메뉴 건너뛰기




Volumn 288, Issue 48, 2013, Pages 34906-34919

Point mutation in syntaxin-1A causes abnormal vesicle recycling, behaviors, and short term plasticity

(18)  Watanabe, Yumi a,b,c   Katayama, Norikazu d   Takeuchi, Kosei a,b   Togano, Tetsuya a,e   Itoh, Rieko a   Sato, Michiko a   Yamazaki, Maya b   Abe, Manabu b   Sato, Toshiya b   Oda, Kanako b   Yokoyama, Minesuke b   Takao, Keizo f,i   Fukaya, Masahiro h   Miyakawa, Tsuyoshi f,g,i   Watanabe, Masahiko h   Sakimura, Kenji b   Manabe, Toshiya d   Igarashia, Michihiro a,b  


Author keywords

[No Author keywords available]

Indexed keywords

COMPLEX FORMATIONS; NEURAL PLASTICITY; NEURONAL PLASTICITY; PRESYNAPTIC PLASTICITY; REGULATORY PROTEIN; SHORT TERM PLASTICITY; SINGLE-POINT MUTATION; SYNAPTIC RESPONSE;

EID: 84889051596     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.504050     Document Type: Article
Times cited : (14)

References (38)
  • 3
    • 34447252763 scopus 로고    scopus 로고
    • Roles of calmodulin and calmodulin- binding proteins in synaptic vesicle recycling during regulated exocytosis at submicromolar Ca2+ concentrations
    • Igarashi, M., and Watanabe, M. (2007) Roles of calmodulin and calmodulin- binding proteins in synaptic vesicle recycling during regulated exocytosis at submicromolar Ca2+ concentrations. Neurosci. Res. 58, 226-233
    • (2007) Neurosci. Res , vol.58 , pp. 226-233
    • Igarashi, M.1    Watanabe, M.2
  • 4
    • 0037446077 scopus 로고    scopus 로고
    • Minimal residues in linker domain of syntaxin 1A required for binding affinity to Ca2+/calmodulin-dependent protein kinase II
    • Nomura, K., Ohyama, A., Komiya, Y., and Igarashi, M. (2003) Minimal residues in linker domain of syntaxin 1A required for binding affinity to Ca2+/calmodulin-dependent protein kinase II. J. Neurosci. Res. 72, 198-202
    • (2003) J. Neurosci. Res , vol.72 , pp. 198-202
    • Nomura, K.1    Ohyama, A.2    Komiya, Y.3    Igarashi, M.4
  • 5
    • 0035997377 scopus 로고    scopus 로고
    • Neuronal Ca2+/calmodulin-dependent protein kinase II: The role of structure and autoregulation in cellular function
    • Hudmon, A., and Schulman, H. (2002) Neuronal Ca2+/calmodulin-dependent protein kinase II: the role of structure and autoregulation in cellular function. Annu. Rev. Biochem. 71, 473-510
    • (2002) Annu. Rev. Biochem , vol.71 , pp. 473-510
    • Hudmon, A.1    Schulman, H.2
  • 6
    • 25644432658 scopus 로고    scopus 로고
    • Neuronal Ca2+/calmodulin-dependent protein kinase II-discovery, progress in a quarter of a century, and perspective: Implication for learning and memory
    • Yamauchi, T. (2005) Neuronal Ca2+/calmodulin-dependent protein kinase II-discovery, progress in a quarter of a century, and perspective: implication for learning and memory. Biol. Pharm. Bull. 28, 1342-1354
    • (2005) Biol. Pharm. Bull , vol.28 , pp. 1342-1354
    • Yamauchi, T.1
  • 7
    • 0026706939 scopus 로고
    • Synaptic vesicle-associated Ca2+/calmodulindependent protein kinase II is a binding protein for synapsin I
    • Benfenati, F., Valtorta, F., Rubenstein, J. L., Gorelick, F. S., Greengard, P., and Czernik, A. J. (1992) Synaptic vesicle-associated Ca2+/calmodulindependent protein kinase II is a binding protein for synapsin I. Nature 359, 417-420
    • (1992) Nature , vol.359 , pp. 417-420
    • Benfenati, F.1    Valtorta, F.2    Rubenstein, J.L.3    Gorelick, F.S.4    Greengard, P.5    Czernik, A.J.6
  • 8
    • 29144493185 scopus 로고    scopus 로고
    • Immunoisolation of two synaptic vesicle pools from synaptosomes: A proteomics analysis
    • Morciano, M., Burré, J., Corvey, C., Karas, M., Zimmermann, H., and Volknandt, W. (2005) Immunoisolation of two synaptic vesicle pools from synaptosomes: a proteomics analysis. J. Neurochem. 95, 1732-1745
    • (2005) J. Neurochem , vol.95 , pp. 1732-1745
    • Morciano, M.1    Burré, J.2    Corvey, C.3    Karas, M.4    Zimmermann, H.5    Volknandt, W.6
  • 10
    • 0018070988 scopus 로고
    • A rapid method for the preparation of relatively pure metabolically competent synaptosomes from rat brain
    • Booth, R. F., and Clark, J. B. (1978) A rapid method for the preparation of relatively pure metabolically competent synaptosomes from rat brain. Biochem. J. 176, 365-370
    • (1978) Biochem. J. , vol.176 , pp. 365-370
    • Booth, R.F.1    Clark, J.B.2
  • 11
    • 0029781368 scopus 로고    scopus 로고
    • Synaptic vesicle recycling in synapsin i knock-out mice
    • Ryan, T. A., Li, L., Chin, L. S., Greengard, P., and Smith, S. J. (1996) Synaptic vesicle recycling in synapsin I knock-out mice. J. Cell Biol. 134, 1219-1227
    • (1996) J. Cell Biol , vol.134 , pp. 1219-1227
    • Ryan, T.A.1    Li, L.2    Chin, L.S.3    Greengard, P.4    Smith, S.J.5
  • 12
    • 34249719431 scopus 로고    scopus 로고
    • Impact of brain-behavior phenotypying of genetically-engineered mice on research of neuropsychiatric disorders
    • Takao, K., Yamasaki, N., and Miyakawa, T. (2007) Impact of brain-behavior phenotypying of genetically-engineered mice on research of neuropsychiatric disorders. Neurosci. Res. 58, 124-132
    • (2007) Neurosci. Res , vol.58 , pp. 124-132
    • Takao, K.1    Yamasaki, N.2    Miyakawa, T.3
  • 13
    • 67651180866 scopus 로고    scopus 로고
    • Brain-behavior phenotypying of genetically-engineered mice using a comprehensive behavioral test battery on research of neuropsychiatric disorders
    • Takao, K., and Miyakawa, T. (2009) Brain-behavior phenotypying of genetically-engineered mice using a comprehensive behavioral test battery on research of neuropsychiatric disorders. J. Toxicol. Sci. 34, SP293-SP305
    • (2009) J. Toxicol. Sci , vol.34
    • Takao, K.1    Miyakawa, T.2
  • 18
    • 38949211822 scopus 로고    scopus 로고
    • Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complex
    • Weninger, K., Bowen, M. E., Choi, U. B., Chu, S., and Brunger, A. T. (2008) Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complex. Structure 16, 308-320
    • (2008) Structure , vol.16 , pp. 308-320
    • Weninger, K.1    Bowen, M.E.2    Choi, U.B.3    Chu, S.4    Brunger, A.T.5
  • 19
    • 79961034486 scopus 로고    scopus 로고
    • Complexin arrests a neighbor
    • Weninger, K. R. (2011) Complexin arrests a neighbor. Nat. Struct. Mol. Biol. 18, 861-863
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 861-863
    • Weninger, K.R.1
  • 20
    • 0028130728 scopus 로고
    • Synaptic vesicle membrane fusion complex: Action of clostridial neurotoxins on assembly
    • Hayashi, T., McMahon, H., Yamasaki, S., Binz, T., Hata, Y., Südhof, T. C., and Niemann, H. (1994) Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly. EMBO J. 13, 5051-5061
    • (1994) EMBO J. , vol.13 , pp. 5051-5061
    • Hayashi, T.1    McMahon, H.2    Yamasaki, S.3    Binz, T.4    Hata, Y.5    Südhof, T.C.6    Niemann, H.7
  • 21
    • 0027368451 scopus 로고
    • Modulation of synaptic transmission and long term potentiation: Effects on paired pulse facilitation and EPSC variance in the CA1 region of the hippocampus
    • Manabe, T., Wyllie, D. J., Perkel, D. J., and Nicoll, R. A. (1993) Modulation of synaptic transmission and long term potentiation: effects on paired pulse facilitation and EPSC variance in the CA1 region of the hippocampus. J. Neurophysiol. 70, 1451-1459
    • (1993) J. Neurophysiol , vol.70 , pp. 1451-1459
    • Manabe, T.1    Wyllie, D.J.2    Perkel, D.J.3    Nicoll, R.A.4
  • 22
    • 79951948881 scopus 로고    scopus 로고
    • Protein scaffolds in the coupling of synaptic exocytosis and endocytosis
    • Haucke, V., Neher, E., and Sigrist, S. J. (2011) Protein scaffolds in the coupling of synaptic exocytosis and endocytosis. Nat. Rev. Neurosci. 12, 127-138
    • (2011) Nat. Rev. Neurosci , vol.12 , pp. 127-138
    • Haucke, V.1    Neher, E.2    Sigrist, S.J.3
  • 23
    • 33846265638 scopus 로고    scopus 로고
    • Fast synaptic vesicle reuse slows the rate of synaptic depression in the CA1 region of hippocampus
    • Ertunc, M., Sara, Y., Chung, C., Atasoy, D., Virmani, T., and Kavalali, E. T. (2007) Fast synaptic vesicle reuse slows the rate of synaptic depression in the CA1 region of hippocampus. J. Neurosci. 27, 341-354
    • (2007) J. Neurosci , vol.27 , pp. 341-354
    • Ertunc, M.1    Sara, Y.2    Chung, C.3    Atasoy, D.4    Virmani, T.5    Kavalali, E.T.6
  • 24
    • 0036889742 scopus 로고    scopus 로고
    • Estimation of quantal parameters at the calyx of Held synapse
    • Sakaba, T., Schneggenburger, R., and Neher, E. (2002) Estimation of quantal parameters at the calyx of Held synapse. Neurosci. Res. 44, 343-356
    • (2002) Neurosci. Res , vol.44 , pp. 343-356
    • Sakaba, T.1    Schneggenburger, R.2    Neher, E.3
  • 25
    • 79955668934 scopus 로고    scopus 로고
    • Short term forms of presynaptic plasticity
    • Fioravante, D., and Regehr, W. G. (2011) Short term forms of presynaptic plasticity. Curr. Opin. Neurobiol. 21, 269-274
    • (2011) Curr. Opin. Neurobiol , vol.21 , pp. 269-274
    • Fioravante, D.1    Regehr, W.G.2
  • 26
    • 84889022429 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 27
    • 84889030365 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 28
    • 84889035501 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 29
    • 0033619769 scopus 로고    scopus 로고
    • Transfection analysis of functional roles of complexin i and II in the exocytosis of two different types of secretory vesicles
    • Itakura, M., Misawa, H., Sekiguchi, M., Takahashi, S., and Takahashi, M. (1999) Transfection analysis of functional roles of complexin I and II in the exocytosis of two different types of secretory vesicles. Biochem. Biophys. Res. Commun. 265, 691-696
    • (1999) Biochem. Biophys. Res. Commun , vol.265 , pp. 691-696
    • Itakura, M.1    Misawa, H.2    Sekiguchi, M.3    Takahashi, S.4    Takahashi, M.5
  • 30
    • 33746319639 scopus 로고    scopus 로고
    • A clamping mechanism involved in SNARE-dependent exocytosis
    • Giraudo, C. G., Eng, W. S., Melia, T. J., and Rothman, J. E. (2006) A clamping mechanism involved in SNARE-dependent exocytosis. Science 313, 676-680
    • (2006) Science , vol.313 , pp. 676-680
    • Giraudo, C.G.1    Eng, W.S.2    Melia, T.J.3    Rothman, J.E.4
  • 31
    • 45549089944 scopus 로고    scopus 로고
    • Complexins facilitate neurotransmitter release at excitatory and inhibitory synapses in mammalian central nervous system
    • Xue, M., Stradomska, A., Chen, H., Brose, N., Zhang, W., Rosenmund, C., and Reim, K. (2008) Complexins facilitate neurotransmitter release at excitatory and inhibitory synapses in mammalian central nervous system. Proc. Natl. Acad. Sci. U.S.A. 105, 7875-7880
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 7875-7880
    • Xue, M.1    Stradomska, A.2    Chen, H.3    Brose, N.4    Zhang, W.5    Rosenmund, C.6    Reim, K.7
  • 32
    • 58849164361 scopus 로고    scopus 로고
    • Complexin controls the force transfer from SNARE complexes to membranes in fusion
    • Maximov, A., Tang, J., Yang, X., Pang, Z. P., and Südhof, T. C. (2009) Complexin controls the force transfer from SNARE complexes to membranes in fusion. Science 323, 516-521
    • (2009) Science , vol.323 , pp. 516-521
    • Maximov, A.1    Tang, J.2    Yang, X.3    Pang, Z.P.4    Südhof, T.C.5
  • 34
    • 0014259321 scopus 로고
    • The role of calcium in neuromuscular facilitation
    • Katz, B., and Miledi, R. (1968) The role of calcium in neuromuscular facilitation. J. Physiol. 195, 481-492
    • (1968) J. Physiol , vol.195 , pp. 481-492
    • Katz, B.1    Miledi, R.2
  • 36
    • 0028987847 scopus 로고
    • The α-Ca2+/calmodulin kinase II: A bidirectional modulator of presynaptic plasticity
    • Chapman, P. F., Frenguelli, B. G., Smith, A., Chen, C. M., and Silva, A. J. (1995) The α-Ca2+/calmodulin kinase II: a bidirectional modulator of presynaptic plasticity. Neuron 14, 591-597
    • (1995) Neuron , vol.14 , pp. 591-597
    • Chapman, P.F.1    Frenguelli, B.G.2    Smith, A.3    Chen, C.M.4    Silva, A.J.5
  • 38
    • 0037389665 scopus 로고    scopus 로고
    • Essential function of α-calcium/calmodulin-dependent protein kinase II in neurotransmitter release at a glutamatergic central synapse
    • Hinds, H. L., Goussakov, I., Nakazawa, K., Tonegawa, S., and Bolshakov, V. Y. (2003) Essential function of α-calcium/calmodulin-dependent protein kinase II in neurotransmitter release at a glutamatergic central synapse. Proc. Natl. Acad. Sci. U.S.A. 100, 4275-4280
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 4275-4280
    • Hinds, H.L.1    Goussakov, I.2    Nakazawa, K.3    Tonegawa, S.4    Bolshakov, V.Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.