메뉴 건너뛰기




Volumn 1761, Issue 8, 2006, Pages 838-849

Membrane binding and subcellular targeting of C2 domains

Author keywords

C2 domain; Calcium; Lipid; Membrane; Membrane trafficking; Signaling; Subcellular localization

Indexed keywords

CALCIUM ION; LIPID;

EID: 33748324514     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2006.06.014     Document Type: Review
Times cited : (228)

References (131)
  • 1
    • 0023764824 scopus 로고
    • The molecular heterogeneity of protein kinase C and its implications for cellular regulation
    • Nishizuka Y. The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature 334 (1988) 661-665
    • (1988) Nature , vol.334 , pp. 661-665
    • Nishizuka, Y.1
  • 2
    • 0024412493 scopus 로고
    • The protein kinase C family: heterogeneity and its implications
    • Kikkawa U., Kishimoto A., and Nishizuka Y. The protein kinase C family: heterogeneity and its implications. Annu. Rev. Biochem. 58 (1989) 31-44
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 31-44
    • Kikkawa, U.1    Kishimoto, A.2    Nishizuka, Y.3
  • 4
    • 0027276016 scopus 로고
    • Ca(2+)-independent protein kinase Cs contain an amino-terminal domain similar to the C2 consensus sequence
    • Sossin W.S., and Schwartz J.H. Ca(2+)-independent protein kinase Cs contain an amino-terminal domain similar to the C2 consensus sequence. Trends Biochem. Sci. 18 (1993) 207-208
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 207-208
    • Sossin, W.S.1    Schwartz, J.H.2
  • 5
    • 0025270739 scopus 로고
    • Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C
    • Perin M.S., Fried V.A., Mignery G.A., Jahn R., and Sudhof T.C. Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C. Nature 345 (1990) 260-263
    • (1990) Nature , vol.345 , pp. 260-263
    • Perin, M.S.1    Fried, V.A.2    Mignery, G.A.3    Jahn, R.4    Sudhof, T.C.5
  • 6
    • 0025810578 scopus 로고
    • A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP
    • Clark J.D., Lin L.L., Kriz R.W., Ramesha C.S., Sultzman L.A., Lin A.Y., Milona N., and Knopf J.L. A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP. Cell 65 (1991) 1043-1051
    • (1991) Cell , vol.65 , pp. 1043-1051
    • Clark, J.D.1    Lin, L.L.2    Kriz, R.W.3    Ramesha, C.S.4    Sultzman, L.A.5    Lin, A.Y.6    Milona, N.7    Knopf, J.L.8
  • 7
    • 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. A single C2 domain from synaptotagmin I is sufficient for high affinity Ca2+/phospholipid binding. J. Biol. Chem. 268 (1993) 26386-26390
    • (1993) J. Biol. Chem. , vol.268 , pp. 26386-26390
    • Davletov, B.A.1    Sudhof, T.C.2
  • 8
    • 0028068586 scopus 로고
    • Calcium-dependent interaction of the cytoplasmic region of synaptotagmin with membranes. Autonomous function of a single C2-homologous domain
    • Chapman E.R., and Jahn R. Calcium-dependent interaction of the cytoplasmic region of synaptotagmin with membranes. Autonomous function of a single C2-homologous domain. J. Biol. Chem. 269 (1994) 5735-5741
    • (1994) J. Biol. Chem. , vol.269 , pp. 5735-5741
    • Chapman, E.R.1    Jahn, R.2
  • 9
    • 0028339812 scopus 로고
    • Delineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca(2+)-dependent lipid-binding domain and a Ca(2+)-independent catalytic domain
    • Nalefski E.A., Sultzman L.A., Martin D.M., Kriz R.W., Towler P.S., Knopf J.L., and Clark J.D. Delineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca(2+)-dependent lipid-binding domain and a Ca(2+)-independent catalytic domain. J. Biol. Chem. 269 (1994) 18239-18249
    • (1994) J. Biol. Chem. , vol.269 , pp. 18239-18249
    • Nalefski, E.A.1    Sultzman, L.A.2    Martin, D.M.3    Kriz, R.W.4    Towler, P.S.5    Knopf, J.L.6    Clark, J.D.7
  • 11
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: identification of signaling domains
    • Schultz J., Milpetz F., Bork P., and Ponting C.P. SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 5857-5864
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 13
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: a prototypical calcium sensor
    • Chin D., and Means A.R. Calmodulin: a prototypical calcium sensor. Trends Cell Biol. 10 (2000) 322-328
    • (2000) Trends Cell Biol. , vol.10 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 14
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: from structure to function
    • Gerke V., and Moss S.E. Annexins: from structure to function. Physiol. Rev. 82 (2002) 331-371
    • (2002) Physiol. Rev. , vol.82 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 15
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: structural and functional diversity
    • Nalefski E.A., and Falke J.J. The C2 domain calcium-binding motif: structural and functional diversity. Protein Sci. 5 (1996) 2375-2390
    • (1996) Protein Sci. , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 16
    • 0032568662 scopus 로고    scopus 로고
    • C2-domains, structure and function of a universal Ca2+-binding domain
    • Rizo J., and Sudhof T.C. C2-domains, structure and function of a universal Ca2+-binding domain. J. Biol. Chem. 273 (1998) 15879-15882
    • (1998) J. Biol. Chem. , vol.273 , pp. 15879-15882
    • Rizo, J.1    Sudhof, T.C.2
  • 17
    • 0035980111 scopus 로고    scopus 로고
    • Membrane targeting by C1 and C2 domains
    • Cho W. Membrane targeting by C1 and C2 domains. J. Biol. Chem. 276 (2001) 32407-32410
    • (2001) J. Biol. Chem. , vol.276 , pp. 32407-32410
    • Cho, W.1
  • 18
    • 0028986240 scopus 로고
    • Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold
    • Sutton R.B., Davletov B.A., Berghuis A.M., Sudhof T.C., and Sprang S.R. Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold. Cell 80 (1995) 929-938
    • (1995) Cell , vol.80 , pp. 929-938
    • Sutton, R.B.1    Davletov, B.A.2    Berghuis, A.M.3    Sudhof, T.C.4    Sprang, S.R.5
  • 19
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta
    • Essen L.O., Perisic O., Cheung R., Katan M., and Williams R.L. Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta. Nature 380 (1996) 595-602
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 20
    • 0030736867 scopus 로고    scopus 로고
    • The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity
    • Gillmor S.A., Villasenor A., Fletterick R., Sigal E., and Browner M.F. The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity. Nat. Struct. Biol. 4 (1997) 1003-1009
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 1003-1009
    • Gillmor, S.A.1    Villasenor, A.2    Fletterick, R.3    Sigal, E.4    Browner, M.F.5
  • 21
    • 0031892519 scopus 로고    scopus 로고
    • Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2
    • Perisic O., Fong S., Lynch D.E., Bycroft M., and Williams R.L. Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2. J. Biol. Chem. 273 (1998) 1596-1604
    • (1998) J. Biol. Chem. , vol.273 , pp. 1596-1604
    • Perisic, O.1    Fong, S.2    Lynch, D.E.3    Bycroft, M.4    Williams, R.L.5
  • 22
    • 0032533457 scopus 로고    scopus 로고
    • Structure of the protein kinase Cbeta phospholipid-binding C2 domain complexed with Ca2+
    • Sutton R.B., and Sprang S.R. Structure of the protein kinase Cbeta phospholipid-binding C2 domain complexed with Ca2+. Structure 6 (1998) 1395-1405
    • (1998) Structure , vol.6 , pp. 1395-1405
    • Sutton, R.B.1    Sprang, S.R.2
  • 24
    • 0033615538 scopus 로고    scopus 로고
    • Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association
    • Lee J.O., Yang H., Georgescu M.M., Di Cristofano A., Maehama T., Shi Y., Dixon J.E., Pandolfi P., and Pavletich N.P. Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. Cell 99 (1999) 323-334
    • (1999) Cell , vol.99 , pp. 323-334
    • Lee, J.O.1    Yang, H.2    Georgescu, M.M.3    Di Cristofano, A.4    Maehama, T.5    Shi, Y.6    Dixon, J.E.7    Pandolfi, P.8    Pavletich, N.P.9
  • 25
    • 0035943428 scopus 로고    scopus 로고
    • Structure of the C2 domain from novel protein kinase Cepsilon. A membrane binding model for Ca(2+)-independent C2 domains
    • Ochoa W.F., Garcia-Garcia J., Fita I., Corbalan-Garcia S., Verdaguer N., and Gomez-Fernandez J.C. Structure of the C2 domain from novel protein kinase Cepsilon. A membrane binding model for Ca(2+)-independent C2 domains. J. Mol. Biol. 311 (2001) 837-849
    • (2001) J. Mol. Biol. , vol.311 , pp. 837-849
    • Ochoa, W.F.1    Garcia-Garcia, J.2    Fita, I.3    Corbalan-Garcia, S.4    Verdaguer, N.5    Gomez-Fernandez, J.C.6
  • 28
    • 28244498659 scopus 로고    scopus 로고
    • Insights from the X-ray crystal structure of coral 8R-lipoxygenase: calcium activation via a C2-like domain and a structural basis of product chirality
    • Oldham M.L., Brash A.R., and Newcomer M.E. Insights from the X-ray crystal structure of coral 8R-lipoxygenase: calcium activation via a C2-like domain and a structural basis of product chirality. J. Biol. Chem. 280 (2005) 39545-39552
    • (2005) J. Biol. Chem. , vol.280 , pp. 39545-39552
    • Oldham, M.L.1    Brash, A.R.2    Newcomer, M.E.3
  • 29
    • 17444403210 scopus 로고    scopus 로고
    • The C2 domain of PKCdelta is a phosphotyrosine binding domain
    • Benes C.H., Wu N., Elia A.E., Dharia T., Cantley L.C., and Soltoff S.P. The C2 domain of PKCdelta is a phosphotyrosine binding domain. Cell 121 (2005) 271-280
    • (2005) Cell , vol.121 , pp. 271-280
    • Benes, C.H.1    Wu, N.2    Elia, A.E.3    Dharia, T.4    Cantley, L.C.5    Soltoff, S.P.6
  • 31
    • 0029666292 scopus 로고    scopus 로고
    • Bipartite Ca2+-binding motif in C2 domains of synaptotagmin and protein kinase C
    • Shao X., Davletov B.A., Sutton R.B., Sudhof T.C., and Rizo J. Bipartite Ca2+-binding motif in C2 domains of synaptotagmin and protein kinase C. Science 273 (1996) 248-251
    • (1996) Science , vol.273 , pp. 248-251
    • Shao, X.1    Davletov, B.A.2    Sutton, R.B.3    Sudhof, T.C.4    Rizo, J.5
  • 32
    • 0032541943 scopus 로고    scopus 로고
    • Solution structures of the Ca2+-free and Ca2+-bound C2A domain of synaptotagmin I: does Ca2+ induce a conformational change?
    • Shao X., Fernandez I., Sudhof T.C., and Rizo J. Solution structures of the Ca2+-free and Ca2+-bound C2A domain of synaptotagmin I: does Ca2+ induce a conformational change?. Biochemistry 37 (1998) 16106-16115
    • (1998) Biochemistry , vol.37 , pp. 16106-16115
    • Shao, X.1    Fernandez, I.2    Sudhof, T.C.3    Rizo, J.4
  • 34
    • 0035924571 scopus 로고    scopus 로고
    • Three-dimensional structure of the synaptotagmin 1 C2B-domain: synaptotagmin 1 as a phospholipid binding machine
    • Fernandez I., Arac D., Ubach J., Gerber S.H., Shin O., Gao Y., Anderson R.G., Sudhof T.C., and Rizo J. Three-dimensional structure of the synaptotagmin 1 C2B-domain: synaptotagmin 1 as a phospholipid binding machine. Neuron 32 (2001) 1057-1069
    • (2001) Neuron , vol.32 , pp. 1057-1069
    • Fernandez, I.1    Arac, D.2    Ubach, J.3    Gerber, S.H.4    Shin, O.5    Gao, Y.6    Anderson, R.G.7    Sudhof, T.C.8    Rizo, J.9
  • 35
    • 0842269784 scopus 로고    scopus 로고
    • A conformational switch in the Piccolo C2A domain regulated by alternative splicing
    • Garcia J., Gerber S.H., Sugita S., Sudhof T.C., and Rizo J. A conformational switch in the Piccolo C2A domain regulated by alternative splicing. Nat. Struct. Mol. Biol. 11 (2004) 45-53
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 45-53
    • Garcia, J.1    Gerber, S.H.2    Sugita, S.3    Sudhof, T.C.4    Rizo, J.5
  • 36
    • 0032504259 scopus 로고    scopus 로고
    • Mutagenesis of the C2 domain of protein kinase C-alpha. Differential roles of Ca2+ ligands and membrane binding residues
    • Medkova M., and Cho W. Mutagenesis of the C2 domain of protein kinase C-alpha. Differential roles of Ca2+ ligands and membrane binding residues. J. Biol. Chem. 273 (1998) 17544-17552
    • (1998) J. Biol. Chem. , vol.273 , pp. 17544-17552
    • Medkova, M.1    Cho, W.2
  • 37
    • 0032527312 scopus 로고    scopus 로고
    • Ca2+ binding to synaptotagmin: how many Ca2+ ions bind to the tip of a C2-domain?
    • Ubach J., Zhang X., Shao X., Sudhof T.C., and Rizo J. Ca2+ binding to synaptotagmin: how many Ca2+ ions bind to the tip of a C2-domain?. EMBO J. 17 (1998) 3921-3930
    • (1998) EMBO J. , vol.17 , pp. 3921-3930
    • Ubach, J.1    Zhang, X.2    Shao, X.3    Sudhof, T.C.4    Rizo, J.5
  • 38
    • 0033515664 scopus 로고    scopus 로고
    • A structure-function study of the C2 domain of cytosolic phospholipase A2. Identification of essential calcium ligands and hydrophobic membrane binding residues
    • Bittova L., Sumandea M., and Cho W. A structure-function study of the C2 domain of cytosolic phospholipase A2. Identification of essential calcium ligands and hydrophobic membrane binding residues. J. Biol. Chem. 274 (1999) 9665-9672
    • (1999) J. Biol. Chem. , vol.274 , pp. 9665-9672
    • Bittova, L.1    Sumandea, M.2    Cho, W.3
  • 39
    • 0036479136 scopus 로고    scopus 로고
    • Membrane targeting of C2 domains of phospholipase C-delta isoforms
    • Ananthanarayanan B., Das S., Rhee S.G., Murray D., and Cho W. Membrane targeting of C2 domains of phospholipase C-delta isoforms. J. Biol. Chem. 277 (2002) 3568-3575
    • (2002) J. Biol. Chem. , vol.277 , pp. 3568-3575
    • Ananthanarayanan, B.1    Das, S.2    Rhee, S.G.3    Murray, D.4    Cho, W.5
  • 40
    • 0031019191 scopus 로고    scopus 로고
    • Synaptotagmin-syntaxin interaction: the C2 domain as a Ca2+-dependent electrostatic switch
    • Shao X., Li C., Fernandez I., Zhang X., Sudhof T.C., and Rizo J. Synaptotagmin-syntaxin interaction: the C2 domain as a Ca2+-dependent electrostatic switch. Neuron 18 (1997) 133-142
    • (1997) Neuron , vol.18 , pp. 133-142
    • Shao, X.1    Li, C.2    Fernandez, I.3    Zhang, X.4    Sudhof, T.C.5    Rizo, J.6
  • 41
    • 0036161583 scopus 로고    scopus 로고
    • Electrostatic control of the membrane targeting of C2 domains
    • Murray D., and Honig B. Electrostatic control of the membrane targeting of C2 domains. Mol. Cell 9 (2002) 145-154
    • (2002) Mol. Cell , vol.9 , pp. 145-154
    • Murray, D.1    Honig, B.2
  • 42
    • 0032497406 scopus 로고    scopus 로고
    • Mechanism of phospholipid binding by the C2A-domain of synaptotagmin I
    • Zhang X., Rizo J., and Sudhof T.C. Mechanism of phospholipid binding by the C2A-domain of synaptotagmin I. Biochemistry 37 (1998) 12395-12403
    • (1998) Biochemistry , vol.37 , pp. 12395-12403
    • Zhang, X.1    Rizo, J.2    Sudhof, T.C.3
  • 43
    • 0033571223 scopus 로고    scopus 로고
    • Ca(2+) bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine
    • Verdaguer N., Corbalan-Garcia S., Ochoa W.F., Fita I., and Gomez-Fernandez J.C. Ca(2+) bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine. EMBO J. 18 (1999) 6329-6338
    • (1999) EMBO J. , vol.18 , pp. 6329-6338
    • Verdaguer, N.1    Corbalan-Garcia, S.2    Ochoa, W.F.3    Fita, I.4    Gomez-Fernandez, J.C.5
  • 45
    • 0037066761 scopus 로고    scopus 로고
    • Molecular basis of the specific subcellular localization of the C2-like domain of 5-lipoxygenase
    • Kulkarni S., Das S., Funk C.D., Murray D., and Cho W. Molecular basis of the specific subcellular localization of the C2-like domain of 5-lipoxygenase. J. Biol. Chem. 277 (2002) 13167-13174
    • (2002) J. Biol. Chem. , vol.277 , pp. 13167-13174
    • Kulkarni, S.1    Das, S.2    Funk, C.D.3    Murray, D.4    Cho, W.5
  • 47
    • 0035884406 scopus 로고    scopus 로고
    • Membrane binding assays for peripheral proteins
    • Cho W., Bittova L., and Stahelin R.V. Membrane binding assays for peripheral proteins. Anal. Biochem. 296 (2001) 153-161
    • (2001) Anal. Biochem. , vol.296 , pp. 153-161
    • Cho, W.1    Bittova, L.2    Stahelin, R.V.3
  • 49
    • 0030612437 scopus 로고    scopus 로고
    • Ca2+-signaling cycle of a membrane-docking C2 domain
    • Nalefski E.A., Slazas M.M., and Falke J.J. Ca2+-signaling cycle of a membrane-docking C2 domain. Biochemistry 36 (1997) 12011-12018
    • (1997) Biochemistry , vol.36 , pp. 12011-12018
    • Nalefski, E.A.1    Slazas, M.M.2    Falke, J.J.3
  • 50
    • 1542569606 scopus 로고    scopus 로고
    • Membrane recognition and targeting by lipid-binding domains
    • DiNitto J.P., Cronin T.C., and Lambright D.G. Membrane recognition and targeting by lipid-binding domains. Sci. STKE 2003 (2003) re16
    • (2003) Sci. STKE , vol.2003
    • DiNitto, J.P.1    Cronin, T.C.2    Lambright, D.G.3
  • 51
    • 20544475665 scopus 로고    scopus 로고
    • Membrane-protein interactions in cell signaling and membrane trafficking
    • Cho W., and Stahelin R.V. Membrane-protein interactions in cell signaling and membrane trafficking. Annu. Rev. Biophys. Biomol. Struct. 34 (2005) 119-151
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , pp. 119-151
    • Cho, W.1    Stahelin, R.V.2
  • 52
    • 0842291506 scopus 로고    scopus 로고
    • PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane
    • Bai J., Tucker W.C., and Chapman E.R. PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane. Nat. Struct. Mol. Biol. 11 (2004) 36-44
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 36-44
    • Bai, J.1    Tucker, W.C.2    Chapman, E.R.3
  • 53
    • 0037648458 scopus 로고    scopus 로고
    • The molecular basis of differential subcellular localization of C2 domains of protein kinase C-alpha and group IVa cytosolic phospholipase A2
    • Stahelin R.V., Rafter J.D., Das S., and Cho W. The molecular basis of differential subcellular localization of C2 domains of protein kinase C-alpha and group IVa cytosolic phospholipase A2. J. Biol. Chem. 278 (2003) 12452-12460
    • (2003) J. Biol. Chem. , vol.278 , pp. 12452-12460
    • Stahelin, R.V.1    Rafter, J.D.2    Das, S.3    Cho, W.4
  • 54
    • 0037015063 scopus 로고    scopus 로고
    • The C2A domain of JFC1 binds to 3′-phosphorylated phosphoinositides and directs plasma membrane association in living cells
    • Catz S.D., Johnson J.L., and Babior B.M. The C2A domain of JFC1 binds to 3′-phosphorylated phosphoinositides and directs plasma membrane association in living cells. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 11652-11657
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 11652-11657
    • Catz, S.D.1    Johnson, J.L.2    Babior, B.M.3
  • 55
    • 0031915943 scopus 로고    scopus 로고
    • Independent folding and ligand specificity of the C2 calcium-dependent lipid binding domain of cytosolic phospholipase A2
    • Nalefski E.A., McDonagh T., Somers W., Seehra J., Falke J.J., and Clark J.D. Independent folding and ligand specificity of the C2 calcium-dependent lipid binding domain of cytosolic phospholipase A2. J. Biol. Chem. 273 (1998) 1365-1372
    • (1998) J. Biol. Chem. , vol.273 , pp. 1365-1372
    • Nalefski, E.A.1    McDonagh, T.2    Somers, W.3    Seehra, J.4    Falke, J.J.5    Clark, J.D.6
  • 56
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau W.M., Wimley W.C., Gawrisch K., and White S.H. The preference of tryptophan for membrane interfaces. Biochemistry 37 (1998) 14713-14718
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 57
    • 0032558436 scopus 로고    scopus 로고
    • Tryptophan-containing mutant of human (group IIa) secreted phospholipase A2 has a dramatically increased ability to hydrolyze phosphatidylcholine vesicles and cell membranes
    • Baker S.F., Othman R., and Wilton D.C. Tryptophan-containing mutant of human (group IIa) secreted phospholipase A2 has a dramatically increased ability to hydrolyze phosphatidylcholine vesicles and cell membranes. Biochemistry 37 (1998) 13203-13211
    • (1998) Biochemistry , vol.37 , pp. 13203-13211
    • Baker, S.F.1    Othman, R.2    Wilton, D.C.3
  • 58
    • 0033178497 scopus 로고    scopus 로고
    • Interfacial binding of secreted phospholipase A2: more than electrostatics and a major role for tryptophan
    • Gelb M.H., Cho W., and Wilton D.C. Interfacial binding of secreted phospholipase A2: more than electrostatics and a major role for tryptophan. Curr. Opin. Struct. Biol. 9 (1999) 428-432
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 428-432
    • Gelb, M.H.1    Cho, W.2    Wilton, D.C.3
  • 60
    • 0038272084 scopus 로고    scopus 로고
    • Membrane-binding and activation mechanism of PTEN
    • Das S., Dixon J.E., and Cho W. Membrane-binding and activation mechanism of PTEN. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 7491-7496
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7491-7496
    • Das, S.1    Dixon, J.E.2    Cho, W.3
  • 61
    • 2442509573 scopus 로고    scopus 로고
    • The C2 domain of the Rsp5 ubiquitin ligase binds membrane phosphoinositides and directs ubiquitination of endosomal cargo
    • Dunn R., Klos D.A., Adler A.S., and Hicke L. The C2 domain of the Rsp5 ubiquitin ligase binds membrane phosphoinositides and directs ubiquitination of endosomal cargo. J. Cell Biol. 165 (2004) 135-144
    • (2004) J. Cell Biol. , vol.165 , pp. 135-144
    • Dunn, R.1    Klos, D.A.2    Adler, A.S.3    Hicke, L.4
  • 62
    • 0032477809 scopus 로고    scopus 로고
    • The C2 domain of the Ca(2+)-independent protein kinase C Apl II inhibits phorbol ester binding to the C1 domain in a phosphatidic acid-sensitive manner
    • Pepio A.M., and Sossin W.S. The C2 domain of the Ca(2+)-independent protein kinase C Apl II inhibits phorbol ester binding to the C1 domain in a phosphatidic acid-sensitive manner. Biochemistry 37 (1998) 1256-1263
    • (1998) Biochemistry , vol.37 , pp. 1256-1263
    • Pepio, A.M.1    Sossin, W.S.2
  • 63
    • 21244504606 scopus 로고    scopus 로고
    • Diacylglycerol-induced membrane targeting and activation of protein kinase Cepsilon: mechanistic differences between protein kinases Cdelta and Cepsilon
    • Stahelin R.V., Digman M.A., Medkova M., Ananthanarayanan B., Melowic H.R., Rafter J.D., and Cho W. Diacylglycerol-induced membrane targeting and activation of protein kinase Cepsilon: mechanistic differences between protein kinases Cdelta and Cepsilon. J. Biol. Chem. 280 (2005) 19784-19793
    • (2005) J. Biol. Chem. , vol.280 , pp. 19784-19793
    • Stahelin, R.V.1    Digman, M.A.2    Medkova, M.3    Ananthanarayanan, B.4    Melowic, H.R.5    Rafter, J.D.6    Cho, W.7
  • 65
    • 0027986795 scopus 로고
    • Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II
    • Fukuda M., Aruga J., Niinobe M., Aimoto S., and Mikoshiba K. Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II. J. Biol. Chem. 269 (1994) 29206-29211
    • (1994) J. Biol. Chem. , vol.269 , pp. 29206-29211
    • Fukuda, M.1    Aruga, J.2    Niinobe, M.3    Aimoto, S.4    Mikoshiba, K.5
  • 66
    • 0028859443 scopus 로고
    • Functional diversity of C2 domains of synaptotagmin family. Mutational analysis of inositol high polyphosphate binding domain
    • Fukuda M., Kojima T., Aruga J., Niinobe M., and Mikoshiba K. Functional diversity of C2 domains of synaptotagmin family. Mutational analysis of inositol high polyphosphate binding domain. J. Biol. Chem. 270 (1995) 26523-26527
    • (1995) J. Biol. Chem. , vol.270 , pp. 26523-26527
    • Fukuda, M.1    Kojima, T.2    Aruga, J.3    Niinobe, M.4    Mikoshiba, K.5
  • 67
    • 0034663849 scopus 로고    scopus 로고
    • Binding kinetics and ligand specificity for the interactions of the C2B domain of synaptogmin II with inositol polyphosphates and phosphoinositides
    • Mehrotra B., Myszka D.G., and Prestwich G.D. Binding kinetics and ligand specificity for the interactions of the C2B domain of synaptogmin II with inositol polyphosphates and phosphoinositides. Biochemistry 39 (2000) 9679-9686
    • (2000) Biochemistry , vol.39 , pp. 9679-9686
    • Mehrotra, B.1    Myszka, D.G.2    Prestwich, G.D.3
  • 69
    • 0037638716 scopus 로고    scopus 로고
    • A new phosphatidylinositol 4,5-bisphosphate-binding site located in the C2 domain of protein kinase Calpha
    • Corbalan-Garcia S., Garcia-Garcia J., Rodriguez-Alfaro J.A., and Gomez-Fernandez J.C. A new phosphatidylinositol 4,5-bisphosphate-binding site located in the C2 domain of protein kinase Calpha. J. Biol. Chem. 278 (2003) 4972-4980
    • (2003) J. Biol. Chem. , vol.278 , pp. 4972-4980
    • Corbalan-Garcia, S.1    Garcia-Garcia, J.2    Rodriguez-Alfaro, J.A.3    Gomez-Fernandez, J.C.4
  • 70
    • 20444371635 scopus 로고    scopus 로고
    • Ceramide 1-phosphate acts as a positive allosteric activator of group IVA cytosolic phospholipase A2 alpha and enhances the interaction of the enzyme with phosphatidylcholine
    • Subramanian P., Stahelin R.V., Szulc Z., Bielawska A., Cho W., and Chalfant C.E. Ceramide 1-phosphate acts as a positive allosteric activator of group IVA cytosolic phospholipase A2 alpha and enhances the interaction of the enzyme with phosphatidylcholine. J. Biol. Chem. 280 (2005) 17601-17607
    • (2005) J. Biol. Chem. , vol.280 , pp. 17601-17607
    • Subramanian, P.1    Stahelin, R.V.2    Szulc, Z.3    Bielawska, A.4    Cho, W.5    Chalfant, C.E.6
  • 72
    • 0346493036 scopus 로고    scopus 로고
    • Role of the lysine-rich cluster of the C2 domain in the phosphatidylserine-dependent activation of PKCalpha
    • Rodriguez-Alfaro J.A., Gomez-Fernandez J.C., and Corbalan-Garcia S. Role of the lysine-rich cluster of the C2 domain in the phosphatidylserine-dependent activation of PKCalpha. J. Mol. Biol. 335 (2004) 1117-1129
    • (2004) J. Mol. Biol. , vol.335 , pp. 1117-1129
    • Rodriguez-Alfaro, J.A.1    Gomez-Fernandez, J.C.2    Corbalan-Garcia, S.3
  • 73
    • 19644373567 scopus 로고    scopus 로고
    • The ATP-dependent membrane localization of protein kinase Calpha is regulated by Ca2+ influx and phosphatidylinositol 4,5-bisphosphate in differentiated PC12 cells
    • Marin-Vicente C., Gomez-Fernandez J.C., and Corbalan-Garcia S. The ATP-dependent membrane localization of protein kinase Calpha is regulated by Ca2+ influx and phosphatidylinositol 4,5-bisphosphate in differentiated PC12 cells. Mol. Biol. Cell 16 (2005) 2848-2861
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2848-2861
    • Marin-Vicente, C.1    Gomez-Fernandez, J.C.2    Corbalan-Garcia, S.3
  • 74
    • 30044437467 scopus 로고    scopus 로고
    • Specific translocation of protein kinase Calpha to the plasma membrane requires both Ca2+ and PIP2 recognition by its C2 domain
    • Evans J.H., Murray D., Leslie C.C., and Falke J.J. Specific translocation of protein kinase Calpha to the plasma membrane requires both Ca2+ and PIP2 recognition by its C2 domain. Mol. Biol. Cell 17 (2006) 56-66
    • (2006) Mol. Biol. Cell , vol.17 , pp. 56-66
    • Evans, J.H.1    Murray, D.2    Leslie, C.C.3    Falke, J.J.4
  • 75
    • 0032563217 scopus 로고    scopus 로고
    • Calcium-dependent membrane penetration is a hallmark of the C2 domain of cytosolic phospholipase A2 whereas the C2A domain of synaptotagmin binds membranes electrostatically
    • Davletov B., Perisic O., and Williams R.L. Calcium-dependent membrane penetration is a hallmark of the C2 domain of cytosolic phospholipase A2 whereas the C2A domain of synaptotagmin binds membranes electrostatically. J. Biol. Chem. 273 (1998) 19093-19096
    • (1998) J. Biol. Chem. , vol.273 , pp. 19093-19096
    • Davletov, B.1    Perisic, O.2    Williams, R.L.3
  • 76
    • 0033536066 scopus 로고    scopus 로고
    • Interfacial membrane docking of cytosolic phospholipase A2 C2 domain using electrostatic potential-modulated spin relaxation magnetic resonance
    • Ball A., Nielsen R., Gelb M.H., and Robinson B.H. Interfacial membrane docking of cytosolic phospholipase A2 C2 domain using electrostatic potential-modulated spin relaxation magnetic resonance. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 6637-6642
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 6637-6642
    • Ball, A.1    Nielsen, R.2    Gelb, M.H.3    Robinson, B.H.4
  • 78
    • 0242401834 scopus 로고    scopus 로고
    • Membrane-docking loops of the cPLA2 C2 domain: detailed structural analysis of the protein-membrane interface via site-directed spin-labeling
    • Malmberg N.J., Van Buskirk D.R., and Falke J.J. Membrane-docking loops of the cPLA2 C2 domain: detailed structural analysis of the protein-membrane interface via site-directed spin-labeling. Biochemistry 42 (2003) 13227-13240
    • (2003) Biochemistry , vol.42 , pp. 13227-13240
    • Malmberg, N.J.1    Van Buskirk, D.R.2    Falke, J.J.3
  • 79
    • 0037435606 scopus 로고    scopus 로고
    • Membrane-bound orientation and position of the synaptotagmin I C2A domain by site-directed spin labeling
    • Frazier A.A., Roller C.R., Havelka J.J., Hinderliter A., and Cafiso D.S. Membrane-bound orientation and position of the synaptotagmin I C2A domain by site-directed spin labeling. Biochemistry 42 (2003) 96-105
    • (2003) Biochemistry , vol.42 , pp. 96-105
    • Frazier, A.A.1    Roller, C.R.2    Havelka, J.J.3    Hinderliter, A.4    Cafiso, D.S.5
  • 80
    • 0347298574 scopus 로고    scopus 로고
    • C2 domain of protein kinase C alpha: elucidation of the membrane docking surface by site-directed fluorescence and spin labeling
    • Kohout S.C., Corbalan-Garcia S., Gomez-Fernandez J.C., and Falke J.J. C2 domain of protein kinase C alpha: elucidation of the membrane docking surface by site-directed fluorescence and spin labeling. Biochemistry 42 (2003) 1254-1265
    • (2003) Biochemistry , vol.42 , pp. 1254-1265
    • Kohout, S.C.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3    Falke, J.J.4
  • 81
    • 11844254393 scopus 로고    scopus 로고
    • Membrane-bound orientation and position of the synaptotagmin C2B domain determined by site-directed spin labeling
    • Rufener E., Frazier A.A., Wieser C.M., Hinderliter A., and Cafiso D.S. Membrane-bound orientation and position of the synaptotagmin C2B domain determined by site-directed spin labeling. Biochemistry 44 (2005) 18-28
    • (2005) Biochemistry , vol.44 , pp. 18-28
    • Rufener, E.1    Frazier, A.A.2    Wieser, C.M.3    Hinderliter, A.4    Cafiso, D.S.5
  • 82
    • 24144438168 scopus 로고    scopus 로고
    • X-ray reflectivity studies of cPLA2{alpha}-C2 domains adsorbed onto Langmuir monolayers of SOPC
    • Malkova S., Long F., Stahelin R.V., Pingali S.V., Murray D., Cho W., and Schlossman M.L. X-ray reflectivity studies of cPLA2{alpha}-C2 domains adsorbed onto Langmuir monolayers of SOPC. Biophys. J. 89 (2005) 1861-1873
    • (2005) Biophys. J. , vol.89 , pp. 1861-1873
    • Malkova, S.1    Long, F.2    Stahelin, R.V.3    Pingali, S.V.4    Murray, D.5    Cho, W.6    Schlossman, M.L.7
  • 83
    • 0037040890 scopus 로고    scopus 로고
    • Synaptotagmins: why so many?
    • Sudhof T.C. Synaptotagmins: why so many?. J. Biol. Chem. 277 (2002) 7629-7632
    • (2002) J. Biol. Chem. , vol.277 , pp. 7629-7632
    • Sudhof, T.C.1
  • 84
    • 1542286172 scopus 로고    scopus 로고
    • The C2 domains of synaptotagmin-Partners in exocytosis
    • Bai J., and Chapman E.R. The C2 domains of synaptotagmin-Partners in exocytosis. Trends Biochem. Sci. 29 (2004) 143-151
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 143-151
    • Bai, J.1    Chapman, E.R.2
  • 85
    • 1842556210 scopus 로고    scopus 로고
    • Dysferlin and the plasma membrane repair in muscular dystrophy
    • Bansal D., and Campbell K.P. Dysferlin and the plasma membrane repair in muscular dystrophy. Trends Cell Biol. 14 (2004) 206-213
    • (2004) Trends Cell Biol. , vol.14 , pp. 206-213
    • Bansal, D.1    Campbell, K.P.2
  • 86
    • 1842486857 scopus 로고    scopus 로고
    • The tricalbin C2 domains: lipid-binding properties of a novel, synaptotagmin-like yeast protein family
    • Schulz T.A., and Creutz C.E. The tricalbin C2 domains: lipid-binding properties of a novel, synaptotagmin-like yeast protein family. Biochemistry 43 (2004) 3987-3995
    • (2004) Biochemistry , vol.43 , pp. 3987-3995
    • Schulz, T.A.1    Creutz, C.E.2
  • 87
    • 0032951129 scopus 로고    scopus 로고
    • Cloning and preliminary characterization of a 121 kDa protein with multiple predicted C2 domains
    • Morris N.J., Ross S.A., Neveu J.M., Lane W.S., and Lienhard G.E. Cloning and preliminary characterization of a 121 kDa protein with multiple predicted C2 domains. Biochim. Biophys. Acta 1431 (1999) 525-530
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 525-530
    • Morris, N.J.1    Ross, S.A.2    Neveu, J.M.3    Lane, W.S.4    Lienhard, G.E.5
  • 88
    • 12544256900 scopus 로고    scopus 로고
    • Evolutionarily conserved multiple C2 domain proteins with two transmembrane regions (MCTPs) and unusual Ca2+ binding properties
    • Shin O.H., Han W., Wang Y., and Sudhof T.C. Evolutionarily conserved multiple C2 domain proteins with two transmembrane regions (MCTPs) and unusual Ca2+ binding properties. J. Biol. Chem. 280 (2005) 1641-1651
    • (2005) J. Biol. Chem. , vol.280 , pp. 1641-1651
    • Shin, O.H.1    Han, W.2    Wang, Y.3    Sudhof, T.C.4
  • 89
    • 0028791349 scopus 로고
    • Mammalian homologues of Caenorhabditis elegans unc-13 gene define novel family of C2-domain proteins
    • Brose N., Hofmann K., Hata Y., and Sudhof T.C. Mammalian homologues of Caenorhabditis elegans unc-13 gene define novel family of C2-domain proteins. J. Biol. Chem. 270 (1995) 25273-25280
    • (1995) J. Biol. Chem. , vol.270 , pp. 25273-25280
    • Brose, N.1    Hofmann, K.2    Hata, Y.3    Sudhof, T.C.4
  • 90
    • 0034719141 scopus 로고    scopus 로고
    • Biochemical characterization of copine: a ubiquitous Ca2+-dependent, phospholipid-binding protein
    • Tomsig J.L., and Creutz C.E. Biochemical characterization of copine: a ubiquitous Ca2+-dependent, phospholipid-binding protein. Biochemistry 39 (2000) 16163-16175
    • (2000) Biochemistry , vol.39 , pp. 16163-16175
    • Tomsig, J.L.1    Creutz, C.E.2
  • 91
    • 0036709870 scopus 로고    scopus 로고
    • Copines: a ubiquitous family of Ca(2+)-dependent phospholipid-binding proteins
    • Tomsig J.L., and Creutz C.E. Copines: a ubiquitous family of Ca(2+)-dependent phospholipid-binding proteins. Cell. Mol. Life Sci. 59 (2002) 1467-1477
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1467-1477
    • Tomsig, J.L.1    Creutz, C.E.2
  • 92
    • 0029776433 scopus 로고    scopus 로고
    • Calcium-dependent phospholipid binding to the C2A domain of a ubiquitous form of double C2 protein (Doc2 beta)
    • Kojima T., Fukuda M., Aruga J., and Mikoshiba K. Calcium-dependent phospholipid binding to the C2A domain of a ubiquitous form of double C2 protein (Doc2 beta). J. Biochem. (Tokyo) 120 (1996) 671-676
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 671-676
    • Kojima, T.1    Fukuda, M.2    Aruga, J.3    Mikoshiba, K.4
  • 93
    • 2542453015 scopus 로고    scopus 로고
    • Ca(2+)-induced recruitment of the secretory vesicle protein DOC2B to the target membrane
    • Groffen A.J., Brian E.C., Dudok J.J., Kampmeijer J., Toonen R.F., and Verhage M. Ca(2+)-induced recruitment of the secretory vesicle protein DOC2B to the target membrane. J. Biol. Chem. 279 (2004) 23740-23747
    • (2004) J. Biol. Chem. , vol.279 , pp. 23740-23747
    • Groffen, A.J.1    Brian, E.C.2    Dudok, J.J.3    Kampmeijer, J.4    Toonen, R.F.5    Verhage, M.6
  • 94
    • 33645861074 scopus 로고    scopus 로고
    • DOC2A and DOC2B are sensors for neuronal activity with unique calcium-dependent and kinetic properties
    • Groffen A.J., Friedrich R., Brian E.C., Ashery U., and Verhage M. DOC2A and DOC2B are sensors for neuronal activity with unique calcium-dependent and kinetic properties. J. Neurochem. (2006)
    • (2006) J. Neurochem.
    • Groffen, A.J.1    Friedrich, R.2    Brian, E.C.3    Ashery, U.4    Verhage, M.5
  • 95
    • 0032562636 scopus 로고    scopus 로고
    • The C2 domains of Rabphilin3A specifically bind phosphatidylinositol 4,5-bisphosphate containing vesicles in a Ca2+-dependent manner. In vitro characteristics and possible significance
    • Chung S.H., Song W.J., Kim K., Bednarski J.J., Chen J., Prestwich G.D., and Holz R.W. The C2 domains of Rabphilin3A specifically bind phosphatidylinositol 4,5-bisphosphate containing vesicles in a Ca2+-dependent manner. In vitro characteristics and possible significance. J. Biol. Chem. 273 (1998) 10240-10248
    • (1998) J. Biol. Chem. , vol.273 , pp. 10240-10248
    • Chung, S.H.1    Song, W.J.2    Kim, K.3    Bednarski, J.J.4    Chen, J.5    Prestwich, G.D.6    Holz, R.W.7
  • 98
    • 0027960576 scopus 로고
    • Synergistic membrane interactions of the two C2 domains of synaptotagmin
    • Damer C.K., and Creutz C.E. Synergistic membrane interactions of the two C2 domains of synaptotagmin. J. Biol. Chem. 269 (1994) 31115-31123
    • (1994) J. Biol. Chem. , vol.269 , pp. 31115-31123
    • Damer, C.K.1    Creutz, C.E.2
  • 99
    • 0035904238 scopus 로고    scopus 로고
    • The tandem C2 domains of synaptotagmin contain redundant Ca2+ binding sites that cooperate to engage t-SNAREs and trigger exocytosis
    • Earles C.A., Bai J., Wang P., and Chapman E.R. The tandem C2 domains of synaptotagmin contain redundant Ca2+ binding sites that cooperate to engage t-SNAREs and trigger exocytosis. J. Cell Biol. 154 (2001) 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
  • 100
    • 0037022307 scopus 로고    scopus 로고
    • C2A activates a cryptic Ca(2+)-triggered membrane penetration activity within the C2B domain of synaptotagmin I
    • Bai J., Wang P., and Chapman E.R. C2A activates a cryptic Ca(2+)-triggered membrane penetration activity within the C2B domain of synaptotagmin I. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 1665-1670
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 1665-1670
    • Bai, J.1    Wang, P.2    Chapman, E.R.3
  • 101
    • 0346729923 scopus 로고    scopus 로고
    • The calcium binding loops of the cytosolic phospholipase A2 C2 domain specify targeting to Golgi and ER in live cells
    • Evans J.H., Gerber S.H., Murray D., and Leslie C.C. The calcium binding loops of the cytosolic phospholipase A2 C2 domain specify targeting to Golgi and ER in live cells. Mol. Biol. Cell 15 (2004) 371-383
    • (2004) Mol. Biol. Cell , vol.15 , pp. 371-383
    • Evans, J.H.1    Gerber, S.H.2    Murray, D.3    Leslie, C.C.4
  • 102
    • 0035943587 scopus 로고    scopus 로고
    • The top loops of the C(2) domains from synaptotagmin and phospholipase A(2) control functional specificity
    • Gerber S.H., Rizo J., and Sudhof T.C. The top loops of the C(2) domains from synaptotagmin and phospholipase A(2) control functional specificity. J. Biol. Chem. 276 (2001) 32288-32292
    • (2001) J. Biol. Chem. , vol.276 , pp. 32288-32292
    • Gerber, S.H.1    Rizo, J.2    Sudhof, T.C.3
  • 104
    • 0035839572 scopus 로고    scopus 로고
    • Intracellular calcium signals regulating cytosolic phospholipase A2 translocation to internal membranes
    • Evans J.H., Spencer D.M., Zweifach A., and Leslie C.C. Intracellular calcium signals regulating cytosolic phospholipase A2 translocation to internal membranes. J. Biol. Chem. 276 (2001) 30150-30160
    • (2001) J. Biol. Chem. , vol.276 , pp. 30150-30160
    • Evans, J.H.1    Spencer, D.M.2    Zweifach, A.3    Leslie, C.C.4
  • 105
    • 0033538433 scopus 로고    scopus 로고
    • Interplay of C1 and C2 domains of protein kinase C-alpha in its membrane binding and activation
    • Medkova M., and Cho W. Interplay of C1 and C2 domains of protein kinase C-alpha in its membrane binding and activation. J. Biol. Chem. 274 (1999) 19852-19861
    • (1999) J. Biol. Chem. , vol.274 , pp. 19852-19861
    • Medkova, M.1    Cho, W.2
  • 106
    • 0142103304 scopus 로고    scopus 로고
    • Mechanism of group IVA cytosolic phospholipase A2 activation by phosphorylation
    • Das S., Rafter J.D., Kim K.P., Gygi S.P., and Cho W. Mechanism of group IVA cytosolic phospholipase A2 activation by phosphorylation. J. Biol. Chem. 278 (2003) 41431-41442
    • (2003) J. Biol. Chem. , vol.278 , pp. 41431-41442
    • Das, S.1    Rafter, J.D.2    Kim, K.P.3    Gygi, S.P.4    Cho, W.5
  • 107
    • 28244484879 scopus 로고    scopus 로고
    • The C2B domain of rabphilin directly interacts with SNAP-25 and regulates the docking step of dense core vesicle exocytosis in PC12 cells
    • Tsuboi T., and Fukuda M. The C2B domain of rabphilin directly interacts with SNAP-25 and regulates the docking step of dense core vesicle exocytosis in PC12 cells. J. Biol. Chem. 280 (2005) 39253-39259
    • (2005) J. Biol. Chem. , vol.280 , pp. 39253-39259
    • Tsuboi, T.1    Fukuda, M.2
  • 108
    • 0036297772 scopus 로고    scopus 로고
    • Additional binding sites for anionic phospholipids and calcium ions in the crystal structures of complexes of the C2 domain of protein kinase calpha
    • Ochoa W.F., Corbalan-Garcia S., Eritja R., Rodriguez-Alfaro J.A., Gomez-Fernandez J.C., Fita I., and Verdaguer N. Additional binding sites for anionic phospholipids and calcium ions in the crystal structures of complexes of the C2 domain of protein kinase calpha. J. Mol. Biol. 320 (2002) 277-291
    • (2002) J. Mol. Biol. , vol.320 , pp. 277-291
    • Ochoa, W.F.1    Corbalan-Garcia, S.2    Eritja, R.3    Rodriguez-Alfaro, J.A.4    Gomez-Fernandez, J.C.5    Fita, I.6    Verdaguer, N.7
  • 109
    • 4143093730 scopus 로고    scopus 로고
    • Thioredoxin-1 binds to the C2 domain of PTEN inhibiting PTEN's lipid phosphatase activity and membrane binding: a mechanism for the functional loss of PTEN's tumor suppressor activity
    • Meuillet E.J., Mahadevan D., Berggren M., Coon A., and Powis G. Thioredoxin-1 binds to the C2 domain of PTEN inhibiting PTEN's lipid phosphatase activity and membrane binding: a mechanism for the functional loss of PTEN's tumor suppressor activity. Arch. Biochem. Biophys. 429 (2004) 123-133
    • (2004) Arch. Biochem. Biophys. , vol.429 , pp. 123-133
    • Meuillet, E.J.1    Mahadevan, D.2    Berggren, M.3    Coon, A.4    Powis, G.5
  • 110
    • 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. Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains. J. Biol. Chem. 277 (2002) 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
  • 111
    • 0942276361 scopus 로고    scopus 로고
    • Investigations into calcium-dependent membrane association of 15-lipoxygenase-1. Mechanistic roles of surface-exposed hydrophobic amino acids and calcium
    • Walther M., Wiesner R., and Kuhn H. Investigations into calcium-dependent membrane association of 15-lipoxygenase-1. Mechanistic roles of surface-exposed hydrophobic amino acids and calcium. J. Biol. Chem. 279 (2004) 3717-3725
    • (2004) J. Biol. Chem. , vol.279 , pp. 3717-3725
    • Walther, M.1    Wiesner, R.2    Kuhn, H.3
  • 112
    • 0031450155 scopus 로고    scopus 로고
    • The C2 domain of the ubiquitin protein ligase Nedd4 mediates Ca2+-dependent plasma membrane localization
    • Plant P.J., Yeger H., Staub O., Howard P., and Rotin D. The C2 domain of the ubiquitin protein ligase Nedd4 mediates Ca2+-dependent plasma membrane localization. J. Biol. Chem. 272 (1997) 32329-32336
    • (1997) J. Biol. Chem. , vol.272 , pp. 32329-32336
    • Plant, P.J.1    Yeger, H.2    Staub, O.3    Howard, P.4    Rotin, D.5
  • 114
    • 14844321553 scopus 로고    scopus 로고
    • Calcium-dependent plasma membrane binding and cell lysis by perforin are mediated through its C2 domain: a critical role for aspartate residues 429, 435, 483, and 485 but not 491
    • Voskoboinik I., Thia M.C., Fletcher J., Ciccone A., Browne K., Smyth M.J., and Trapani J.A. Calcium-dependent plasma membrane binding and cell lysis by perforin are mediated through its C2 domain: a critical role for aspartate residues 429, 435, 483, and 485 but not 491. J. Biol. Chem. 280 (2005) 8426-8434
    • (2005) J. Biol. Chem. , vol.280 , pp. 8426-8434
    • Voskoboinik, I.1    Thia, M.C.2    Fletcher, J.3    Ciccone, A.4    Browne, K.5    Smyth, M.J.6    Trapani, J.A.7
  • 117
    • 0037167614 scopus 로고    scopus 로고
    • C2 domains of protein kinase C isoforms alpha, beta, and gamma: activation parameters and calcium stoichiometries of the membrane-bound state
    • Kohout S.C., Corbalan-Garcia S., Torrecillas A., Gomez-Fernandez J.C., and Falke J.J. C2 domains of protein kinase C isoforms alpha, beta, and gamma: activation parameters and calcium stoichiometries of the membrane-bound state. Biochemistry 41 (2002) 11411-11424
    • (2002) Biochemistry , vol.41 , pp. 11411-11424
    • Kohout, S.C.1    Corbalan-Garcia, S.2    Torrecillas, A.3    Gomez-Fernandez, J.C.4    Falke, J.J.5
  • 118
    • 20444388673 scopus 로고    scopus 로고
    • The role of EF-hand domains and C2 domain in regulation of enzymatic activity of phospholipase Czeta
    • Kouchi Z., Shikano T., Nakamura Y., Shirakawa H., Fukami K., and Miyazaki S. The role of EF-hand domains and C2 domain in regulation of enzymatic activity of phospholipase Czeta. J. Biol. Chem. 280 (2005) 21015-21021
    • (2005) J. Biol. Chem. , vol.280 , pp. 21015-21021
    • Kouchi, Z.1    Shikano, T.2    Nakamura, Y.3    Shirakawa, H.4    Fukami, K.5    Miyazaki, S.6
  • 119
    • 0034733042 scopus 로고    scopus 로고
    • Distinct Ca2+ binding properties of novel C2 domains of plant phospholipase dalpha and beta
    • Zheng L., Krishnamoorthi R., Zolkiewski M., and Wang X. Distinct Ca2+ binding properties of novel C2 domains of plant phospholipase dalpha and beta. J. Biol. Chem. 275 (2000) 19700-19706
    • (2000) J. Biol. Chem. , vol.275 , pp. 19700-19706
    • Zheng, L.1    Krishnamoorthi, R.2    Zolkiewski, M.3    Wang, X.4
  • 120
    • 1342346595 scopus 로고    scopus 로고
    • Reconstitution of phosphatidylserine transport from chemically defined donor membranes to phosphatidylserine decarboxylase 2 implicates specific lipid domains in the process
    • Wu W.I., and Voelker D.R. Reconstitution of phosphatidylserine transport from chemically defined donor membranes to phosphatidylserine decarboxylase 2 implicates specific lipid domains in the process. J. Biol. Chem. 279 (2004) 6635-6642
    • (2004) J. Biol. Chem. , vol.279 , pp. 6635-6642
    • Wu, W.I.1    Voelker, D.R.2
  • 121
    • 5444221254 scopus 로고    scopus 로고
    • The C2 domains of the class I Rab11 family of interacting proteins target recycling vesicles to the plasma membrane
    • Lindsay A.J., and McCaffrey M.W. The C2 domains of the class I Rab11 family of interacting proteins target recycling vesicles to the plasma membrane. J. Cell Sci. 117 (2004) 4365-4375
    • (2004) J. Cell Sci. , vol.117 , pp. 4365-4375
    • Lindsay, A.J.1    McCaffrey, M.W.2
  • 122
    • 0029872616 scopus 로고    scopus 로고
    • Phospholipid composition dependence of Ca2+-dependent phospholipid binding to the C2A domain of synaptotagmin IV
    • Fukuda M., Kojima T., and Mikoshiba K. Phospholipid composition dependence of Ca2+-dependent phospholipid binding to the C2A domain of synaptotagmin IV. J. Biol. Chem. 271 (1996) 8430-8434
    • (1996) J. Biol. Chem. , vol.271 , pp. 8430-8434
    • Fukuda, M.1    Kojima, T.2    Mikoshiba, K.3
  • 123
    • 1942520207 scopus 로고    scopus 로고
    • Reconstitution of Ca2+-regulated membrane fusion by synaptotagmin and SNAREs
    • Tucker W.C., Weber T., and Chapman E.R. Reconstitution of Ca2+-regulated membrane fusion by synaptotagmin and SNAREs. Science 304 (2004) 435-438
    • (2004) Science , vol.304 , pp. 435-438
    • Tucker, W.C.1    Weber, T.2    Chapman, E.R.3
  • 124
    • 2342503800 scopus 로고    scopus 로고
    • Characterization of Tollip protein upon Lipopolysaccharide challenge
    • Li T., Hu J., and Li L. Characterization of Tollip protein upon Lipopolysaccharide challenge. Mol. Immunol. 41 (2004) 85-92
    • (2004) Mol. Immunol. , vol.41 , pp. 85-92
    • Li, T.1    Hu, J.2    Li, L.3
  • 125
    • 0035816711 scopus 로고    scopus 로고
    • The C2A domain of double C2 protein gamma contains a functional nuclear localization signal
    • Fukuda M., Saegusa C., Kanno E., and Mikoshiba K. The C2A domain of double C2 protein gamma contains a functional nuclear localization signal. J. Biol. Chem. 276 (2001) 24441-24444
    • (2001) J. Biol. Chem. , vol.276 , pp. 24441-24444
    • Fukuda, M.1    Saegusa, C.2    Kanno, E.3    Mikoshiba, K.4
  • 127
    • 0033529292 scopus 로고    scopus 로고
    • Selective interaction of the C2 domains of phospholipase C-beta1 and-beta2 with activated Galphaq subunits: an alternative function for C2-signaling modules
    • Wang T., Pentyala S., Elliott J.T., Dowal L., Gupta E., Rebecchi M.J., and Scarlata S. Selective interaction of the C2 domains of phospholipase C-beta1 and-beta2 with activated Galphaq subunits: an alternative function for C2-signaling modules. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 7843-7846
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 7843-7846
    • Wang, T.1    Pentyala, S.2    Elliott, J.T.3    Dowal, L.4    Gupta, E.5    Rebecchi, M.J.6    Scarlata, S.7
  • 128
    • 28244498726 scopus 로고    scopus 로고
    • Phospholipase Cdelta4 associates with glutamate receptor interacting protein 1 in testis
    • Irino Y., Ichinohe M., Nakamura Y., Nakahara M., and Fukami K. Phospholipase Cdelta4 associates with glutamate receptor interacting protein 1 in testis. J. Biochem. (Tokyo) 138 (2005) 451-456
    • (2005) J. Biochem. (Tokyo) , vol.138 , pp. 451-456
    • Irino, Y.1    Ichinohe, M.2    Nakamura, Y.3    Nakahara, M.4    Fukami, K.5
  • 129
    • 0035396862 scopus 로고    scopus 로고
    • Protein kinase C-delta C2-like domain is a binding site for actin and enables actin redistribution in neutrophils
    • Lopez-Lluch G., Bird M.M., Canas B., Godovac-Zimmerman J., Ridley A., Segal A.W., and Dekker L.V. Protein kinase C-delta C2-like domain is a binding site for actin and enables actin redistribution in neutrophils. Biochem. J. 357 (2001) 39-47
    • (2001) Biochem. J. , vol.357 , pp. 39-47
    • Lopez-Lluch, G.1    Bird, M.M.2    Canas, B.3    Godovac-Zimmerman, J.4    Ridley, A.5    Segal, A.W.6    Dekker, L.V.7
  • 130
    • 16844370879 scopus 로고    scopus 로고
    • Involvement of NH2 terminus of PKC-delta in binding to F-actin during activation of Calu-3 airway epithelial NKCC1
    • Smallwood N.D., Hausman B.S., Wang X., and Liedtke C.M. Involvement of NH2 terminus of PKC-delta in binding to F-actin during activation of Calu-3 airway epithelial NKCC1. Am. J. Physiol.: Cell Physiol. 288 (2005) C906-C912
    • (2005) Am. J. Physiol.: Cell Physiol. , vol.288
    • Smallwood, N.D.1    Hausman, B.S.2    Wang, X.3    Liedtke, C.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.