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Volumn 11, Issue 9, 2004, Pages 844-849

Structural basis for the evolutionary inactivation of Ca2+ binding to synaptotagmin 4

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; PHOSPHOLIPID; SYNAPTOTAGMIN; SYNAPTOTAGMIN 4; UNCLASSIFIED DRUG;

EID: 4344616380     PISSN: 15459993     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsmb817     Document Type: Article
Times cited : (87)

References (35)
  • 1
    • 2042437650 scopus 로고    scopus 로고
    • Initial sequencing and analysis of the human genome
    • Lander, E.S. et al. Initial sequencing and analysis of the human genome. Nature 409, 860-921 (2001).
    • (2001) Nature , vol.409 , pp. 860-921
    • Lander, E.S.1
  • 3
    • 0035282457 scopus 로고    scopus 로고
    • Synaptotagmin I functions as a calcium regulator of release probability
    • Fernandez-Chacon, R. et al. Synaptotagmin I functions as a calcium regulator of release probability. Nature 410, 41-49 (2001).
    • (2001) Nature , vol.410 , pp. 41-49
    • Fernandez-Chacon, R.1
  • 4
    • 0037130255 scopus 로고    scopus 로고
    • The C(2)B Ca(2+)-binding motif of synaptotagmin is required for synaptic transmission in vivo
    • Mackler, J.M., Drummond, J.A., Loewen, C.A., Robinson, I.M. & Reist, N.E. The C(2)B Ca(2+)-binding motif of synaptotagmin is required for synaptic transmission in vivo. Nature 418, 340-344 (2002).
    • (2002) Nature , vol.418 , pp. 340-344
    • Mackler, J.M.1    Drummond, J.A.2    Loewen, C.A.3    Robinson, I.M.4    Reist, N.E.5
  • 5
    • 0037040890 scopus 로고    scopus 로고
    • Synaptotagmins: Why so many?
    • Südhof, T.C. Synaptotagmins: why so many? J. Biol. Chem. 277, 7629-7632 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 7629-7632
    • Südhof, T.C.1
  • 6
    • 0035078239 scopus 로고    scopus 로고
    • Genetic and molecular analysis of the synaptotagmin family
    • Adolfsen, B. & Littleton, J.T. Genetic and molecular analysis of the synaptotagmin family. Cell Mol. Life Sci. 58, 393-402 (2001).
    • (2001) Cell Mol. Life Sci. , vol.58 , pp. 393-402
    • Adolfsen, B.1    Littleton, J.T.2
  • 8
    • 0035924571 scopus 로고    scopus 로고
    • Three-dimensional structure of the synaptotagmin 1 c(2)b-domain. Synaptotagmin 1 as a phospholipid binding machine
    • Fernandez, I. et al. Three-dimensional structure of the synaptotagmin 1 c(2)b-domain. Synaptotagmin 1 as a phospholipid binding machine. Neuron 32, 1057-1069 (2001).
    • (2001) Neuron , vol.32 , pp. 1057-1069
    • Fernandez, I.1
  • 10
    • 0032527312 scopus 로고    scopus 로고
    • 2+ binding to synaptotagmin: How many Ca2+ ions bind to the tip of a C2-domain?
    • 2+ binding to synaptotagmin: how many Ca2+ ions bind to the tip of a C2-domain? EMBO J. 17, 3921-3930 (1998).
    • (1998) EMBO J. , vol.17 , pp. 3921-3930
    • Ubach, J.1    Zhang, X.2    Shao, X.3    Südhof, T.C.4    Rizo, J.5
  • 12
    • 0036307988 scopus 로고    scopus 로고
    • Synaptotagmin function in dense core vesicle exocytosis studied in cracked PC12 cells
    • Shin, O.H., Rizo, J. & Südhof, T.C. Synaptotagmin function in dense core vesicle exocytosis studied in cracked PC12 cells. Nat. Neurosci. 5, 649-656 (2002).
    • (2002) Nat. Neurosci. , vol.5 , pp. 649-656
    • Shin, O.H.1    Rizo, J.2    Südhof, T.C.3
  • 13
    • 0032497406 scopus 로고    scopus 로고
    • Mechanism of phospholipid binding by the C2A-domain of synaptotagmin I
    • Zhang, X., Rizo, J. & Südhof, T.C. Mechanism of phospholipid binding by the C2A-domain of synaptotagmin I. Biochemistry 37, 12395-12403 (1998).
    • (1998) Biochemistry , vol.37 , pp. 12395-12403
    • Zhang, X.1    Rizo, J.2    Südhof, T.C.3
  • 14
    • 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).
    • (1998) J. Biol. Chem. , vol.273 , pp. 13995-14001
    • Chapman, E.R.1    Davis, A.F.2
  • 15
    • 0036318064 scopus 로고    scopus 로고
    • Role of electrostatic and hydrophobic interactions in ca(2+)-dependent phospholipid binding by the c(2)a-domain from synaptotagmin I
    • Gerber, S.H., Rizo, J. & Südhof, T.C. Role of electrostatic and hydrophobic interactions in ca(2+)-dependent phospholipid binding by the c(2)a-domain from synaptotagmin I. Diabetes 51 (suppl. 1), 512-518(2002).
    • (2002) Diabetes , vol.51 , Issue.SUPPL. 1 , pp. 512-518
    • Gerber, S.H.1    Rizo, J.2    Südhof, T.C.3
  • 16
    • 0036469818 scopus 로고    scopus 로고
    • Synaptotagmins form a hierarchy of exocytotic Ca(2+) sensors with distinct Ca(2+) affinities
    • Sugita, S., Shin, O.H., Man, W., Lao, Y. & Südhof, T.C. Synaptotagmins form a hierarchy of exocytotic Ca(2+) sensors with distinct Ca(2+) affinities. EMBO J. 21, 270-280 (2002).
    • (2002) EMBO J. , vol.21 , pp. 270-280
    • Sugita, S.1    Shin, O.H.2    Man, W.3    Lao, Y.4    Südhof, T.C.5
  • 17
    • 0000635864 scopus 로고    scopus 로고
    • Synaptotagmin I and IV define distinct populations of neuronal transport vesicles
    • Berton, F. et al. Synaptotagmin I and IV define distinct populations of neuronal transport vesicles. Eur. J. Neurosci. 12, 1294-1302 (2000).
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 1294-1302
    • Berton, F.1
  • 18
    • 0028901750 scopus 로고
    • Synaptotagmin IV is an immediate early gene induced by depolarization in PC12 cells and in brain
    • Vician, L. et al. Synaptotagmin IV is an immediate early gene induced by depolarization in PC12 cells and in brain. Proc. Natl. Acad. Sci. USA 92, 2164-2168 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2164-2168
    • Vician, L.1
  • 19
    • 0030952081 scopus 로고    scopus 로고
    • The evolutionary pressure to inactivate. A subclass of synaptotagmins with an amino acid substitution that abolishes Ca2+ binding
    • von Poser, C., Ichtchenko, K., Shao, X., Rizo, J. & Südhof, T.C. The evolutionary pressure to inactivate. A subclass of synaptotagmins with an amino acid substitution that abolishes Ca2+ binding. J. Biol. Chem. 272, 14314-14319 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 14314-14319
    • Von Poser, C.1    Ichtchenko, K.2    Shao, X.3    Rizo, J.4    Südhof, T.C.5
  • 20
    • 0033584339 scopus 로고    scopus 로고
    • Synaptic function modulated by changes in the ratio of synaptotagmin I and IV
    • Littleton, J.T., Serano, T.L., Rubin, G.M., Ganetzky, B. & Chapman, E.R. Synaptic function modulated by changes in the ratio of synaptotagmin I and IV. Nature 400, 757-760(1999).
    • (1999) Nature , vol.400 , pp. 757-760
    • Littleton, J.T.1    Serano, T.L.2    Rubin, G.M.3    Ganetzky, B.4    Chapman, E.R.5
  • 21
    • 0035798162 scopus 로고    scopus 로고
    • Synaptotagmin modulation of fusion pore kinetics in regulated exocytosis of dense-core vesicles
    • Wang, C.T. et al. Synaptotagmin modulation of fusion pore kinetics in regulated exocytosis of dense-core vesicles. Science294, 1111-1115 (2001).
    • (2001) Science , vol.294 , pp. 1111-1115
    • Wang, C.T.1
  • 22
    • 0041858035 scopus 로고    scopus 로고
    • Different domains of synaptotagmin control the choice between kiss-and-run and full fusion
    • Wang, C.T. et al. Different domains of synaptotagmin control the choice between kiss-and-run and full fusion. Nature 424, 943-947 (2003).
    • (2003) Nature , vol.424 , pp. 943-947
    • Wang, C.T.1
  • 23
    • 0037130260 scopus 로고    scopus 로고
    • Synaptotagmins I IV promote transmitter release independently of Ca(2+) binding in the C(2)A domain
    • Robinson, I.M., Ranjan, R. & Schwarz, T.L. Synaptotagmins I and IV promote transmitter release independently of Ca(2+) binding in the C(2)A domain. Nature 418, 336-340 (2002).
    • (2002) Nature , vol.418 , pp. 336-340
    • Robinson, I.M.1    Ranjan, R.2    Schwarz, T.L.3
  • 24
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. & Sander, C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138 (1993).
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 26
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F. et al. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293 (1995).
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1
  • 27
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson, B.A. & Blevins, R.A. NMRView: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4, 603-614(1994).
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 28
    • 0037427025 scopus 로고    scopus 로고
    • 2+ binding site of the synaptotagmin I C2B domain triggers fast exocytosis without stimulating SNARE interactions
    • 2+ binding site of the synaptotagmin I C2B domain triggers fast exocytosis without stimulating SNARE interactions. Neuron 37, 99-108 (2003).
    • (2003) Neuron , vol.37 , pp. 99-108
    • Shin, O.H.1
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 31
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G.N., Vagin, A.A. & Dodson, E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255 (1997).
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 32
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4.-The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 33
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, TA., Zou, J.Y., Cowan, S.W. and Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 35
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


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