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Volumn 443, Issue 1, 2012, Pages 223-229

The importance of an asymmetric distribution of acidic lipids for synaptotagmin 1 function as a Ca 2+ sensor

Author keywords

1,2 dioleoyl sn glycero 3 phospho L serine (DOPS); Charge asymmetry; Soluble N ethylmaleimide sensitive fusion protein attachment protein receptor (SNARE); Synaptotagmin 1; Vesicle fusion

Indexed keywords

PHOSPHATIDYLSERINE; PROTEOLIPOSOME; SNARE PROTEIN; SYNAPTOTAGMIN I; THREO 3,4 DIHYDROXYPHENYLSERINE;

EID: 84858328639     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20112044     Document Type: Article
Times cited : (14)

References (44)
  • 1
    • 33644770187 scopus 로고    scopus 로고
    • Structure and function of SNARE and SNARE-interacting proteins
    • Brunger, A. T. (2005) Structure and function of SNARE and SNARE-interacting proteins. Q. Rev. Biophys. 38, 1-47
    • (2005) Q. Rev. Biophys. , vol.38 , pp. 1-47
    • Brunger, A.T.1
  • 4
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • DOI 10.1038/26412
    • Sutton, R. B., Fasshauer, D., Jahn, R. and Brunger, A. T. (1998) Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution. Nature 395, 347-353 (Pubitemid 28450677)
    • (1998) Nature , vol.395 , Issue.6700 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 7
    • 2942556680 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • Sudhof, T. C. (2004) The synaptic vesicle cycle. Annu. Rev. Neurosci. 27, 509-547
    • (2004) Annu. Rev. Neurosci. , vol.27 , pp. 509-547
    • Sudhof, T.C.1
  • 9
    • 0037027739 scopus 로고    scopus 로고
    • Synaptotagmin functions as a calcium sensor to synchronize neurotransmitter release
    • DOI 10.1016/S0896-6273(02)01065-6
    • Yoshihara, M. and Littleton, J. T. (2002) Synaptotagmin I functions as a calcium sensor to synchronize neurotransmitter release. Neuron 36, 897-908 (Pubitemid 35447861)
    • (2002) Neuron , vol.36 , Issue.5 , pp. 897-908
    • Yoshihara, M.1    Littleton, J.T.2
  • 13
    • 33847269603 scopus 로고    scopus 로고
    • 2+-phospholipid complex in neurotransmitter release
    • 2+-phospholipid complex in neurotransmitter release. J. Mol. Biol. 367, 848-863
    • (2007) J. Mol. Biol. , vol.367 , pp. 848-863
    • Dai, H.1    Shen, N.2    Arac, D.3    Rizo, J.4
  • 14
    • 0027332736 scopus 로고
    • A single C2 domain from synaptotagmin I is sufficient for high affinity Ca2+/phospholipid binding
    • Davletov, B. A. and Sudhof, T. C. (1993) A single C2 domain from synaptotagmin I is sufficient for high affinity Ca2+/phospholipid binding. J. Biol. Chem. 268, 26386-26390 (Pubitemid 2013546)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.35 , pp. 26386-26390
    • Davletov, B.A.1    Sudhof, T.C.2
  • 15
    • 0032577067 scopus 로고    scopus 로고
    • 2+-binding loop of synaptotagmin with lipid bilayers
    • 2+-binding loop of synaptotagmin with lipid bilayers. J. Biol. Chem. 273, 13995-14001
    • (1998) J. Biol. Chem. , vol.273 , pp. 13995-14001
    • Chapman, E.R.1    Davis, A.F.2
  • 16
    • 0035924571 scopus 로고    scopus 로고
    • 2B-domain: Synaptotagmin 1 as a phospholipid binding machine
    • DOI 10.1016/S0896-6273(01)00548-7
    • Fernandez, I., Arac, D., Ubach, J., Gerber, S. H., Shin, O., Gao, Y., Anderson, R. G., Sudhof, T. C. and Rizo, J. (2001) Three-dimensional structure of the synaptotagmin 1 C2B-domain: synaptotagmin 1 as a phospholipid binding machine. Neuron 32, 1057-1069 (Pubitemid 34075396)
    • (2001) Neuron , vol.32 , Issue.6 , pp. 1057-1069
    • Fernandez, I.1    Arac, D.2    Ubach, J.3    Gerber, S.H.4    Shin, O.-H.5    Gao, Y.6    Anderson, R.G.W.7    Sudhof, T.C.8    Rizo, J.9
  • 20
    • 23144455040 scopus 로고    scopus 로고
    • Single-molecule studies of synaptotagmin and complexin binding to the SNARE complex
    • DOI 10.1529/biophysj.104.054064
    • Bowen, M. E., Weninger, K., Ernst, J., Chu, S. and Brunger, A. T. (2005) Single-molecule studies of synaptotagmin and complexin binding to the SNARE complex. Biophys. J. 89, 690-702 (Pubitemid 41098319)
    • (2005) Biophysical Journal , vol.89 , Issue.1 , pp. 690-702
    • Bowen, M.E.1    Weninger, K.2    Ernst, J.3    Chu, S.4    Brunger, A.T.5
  • 22
    • 0037204076 scopus 로고    scopus 로고
    • Three-dimensional structure of the complexin/SNARE complex
    • DOI 10.1016/S0896-6273(02)00583-4
    • Chen, X., Tomchick, D. R., Kovrigin, E., Arac, D., Machius, M., Sudhof, T. C. and Rizo, J. (2002) Three-dimensional structure of the complexin/SNARE complex. Neuron 33, 397-409 (Pubitemid 34158843)
    • (2002) Neuron , vol.33 , Issue.3 , pp. 397-409
    • Chen, X.1    Tomchick, D.R.2    Kovrigin, E.3    Arac, D.4    Machius, M.5    Sudhof, T.C.6    Rizo, J.7
  • 23
    • 0037040873 scopus 로고    scopus 로고
    • Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis
    • DOI 10.1074/jbc.M109507200
    • Pabst, S., Margittai, M., Vainius, D., Langen, R., Jahn, R. and Fasshauer, D. (2002) Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis. J. Biol. Chem. 277, 7838-7848 (Pubitemid 34968232)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.10 , pp. 7838-7848
    • Pabst, S.1    Margittai, M.2    Vainius, D.3    Langen, R.4    Jahn, R.5    Fasshauer, D.6
  • 24
    • 33746319639 scopus 로고    scopus 로고
    • A clamping mechanism involved in SNARE-dependent exocytosis
    • DOI 10.1126/science.1129450
    • 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 (Pubitemid 44201147)
    • (2006) Science , vol.313 , Issue.5787 , pp. 676-680
    • Giraudo, C.G.1    Eng, W.S.2    Melia, T.J.3    Rothman, J.E.4
  • 26
    • 33748605056 scopus 로고    scopus 로고
    • A Complexin/Synaptotagmin 1 Switch Controls Fast Synaptic Vesicle Exocytosis
    • DOI 10.1016/j.cell.2006.08.030, PII S0092867406011007
    • Tang, J., Maximov, A., Shin, O. H., Dai, H., Rizo, J. and Sudhof, T. C. (2006) A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis. Cell 126, 1175-1187 (Pubitemid 44380295)
    • (2006) Cell , vol.126 , Issue.6 , pp. 1175-1187
    • Tang, J.1    Maximov, A.2    Shin, O.-H.3    Dai, H.4    Rizo, J.5    Sudhof, T.C.6
  • 27
    • 77949330731 scopus 로고    scopus 로고
    • Accessory α-helix of complexin I can displace VAMP2 locally in the complexin-SNARE quaternary complex
    • Lu, B., Song, S. and Shin, Y. K. (2009) Accessory α-helix of complexin I can displace VAMP2 locally in the complexin-SNARE quaternary complex. J. Mol. Biol. 396, 602-609
    • (2009) J. Mol. Biol. , vol.396 , pp. 602-609
    • Lu, B.1    Song, S.2    Shin, Y.K.3
  • 31
    • 34249933061 scopus 로고    scopus 로고
    • How synaptotagmin promotes membrane fusion
    • DOI 10.1126/science.1142614
    • Martens, S., Kozlov, M. M. and McMahon, H. T. (2007) How synaptotagmin promotes membrane fusion. Science 316, 1205-1208 (Pubitemid 46877485)
    • (2007) Science , vol.316 , Issue.5828 , pp. 1205-1208
    • Martens, S.1    Kozlov, M.M.2    McMahon, H.T.3
  • 33
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • DOI 10.1146/annurev.biochem.72.121801.161504
    • Chernomordik, L. V. and Kozlov, M. M. (2003) Protein-lipid interplay in fusion and fission of biological membranes. Annu. Rev. Biochem. 72, 175-207 (Pubitemid 36930445)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 34
    • 0842291506 scopus 로고    scopus 로고
    • 2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane
    • 2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane. Nat. Struct. Mol. Biol. 11, 36-44
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 36-44
    • Bai, J.1    Tucker, W.C.2    Chapman, E.R.3
  • 35
    • 0042672953 scopus 로고    scopus 로고
    • Identification of synaptotagmin effectors via acute inhibition of secretion from cracked PC12 cells
    • DOI 10.1083/jcb.200302060
    • Tucker, W. C., Edwardson, J. M., Bai, J., Kim, H. J., Martin, T. F. and Chapman, E. R. (2003) Identification of synaptotagmin effectors via acute inhibition of secretion from cracked PC12 cells. J. Cell Biol. 162, 199-209 (Pubitemid 36928834)
    • (2003) Journal of Cell Biology , vol.162 , Issue.2 , pp. 199-209
    • Tucker, W.C.1    Edwardson, J.M.2    Bai, J.3    Kim, H.-J.4    Martin, T.F.J.5    Chapman, E.R.6
  • 39
    • 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) Science , vol.304 , pp. 435-438
    • Tucker, W.C.1    Weber, T.2    Chapman, E.R.3
  • 41
    • 0028023444 scopus 로고
    • Calcium dependence of the rate of exocytosis in a synaptic terminal
    • DOI 10.1038/371513a0
    • Heidelberger, R., Heinemann, C., Neher, E. and Matthews, G. (1994) Calcium dependence of the rate of exocytosis in a synaptic terminal. Nature 371, 513-515 (Pubitemid 24306608)
    • (1994) Nature , vol.371 , Issue.6497 , pp. 513-515
    • Heidelberger, R.1    Heinemann, C.2    Neher, E.3    Matthews, G.4
  • 42
    • 0017262014 scopus 로고
    • Ion-binding to phospholipids. Interaction of calcium with phosphatidylserine
    • Hauser, H., Darke, A. and Phillips, M. C. (1976) Ion-binding to phospholipids. Interaction of calcium with phosphatidylserine. Eur. J. Biochem. 62, 335-344
    • (1976) Eur. J. Biochem. , vol.62 , pp. 335-344
    • Hauser, H.1    Darke, A.2    Phillips, M.C.3
  • 44
    • 0014601923 scopus 로고
    • Lipid composition of synaptic plasma membranes isolated from rat brain by zonal centrifugation
    • Cotman, C., Blank, M. L., Moehl, A. and Snyder, F. (1969) Lipid composition of synaptic plasma membranes isolated from rat brain by zonal centrifugation. Biochemistry 8, 4606-4612
    • (1969) Biochemistry , vol.8 , pp. 4606-4612
    • Cotman, C.1    Blank, M.L.2    Moehl, A.3    Snyder, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.