-binding protein βγ subunits mediate presynaptic calcium current inhibition by GABA(B) receptor. Proc. Natl. Acad. Sci. USA 98, 8054-8058 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8054-8058
    • Kajikawa, Y.1    Saitoh, N.2    Takahashi, T.3
  • 6
    • 0031984517 scopus 로고    scopus 로고
    • The many faces of G protein signaling
    • Hamm, H.E. The many faces of G protein signaling. J. Biol. Chem. 273, 669-672 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 669-672
    • Hamm, H.E.1
  • 7
    • 0035853270 scopus 로고    scopus 로고
    • 2+ entry
    • 2+ entry. Science 292, 293-297 (2001).
    • (2001) Science , vol.292 , pp. 293-297
    • Blackmer, T.1
  • 8
    • 0035870869 scopus 로고    scopus 로고
    • Calcium influx-independent depression of transmitter release by 5-HT at lamprey spiral cord synapses
    • Takahashi, M., Freed, R., Blackmer, T. & Alford, S. Calcium influx-independent depression of transmitter release by 5-HT at lamprey spiral cord synapses. J. Physiol. (Lond.) 532, 323-336 (2001).
    • (2001) J. Physiol. (Lond.) , vol.532 , pp. 323-336
    • Takahashi, M.1    Freed, R.2    Blackmer, T.3    Alford, S.4
  • 9
    • 0026473109 scopus 로고
    • Calcium currents at motor nerve endings: Absence of effects of adenosine receptor agonists in the frog
    • Silinsky, E.M. & Solsona, C.S. Calcium currents at motor nerve endings: absence of effects of adenosine receptor agonists in the frog. J. Physiol. (Lond.) 457, 315-328 (1992).
    • (1992) J. Physiol. (Lond.) , vol.457 , pp. 315-328
    • Silinsky, E.M.1    Solsona, C.S.2
  • 10
    • 0034054672 scopus 로고    scopus 로고
    • G protein modulation of N-type calcium channels is facilitated by physical interactions between syntaxin 1A and Gβγ
    • Jarvis, S.E., Magga, J.M., Beedle, A.M., Braun, J.E. & Zamponi, G.W. G protein modulation of N-type calcium channels is facilitated by physical interactions between syntaxin 1A and Gβγ. J. Biol. Chem. 275, 6388-6394 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 6388-6394
    • Jarvis, S.E.1    Magga, J.M.2    Beedle, A.M.3    Braun, J.E.4    Zamponi, G.W.5
  • 11
    • 17844372569 scopus 로고    scopus 로고
    • G protein βγ directly regulates the SNARE protein fusion machinery for secretory granule exocytosis
    • Blackmer, T. et al. G protein βγ directly regulates the SNARE protein fusion machinery for secretory granule exocytosis. Nat. Neurosci. 8, 421-425 (2005).
    • (2005) Nat. Neurosci. , vol.8 , pp. 421-425
    • Blackmer, T.1
  • 12
    • 0022544480 scopus 로고
    • A spinal projection of 5-hydroxytryptamine neurons in the lamprey brainstem; evidence from combined retrograde tracing and immunohistochemistry
    • Brodin, L., Buchanan, J.T., Hokfelt, T., Grillner, S. & Verhofstad, A.A. A spinal projection of 5-hydroxytryptamine neurons in the lamprey brainstem; evidence from combined retrograde tracing and immunohistochemistry. Neurosci. Lett. 67, 53-57 (1986).
    • (1986) Neurosci. Lett. , vol.67 , pp. 53-57
    • Brodin, L.1    Buchanan, J.T.2    Hokfelt, T.3    Grillner, S.4    Verhofstad, A.A.5
  • 14
    • 0023732710 scopus 로고
    • Reticulospinal neurons in lamprey: Transmitters, synaptic interactions and their role during locomotion
    • Brodin, L. et al. Reticulospinal neurons in lamprey: transmitters, synaptic interactions and their role during locomotion. Arch. Ital. Biol. 126, 317-345 (1988).
    • (1988) Arch. Ital. Biol. , vol.126 , pp. 317-345
    • Brodin, L.1
  • 15
    • 0037047501 scopus 로고    scopus 로고
    • Ultrastructural organization of lamprey reticulospinal synapses in three dimensions
    • Gustafsson, J.S. et al. Ultrastructural organization of lamprey reticulospinal synapses in three dimensions. J. Comp. Neurol. 450, 167-182 (2002).
    • (2002) J. Comp. Neurol. , vol.450 , pp. 167-182
    • Gustafsson, J.S.1
  • 16
    • 0029074686 scopus 로고
    • Synaptic vesicle depletion in reticulospinal axons is reduced by 5-hydroxytryptamine: Direct evidence for presynaptic modulation of glutamatergic transmission
    • Shupliakov, O., Pieribone, V.A., Gad, H. & Brodin, L. Synaptic vesicle depletion in reticulospinal axons is reduced by 5-hydroxytryptamine: direct evidence for presynaptic modulation of glutamatergic transmission. Eur. J. Neurosci. 7, 1111-1116 (1995).
    • (1995) Eur. J. Neurosci. , vol.7 , pp. 1111-1116
    • Shupliakov, O.1    Pieribone, V.A.2    Gad, H.3    Brodin, L.4
  • 17
    • 0027409301 scopus 로고
    • Multiple calcium-dependent processes related to secretion in bovine chromaffin cells
    • Neher, E. & Zucker, R.S. Multiple calcium-dependent processes related to secretion in bovine chromaffin cells. Neuron 10, 21-30 (1993).
    • (1993) Neuron , vol.10 , pp. 21-30
    • Neher, E.1    Zucker, R.S.2
  • 18
    • 0025306828 scopus 로고
    • Calcium released by photolysis of DM-nitrophen stimulates transmitter release at squid giant synapse
    • Delaney, K.R. & Zucker, R.S. Calcium released by photolysis of DM-nitrophen stimulates transmitter release at squid giant synapse. J. Physiol. (Lond.) 426, 473-498 (1990).
    • (1990) J. Physiol. (Lond.) , vol.426 , pp. 473-498
    • Delaney, K.R.1    Zucker, R.S.2
  • 19
    • 0027450210 scopus 로고
    • Calcium released by photolysis of DM-nitrophen triggers transmitter release at the crayfish neuromusculsr junction
    • Mulkey, R.M. & Zucker, R.S. Calcium released by photolysis of DM-nitrophen triggers transmitter release at the crayfish neuromusculsr junction. J. Physiol. (Lond.) 462, 243-260 (1993).
    • (1993) J. Physiol. (Lond.) , vol.462 , pp. 243-260
    • Mulkey, R.M.1    Zucker, R.S.2
  • 20
    • 0028268948 scopus 로고
    • Clostridial neurotoxins: New tools for dissecting exocytosis
    • Niemann, H., Blasi, J. & Jahn, R. Clostridial neurotoxins: new tools for dissecting exocytosis. Trends Cell Biol. 4, 179-185 (1994).
    • (1994) Trends Cell Biol. , vol.4 , pp. 179-185
    • Niemann, H.1    Blasi, J.2    Jahn, R.3
  • 21
    • 0029613765 scopus 로고
    • Structure and function of tetanus and botulinum neurotoxins
    • Montecucco, C. & Schiavo, G. Structure and function of tetanus and botulinum neurotoxins. Q. Rev. Biophys. 28, 423-472 (1995).
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 423-472
    • Montecucco, C.1    Schiavo, G.2
  • 22
    • 0029980484 scopus 로고    scopus 로고
    • Clostridial neurotoxins and substrate proteolysis in intact neurons: Botulinum neurotoxin C acts on synaptosomal-associated protein of 25 kDa
    • Williamson, L.C., Halpern, J.L., Montecucco, C., Brown, J.E. & Neale, E.A. Clostridial neurotoxins and substrate proteolysis in intact neurons: botulinum neurotoxin C acts on synaptosomal-associated protein of 25 kDa. J. Biol. Chem. 271, 7694-7699 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 7694-7699
    • Williamson, L.C.1    Halpern, J.L.2    Montecucco, C.3    Brown, J.E.4    Neale, E.A.5
  • 24
    • 0034121745 scopus 로고    scopus 로고
    • How botulinum and tetanus neurotoxins block neurotransmitter release
    • Humeau, Y., Doussau, F., Grant, N.J. & Poulain, B. How botulinum and tetanus neurotoxins block neurotransmitter release. Biochimie 82, 427-446 (2000).
    • (2000) Biochimie , vol.82 , pp. 427-446
    • Humeau, Y.1    Doussau, F.2    Grant, N.J.3    Poulain, B.4
  • 25
    • 0029074299 scopus 로고
    • Molecular aspects of tetanus and botulinum neurotoxin poisoning
    • Ahnert-Hilger, G. & Bigalke, H. Molecular aspects of tetanus and botulinum neurotoxin poisoning. Prog. Neurobiol. 46, 83-96 (1995).
    • (1995) Prog. Neurobiol. , vol.46 , pp. 83-96
    • Ahnert-Hilger, G.1    Bigalke, H.2
  • 27
    • 0026497466 scopus 로고
    • Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin
    • Schiavo, G. et al. Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin. Nature 359, 832-835 (1992).
    • (1992) Nature , vol.359 , pp. 832-835
    • Schiavo, G.1
  • 28
    • 0033887403 scopus 로고    scopus 로고
    • Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution
    • Hanson, M.A. & Stevens, R.C. Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution. Nat. Struct. Biol. 7, 687-692 (2000).
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 687-692
    • Hanson, M.A.1    Stevens, R.C.2
  • 29
    • 0028130728 scopus 로고
    • Synaptic vesicle membrane fusion complex: Action of clostridial neurotoxins on assembly
    • Hayashi, T. et al. Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly. EMBO J. 13, 5051-5061 (1994).
    • (1994) EMBO J. , vol.13 , pp. 5051-5061
    • Hayashi, T.1
  • 30
    • 0027946206 scopus 로고
    • Fusion complex formation protects synaptobrevin against proteolysis by tetanus toxin light chain
    • Pellegrini, L.L., O'Connor, V. & Betz, H. Fusion complex formation protects synaptobrevin against proteolysis by tetanus toxin light chain. FEBS Lett. 353, 319-323 (1994).
    • (1994) FEBS Lett. , vol.353 , pp. 319-323
    • Pellegrini, L.L.1    O'Connor, V.2    Betz, H.3
  • 31
    • 0033638109 scopus 로고    scopus 로고
    • Cysteine string protein regulates G protein modulation of N-type calcium channels
    • Magga, J.M., Jarvis, S.E., Arnot, M.I., Zamponi, G.W. & Braun, J.E. Cysteine string protein regulates G protein modulation of N-type calcium channels. Neuron 28, 195-204 (2000).
    • (2000) Neuron , vol.28 , pp. 195-204
    • Magga, J.M.1    Jarvis, S.E.2    Arnot, M.I.3    Zamponi, G.W.4    Braun, J.E.5
  • 32
    • 0027438184 scopus 로고
    • Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-terminal peptide bonds
    • Schiavo, G. et al. Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-terminal peptide bonds. FEBS Lett. 335, 99-103 (1993).
    • (1993) FEBS Lett. , vol.335 , pp. 99-103
    • Schiavo, G.1
  • 33
    • 0028069674 scopus 로고
    • Proteolysis of SNAP-25 by types E and A botulinal neurotoxins
    • Binz, T. et al. Proteolysis of SNAP-25 by types E and A botulinal neurotoxins. J. Biol. Chem. 269, 1617-1620 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 1617-1620
    • Binz, T.1
  • 34
    • 0029164314 scopus 로고
    • Poisoning by botulinum neurotoxin A does not inhibit formation or disassembly of the synaptosomal fusion complex
    • Otto, H., Hanson, P.I., Chapman, E.R., Blasi, J. & Jahn, R. Poisoning by botulinum neurotoxin A does not inhibit formation or disassembly of the synaptosomal fusion complex. Biochem. Biophys. Res. Commun. 212, 945-952 (1995).
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 945-952
    • Otto, H.1    Hanson, P.I.2    Chapman, E.R.3    Blasi, J.4    Jahn, R.5
  • 35
    • 33644681150 scopus 로고    scopus 로고
    • Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity
    • Xu, T., Binz, T., Niemann, H. & Neher, E. Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity. Nat. Neurosci. 1, 192-200 (1998).
    • (1998) Nat. Neurosci. , vol.1 , pp. 192-200
    • Xu, T.1    Binz, T.2    Niemann, H.3    Neher, E.4
  • 36
    • 0342751280 scopus 로고    scopus 로고
    • Exocytotic mechanism studied by truncated and zero layer mutants of the C-terminus of SNAP-25
    • Wei, S. et al. Exocytotic mechanism studied by truncated and zero layer mutants of the C-terminus of SNAP-25. EMBO J. 19, 1279-1289 (2000).
    • (2000) EMBO J. , vol.19 , pp. 1279-1289
    • Wei, S.1
  • 37
    • 1942520207 scopus 로고    scopus 로고
    • 2+-regulated membrane fusion by synaptotagmin and SNAREs
    • 2+-regulated membrane fusion by synaptotagmin and SNAREs. Science 304, 435-438 (2004).
    • (2004) Science , vol.304 , pp. 435-438
    • Tucker, W.C.1    Weber, T.2    Chapman, E.R.3
  • 40
    • 0032476669 scopus 로고    scopus 로고
    • Regulation of exocytosis from rat peritoneal mast cells by G protein βγ-subunits
    • Pinxteren, J.A., O'Sullivan, A.J., Tatham, P.E. & Gomperts, B.D. Regulation of exocytosis from rat peritoneal mast cells by G protein βγ-subunits. EMBO J. 17, 6210-6218 (1998).
    • (1998) EMBO J. , vol.17 , pp. 6210-6218
    • Pinxteren, J.A.1    O'Sullivan, A.J.2    Tatham, P.E.3    Gomperts, B.D.4
  • 41
    • 0033556082 scopus 로고    scopus 로고
    • Molecular mechanisms and regulation of insulin exocytosis as a paradigm of endocrine secretion
    • Lang, J. Molecular mechanisms and regulation of insulin exocytosis as a paradigm of endocrine secretion. Eur. J. Biochem. 259, 3-17 (1999).
    • (1999) Eur. J. Biochem. , vol.259 , pp. 3-17
    • Lang, J.1
  • 42
    • 0027219725 scopus 로고
    • Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25
    • Blasi, J. et al. Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25. Nature 365, 160-163 (1993).
    • (1993) Nature , vol.365 , pp. 160-163
    • Blasi, J.1
  • 43
    • 0031016979 scopus 로고    scopus 로고
    • Inhibition of transmitter release correlates with the proteolytic activity of tetanus toxin and botulinus toxin A in individual cultured synapses of Hirudo medicinalis
    • Bruns, D. et al. Inhibition of transmitter release correlates with the proteolytic activity of tetanus toxin and botulinus toxin A in individual cultured synapses of Hirudo medicinalis. J. Neurosci. 17, 1898-1910 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 1898-1910
    • Bruns, D.1
  • 44
    • 53249097614 scopus 로고    scopus 로고
    • Endoproteinase activity of type A botulinum neurotoxin: Substrate requirements and activation by serum albumin
    • Schmidt, J.J. & Bostian, K.A. Endoproteinase activity of type A botulinum neurotoxin: substrate requirements and activation by serum albumin. J. Protein Chem. 16, 19-26 (1997).
    • (1997) J. Protein Chem. , vol.16 , pp. 19-26
    • Schmidt, J.J.1    Bostian, K.A.2
  • 45
    • 14644415031 scopus 로고    scopus 로고
    • The synaptic vesicle protein CSP α prevents presynaptic degeneration
    • Fernandez-Chacon, R. et al. The synaptic vesicle protein CSP α prevents presynaptic degeneration. Neuron 42, 237-251 (2004).
    • (2004) Neuron , vol.42 , pp. 237-251
    • Fernandez-Chacon, R.1
  • 46
    • 12544260667 scopus 로고    scopus 로고
    • 5-HT prolongs ventral root bursting via presynaptic inhibition of synaptic activity during fictive locomotion in lamprey
    • Schwartz, E.J., Gerachshenko, T. & Alford, S. 5-HT prolongs ventral root bursting via presynaptic inhibition of synaptic activity during fictive locomotion in lamprey. J. Neurophysiol. 93, 980-988 (2005).
    • (2005) J. Neurophysiol. , vol.93 , pp. 980-988
    • Schwartz, E.J.1    Gerachshenko, T.2    Alford, S.3
  • 47
    • 0032557490 scopus 로고    scopus 로고
    • Molecular basis for interactions of G protein βγ subunits with effectors
    • Ford, C.E. et al. Molecular basis for interactions of G protein βγ subunits with effectors. Science 280, 1271-1274 (1998).
    • (1998) Science , vol.280 , pp. 1271-1274
    • Ford, C.E.1
  • 48
    • 0141988381 scopus 로고    scopus 로고
    • Identification of SNARE complex modulators that inhibit exocytosis from an α-helix-constrained combinatorial library
    • Blanes-Mira, C. et al. Identification of SNARE complex modulators that inhibit exocytosis from an α-helix-constrained combinatorial library. Biochem. J. 375, 159-166 (2003).
    • (2003) Biochem. J. , vol.375 , pp. 159-166
    • Blanes-Mira, C.1
  • 49
    • 0025833084 scopus 로고
    • Labeling of the βγ subunit complex of transducin with an environmentally sensitive cysteine reagent. Use of fluorescence spectroscopy to monitor transducin subunit interactions
    • Phillips, W.J. & Cerione, R.A. Labeling of the βγ subunit complex of transducin with an environmentally sensitive cysteine reagent. Use of fluorescence spectroscopy to monitor transducin subunit interactions. J. Biol. Chem. 266, 11017-11024 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 11017-11024
    • Phillips, W.J.1    Cerione, R.A.2
  • 50
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • Sutton, R.B., Fasshauer, D., Jahn, R. & Brunger, A.T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature 395, 347-353 (1998).
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.