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Volumn 43, Issue 13, 2004, Pages 3987-3995

The Tricalbin C2 Domains: Lipid-Binding Properties of a Novel, Synaptotagmin-Like Yeast Protein Family

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CALCIUM; LIPIDS; OLIGOMERS; PROTEINS;

EID: 1842486857     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036082w     Document Type: Article
Times cited : (42)

References (36)
  • 1
    • 0037040890 scopus 로고    scopus 로고
    • Synaptotagmins: Why so many?
    • Sudhof, T. C. (2001) Synaptotagmins: why so many? J. Biol. Chem. 277, 7629-7632.
    • (2001) J. Biol. Chem. , vol.277 , pp. 7629-7632
    • Sudhof, T.C.1
  • 2
    • 0030222771 scopus 로고    scopus 로고
    • Synaptotagmins: C2 domain proteins that regulate membrane traffic
    • Sudhof, T. C., and Rizo, J. (1996) Synaptotagmins: C2 domain proteins that regulate membrane traffic, Neuron 17, 379-388.
    • (1996) Neuron , vol.17 , pp. 379-388
    • Sudhof, T.C.1    Rizo, J.2
  • 3
    • 0037151075 scopus 로고    scopus 로고
    • Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains
    • Davis, D. B., Doherty, K. R., Delmonte, A. J., and McNally, E. M. (2002) Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains, J. Biol. Chem. 277, 22883-22888.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22883-22888
    • Davis, D.B.1    Doherty, K.R.2    Delmonte, A.J.3    McNally, E.M.4
  • 4
    • 0037027739 scopus 로고    scopus 로고
    • Synaptotagmin I functions as a calcium sensor to synchronize neurotransmitter release
    • Yoshihara, M., and Littleton, J. T. (2002) Synaptotagmin I functions as a calcium sensor to synchronize neurotransmitter release, Neuron 36, 897-908.
    • (2002) Neuron , vol.36 , pp. 897-908
    • Yoshihara, M.1    Littleton, J.T.2
  • 5
    • 0027960576 scopus 로고
    • Synergistic membrane interactions of the two C2 domains of synaptotagmin
    • Damer, C. K., and Creutz, C. E. (1994) Synergistic membrane interactions of the two C2 domains of synaptotagmin, J. Biol. Chem. 49, 31115-31123.
    • (1994) J. Biol. Chem. , vol.49 , pp. 31115-31123
    • Damer, C.K.1    Creutz, C.E.2
  • 6
    • 0035904238 scopus 로고    scopus 로고
    • 2+ binding sites that cooperate to engage t-SNAREs and trigger exocytosis
    • 2+ binding sites that cooperate to engage t-SNAREs and trigger exocytosis, J. Cell Biol. 154, 1117-1123.
    • (2001) J. Cell Biol. , vol.154 , pp. 1117-1123
    • Earles, C.A.1    Bai, J.2    Wang, P.3    Chapman, E.R.4
  • 7
    • 23544467279 scopus 로고    scopus 로고
    • The tricalbins: Yeast synaptotagmin homologues?
    • Creutz, C. E., and Snyder, S. L. (1999) The tricalbins: yeast synaptotagmin homologues? Mol. Biol. Cell 10, 215a.
    • (1999) Mol. Biol. Cell , vol.10
    • Creutz, C.E.1    Snyder, S.L.2
  • 8
    • 0035078239 scopus 로고    scopus 로고
    • Genetic and molecular analysis of the synaptotagmin family
    • Adolfsen, B., and Littleton, J. T. (2000) Genetic and molecular analysis of the synaptotagmin family, Cell. Mol. Life Sci. 58, 393-402.
    • (2000) Cell. Mol. Life Sci. , vol.58 , pp. 393-402
    • Adolfsen, B.1    Littleton, J.T.2
  • 9
    • 0038647468 scopus 로고    scopus 로고
    • Molecular cloning, expression, and characterization of a novel class of synaptotagmin (SytXIV) conserved from Drosophila to humans
    • Fukuda, M. (2003) Molecular cloning, expression, and characterization of a novel class of synaptotagmin (SytXIV) conserved from Drosophila to humans, J. Biochem. 133, 641-649.
    • (2003) J. Biochem. , vol.133 , pp. 641-649
    • Fukuda, M.1
  • 10
    • 1842442169 scopus 로고    scopus 로고
    • Characterization of the yeast tricalbins: Membrane-bound multi-C2 domain proteins that form complexes involved in membrane trafficking
    • submitted for publication
    • Creutz, C. E., Snyder, S. L., and Schulz, T. A. (2003) Characterization of the yeast tricalbins: membrane-bound multi-C2 domain proteins that form complexes involved in membrane trafficking, Cellular and Molecular Life Sciences, submitted for publication.
    • (2003) Cellular and Molecular Life Sciences
    • Creutz, C.E.1    Snyder, S.L.2    Schulz, T.A.3
  • 11
    • 0345713152 scopus 로고    scopus 로고
    • Disruption of six Saccharomyces cerevisae novel genes and phenotypic analysis of the deletants
    • Zuniga, S., Boskovic, J., Jimenez, A., Ballesta, J. P., and Remacha, M. (1999) Disruption of six Saccharomyces cerevisae novel genes and phenotypic analysis of the deletants, Yeast 15, 945-953.
    • (1999) Yeast , vol.15 , pp. 945-953
    • Zuniga, S.1    Boskovic, J.2    Jimenez, A.3    Ballesta, J.P.4    Remacha, M.5
  • 13
    • 0035968336 scopus 로고    scopus 로고
    • Coordinate control of sphingolipid biosynthesis and multidrug resistance in Saccharomyces cerevisae
    • Hallstrom, T. C., Lambert, L., Schorling, S., Balzi, E., Goffeau, A., and Moye-Rowley, W. S. (2001) Coordinate control of sphingolipid biosynthesis and multidrug resistance in Saccharomyces cerevisae, J. Biol. Chem 276, 23674-23680.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23674-23680
    • Hallstrom, T.C.1    Lambert, L.2    Schorling, S.3    Balzi, E.4    Goffeau, A.5    Moye-Rowley, W.S.6
  • 14
    • 0035430918 scopus 로고    scopus 로고
    • The effects of transcription regulating genes PDR1, pdr1-3 and PDR3 in pleiotropic drug resistance
    • Nawrocki, A., Fey, S. J., Goffeau, A., Roepstorff, P., and Larsen, P. M. (2001) The effects of transcription regulating genes PDR1, pdr1-3 and PDR3 in pleiotropic drug resistance, Proteomics 1, 1022-1032.
    • (2001) Proteomics , vol.1 , pp. 1022-1032
    • Nawrocki, A.1    Fey, S.J.2    Goffeau, A.3    Roepstorff, P.4    Larsen, P.M.5
  • 15
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione 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 glutathione S-transferase, Anal. Biochem. 192, 262-267.
    • (1991) Anal. Biochem. , vol.192 , pp. 262-267
    • Guan, K.L.1    Dixon, J.E.2
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of micrograms quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of micrograms quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0027050183 scopus 로고
    • Phosphoinositide-specific phospholipase C-delta 1 binds with high affinity to phospholipid vesicles containing phosphatidylinositol 4,5-bisphosphate
    • Rebecchi, M., Peterson, A., and McLaughlin, S. (1992) Phosphoinositide-specific phospholipase C-delta 1 binds with high affinity to phospholipid vesicles containing phosphatidylinositol 4,5-bisphosphate, Biochemistry 31, 12742-12747.
    • (1992) Biochemistry , vol.31 , pp. 12742-12747
    • Rebecchi, M.1    Peterson, A.2    McLaughlin, S.3
  • 18
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: Structural and functional diversity
    • Nalefski, E. A., and Falke, J. J. (1996) The C2 domain calcium-binding motif: structural and functional diversity, Protein Sci. 5, 2375-2390.
    • (1996) Protein Sci. , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 20
    • 0032848506 scopus 로고    scopus 로고
    • Lipid compositions of subcellular membranes of an FY1679-derived haploid yeast wild-type strain grown on different carbon sources
    • Tuller, G., Nemec, T., Hrastnik, C., and Daum, G. (1999) Lipid compositions of subcellular membranes of an FY1679-derived haploid yeast wild-type strain grown on different carbon sources, Yeast 15, 1555-1564.
    • (1999) Yeast , vol.15 , pp. 1555-1564
    • Tuller, G.1    Nemec, T.2    Hrastnik, C.3    Daum, G.4
  • 21
    • 0025905908 scopus 로고
    • Calcium-dependent secretory vesicle-binding and lipid-binding proteins of Saccharomyces cerevisae
    • Creutz, C. E., Snyder, S. L., and Kambouris, N. G. (1991) Calcium-dependent secretory vesicle-binding and lipid-binding proteins of Saccharomyces cerevisae, Yeast 7, 229-244.
    • (1991) Yeast , vol.7 , pp. 229-244
    • Creutz, C.E.1    Snyder, S.L.2    Kambouris, N.G.3
  • 22
    • 0032217266 scopus 로고    scopus 로고
    • Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body
    • Odorizzi, G., Babst, M., and Emr, S. D. (1998) Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body, Cell 95, 847-858.
    • (1998) Cell , vol.95 , pp. 847-858
    • Odorizzi, G.1    Babst, M.2    Emr, S.D.3
  • 23
    • 0032487577 scopus 로고    scopus 로고
    • Fab1p is essential for PtdIns(3)P 5-kinase activity and the maintenance of vacuolar size and membrane homeostasis
    • Gary, J. D., Wurmser, A. E., Bonangelino, C. J., Weisman, L. S., and Emr, S. D. (1998) Fab1p is essential for PtdIns(3)P 5-kinase activity and the maintenance of vacuolar size and membrane homeostasis, J. Cell Biol. 143, 65-79.
    • (1998) J. Cell Biol. , vol.143 , pp. 65-79
    • Gary, J.D.1    Wurmser, A.E.2    Bonangelino, C.J.3    Weisman, L.S.4    Emr, S.D.5
  • 26
    • 0037024343 scopus 로고    scopus 로고
    • Phospholipase C is required for glucose-induced calcium influx in budding yeast
    • Tisi, R., Baldassa, S., Belotti, F., and Martegani, E. (2002) Phospholipase C is required for glucose-induced calcium influx in budding yeast, FEBS Lett. 520, 133-138.
    • (2002) FEBS Lett. , vol.520 , pp. 133-138
    • Tisi, R.1    Baldassa, S.2    Belotti, F.3    Martegani, E.4
  • 28
    • 0024472758 scopus 로고
    • 2+-sensitive fluorescence dye indo-1
    • 2+-sensitive fluorescence dye indo-1, FEBS Lett. 256, 55-61.
    • (1989) FEBS Lett. , vol.256 , pp. 55-61
    • Halachmi, D.1    Eilam, Y.2
  • 29
    • 0037033784 scopus 로고    scopus 로고
    • 2+ release in yeast is triggered by hypertonic shock and mediated by a TRP channel homologue
    • 2+ release in yeast is triggered by hypertonic shock and mediated by a TRP channel homologue, J. Cell Biol. 156, 29-34.
    • (2002) J. Cell Biol. , vol.156 , pp. 29-34
    • Denis, V.M.1    Cyert, M.S.2
  • 30
    • 0032951128 scopus 로고    scopus 로고
    • Calcium-dependent oligomerization of synaptotagmins I and II. Synaptotagmins I and II are localized on the same synaptic vesicle and heterodimerize in the presence of calcium
    • Osbome, S. L., Herreros, J., Bastiaens, P. I., and Schiavo, G. (1999) Calcium-dependent oligomerization of synaptotagmins I and II. Synaptotagmins I and II are localized on the same synaptic vesicle and heterodimerize in the presence of calcium, J. Biol. Chem. 274, 59-66.
    • (1999) J. Biol. Chem. , vol.274 , pp. 59-66
    • Osbome, S.L.1    Herreros, J.2    Bastiaens, P.I.3    Schiavo, G.4
  • 32
    • 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., and Chapman, E. R. (1999) Synaptic function modulated by changes in the ratio of synaptotagmin I and IV, Nature 400, 757-760.
    • (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
  • 34
    • 0029036903 scopus 로고
    • Identification of a nonneuronal form of synaptotagmin
    • Hudson, A. W., and Birnbaum, M. J. (1995) Identification of a nonneuronal form of synaptotagmin, Proc. Natl. Acad. Sci. U.S.A. 92, 5895-5899.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 5895-5899
    • Hudson, A.W.1    Birnbaum, M.J.2


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