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Volumn 5, Issue 12, 1996, Pages 2375-2390

The C2 domain calcium-binding motif: Structural and functional diversity

Author keywords

C2 domain; calcium signaling; calcium dependent phospholipid binding domain; cytosolic phospholipase A2; phospholipase C; protein kinase C; ras GTPase activating protein; synaptotagmin

Indexed keywords

CALCIUM BINDING PROTEIN;

EID: 0030467967     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560051201     Document Type: Review
Times cited : (716)

References (139)
  • 1
    • 0028950269 scopus 로고
    • The biochemistry of neurotransmitter secretion
    • Bajjalieh SM, Scheller RH. 1995. The biochemistry of neurotransmitter secretion. J Biol Chem 270:1971-1974.
    • (1995) J Biol Chem , vol.270 , pp. 1971-1974
    • Bajjalieh, S.M.1    Scheller, R.H.2
  • 2
    • 0023109718 scopus 로고
    • Association of protein kinase C with phospholipid vesicles
    • Bazzi MD, Nelsestuen GL 1987. Association of protein kinase C with phospholipid vesicles. Biochemistry 26:115-122.
    • (1987) Biochemistry , vol.26 , pp. 115-122
    • Bazzi, M.D.1    Nelsestuen, G.L.2
  • 3
    • 0025170867 scopus 로고
    • Protein kinase C interaction with calcium: A phospholipid-dependent process
    • Bazzi MD, Nelsestuen GL. 1990. Protein kinase C interaction with calcium: A phospholipid-dependent process. Biochemistry 29:7624-7630.
    • (1990) Biochemistry , vol.29 , pp. 7624-7630
    • Bazzi, M.D.1    Nelsestuen, G.L.2
  • 4
    • 0026778460 scopus 로고
    • Syntaxin: A synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • Bennett MK, Calakos N, Scheller RH 1992. Syntaxin: A synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science 257:255-259.
    • (1992) Science , vol.257 , pp. 255-259
    • Bennett, M.K.1    Calakos, N.2    Scheller, R.H.3
  • 5
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • Berridge MJ. 1993. Inositol trisphosphate and calcium signalling. Nature 361:315-325.
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 6
    • 0024453294 scopus 로고
    • Inositol phosphates and cell signalling
    • Berridge MJ, Irvine RF. 1989. Inositol phosphates and cell signalling. Nature 341:197-205
    • (1989) Nature , vol.341 , pp. 197-205
    • Berridge, M.J.1    Irvine, R.F.2
  • 7
    • 0026822891 scopus 로고
    • Analysis of conserved domains and sequence motifs in cellular regulatory proteins and locus control regions using new software tools for multiple alignment and visualization
    • Boguski MS, Hardinson RC, Schwartz S, Miller W. 1992 Analysis of conserved domains and sequence motifs in cellular regulatory proteins and locus control regions using new software tools for multiple alignment and visualization. New Biol 4:247-260.
    • (1992) New Biol , vol.4 , pp. 247-260
    • Boguski, M.S.1    Hardinson, R.C.2    Schwartz, S.3    Miller, W.4
  • 8
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • Boguski MS, McCormick F. 1993. Proteins regulating Ras and its relatives. Nature 366:643-654.
    • (1993) Nature , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 9
    • 0027988814 scopus 로고    scopus 로고
    • The WW domain: A signalling site in dystrophin?
    • Bork P, Sudol M. 1996. The WW domain: A signalling site in dystrophin? Trends Biochem Sci 19:531-533.
    • (1996) Trends Biochem Sci , vol.19 , pp. 531-533
    • Bork, P.1    Sudol, M.2
  • 10
    • 0027964479 scopus 로고
    • Localization of 5-lipoxygenase to the nucleus of unstimulated rat basophilic leukemia cells
    • Brock TG, Paine R III, Peters-Golden M 1994. Localization of 5-lipoxygenase to the nucleus of unstimulated rat basophilic leukemia cells. J Biol Chem 269:22059-22066.
    • (1994) J Biol Chem , vol.269 , pp. 22059-22066
    • Brock, T.G.1    Paine III, R.2    Peters-Golden, M.3
  • 12
    • 0026631563 scopus 로고
    • Synaptotagmin: A calcium sensor on the synaptic vesicle surface
    • Brose N, Petrenko AG, Südhof TC, Jahn R. 1992. Synaptotagmin: A calcium sensor on the synaptic vesicle surface. Science 256:1021-1025.
    • (1992) Science , vol.256 , pp. 1021-1025
    • Brose, N.1    Petrenko, A.G.2    Südhof, T.C.3    Jahn, R.4
  • 13
    • 0026676806 scopus 로고
    • Isozyme-selective stimulation of phospholipase C-β2 by G protein βγ-subunits
    • Camps M, Carozzi A, Schnabel P, Scheer A, Parker PJ, Gierschik P. 1992. Isozyme-selective stimulation of phospholipase C-β2 by G protein βγ-subunits. Nature 360:684-686.
    • (1992) Nature , vol.360 , pp. 684-686
    • Camps, M.1    Carozzi, A.2    Schnabel, P.3    Scheer, A.4    Parker, P.J.5    Gierschik, P.6
  • 16
    • 0028970788 scopus 로고
    • 2- regulates the interaction between synaptotagmin and syntaxin I
    • 2- regulates the interaction between synaptotagmin and syntaxin I. J Biol Chem 270:23667-23671.
    • (1995) J Biol Chem , vol.270 , pp. 23667-23671
    • Chapman, E.R.1    Hanson, P.I.2    An, S.3    Jahn, R.4
  • 18
    • 0029146286 scopus 로고
    • Releasing the calcium trigger
    • Chazin WJ. 1995. Releasing the calcium trigger. Nat Struct Biol 2:707-710.
    • (1995) Nat Struct Biol , vol.2 , pp. 707-710
    • Chazin, W.J.1
  • 19
    • 0029077932 scopus 로고
    • Evidence that the Rab3a-binding protein, rabphilin3a, enhances regulated secretion
    • Chung S-H, Takai Y, Holz RW. 1995. Evidence that the Rab3a-binding protein, rabphilin3a, enhances regulated secretion. J Biol Chem 270:16714-16718.
    • (1995) J Biol Chem , vol.270 , pp. 16714-16718
    • Chung, S.-H.1    Takai, Y.2    Holz, R.W.3
  • 25
    • 0025951251 scopus 로고
    • Implicating the bcr/abl gene in the pathogenesis of Philadelphia chromosome-positive human leukemia
    • Daley GQ, Ben-Neriah Y. 1991. Implicating the bcr/abl gene in the pathogenesis of Philadelphia chromosome-positive human leukemia. Adv Cancer Res 57: 151-184.
    • (1991) Adv Cancer Res , vol.57 , pp. 151-184
    • Daley, G.Q.1    Ben-Neriah, Y.2
  • 26
    • 0027960576 scopus 로고
    • Synergistic membrane interactions of the two C2 domains of synaptotagmin
    • Damer CK, Creutz CE. 1994. Synergistic membrane interactions of the two C2 domains of synaptotagmin. J Biol Chem 269:31115-31123.
    • (1994) J Biol Chem , vol.269 , pp. 31115-31123
    • Damer, C.K.1    Creutz, C.E.2
  • 28
    • 0028172171 scopus 로고
    • 2+-dependent conformational change in synaptotagmin I
    • 2+-dependent conformational change in synaptotagmin I. J Biol Chem 269:28547-28550.
    • (1994) J Biol Chem , vol.269 , pp. 28547-28550
    • Davletov, B.A.1    Südhof, T.C.2
  • 29
    • 0028082161 scopus 로고
    • Protein kinase C - A question of specificity
    • Dekker LV, Parker PJ. 1994. Protein kinase C - A question of specificity. Trends Biochem Sci 19:73-77.
    • (1994) Trends Biochem Sci , vol.19 , pp. 73-77
    • Dekker, L.V.1    Parker, P.J.2
  • 30
    • 0027180569 scopus 로고
    • Synaptic transmission persists in synaptotagmin mutants of Drosophila
    • DiAntonio A, Parfitt KD, Schwarz TL. 1993. Synaptic transmission persists in synaptotagmin mutants of Drosophila. Cell 73:1281-1290.
    • (1993) Cell , vol.73 , pp. 1281-1290
    • Diantonio, A.1    Parfitt, K.D.2    Schwarz, T.L.3
  • 32
    • 0026764896 scopus 로고
    • SPT3 interacts with TFIID to allow normal transcription in Saccharomyces cerevisiae
    • Eisenmann DM, Arndt KM, Ricupero SL, Rooney JW, Winston F. 1992. SPT3 interacts with TFIID to allow normal transcription in Saccharomyces cerevisiae. Genes Dev 6:1319-1331.
    • (1992) Genes Dev , vol.6 , pp. 1319-1331
    • Eisenmann, D.M.1    Arndt, K.M.2    Ricupero, S.L.3    Rooney, J.W.4    Winston, F.5
  • 34
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ
    • Essen L-O, Perisic O, Katan M, Williams RL. 1996. Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ. Nature 380:595-602.
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.-O.1    Perisic, O.2    Katan, M.3    Williams, R.L.4
  • 35
    • 0027945446 scopus 로고
    • Molecular tuning of ion binding to calcium signaling proteins
    • Falke JJ, Drake SK, Hazard AL, Peersen OB 1994. Molecular tuning of ion binding to calcium signaling proteins. Q Rev Biophys 27:219-290.
    • (1994) Q Rev Biophys , vol.27 , pp. 219-290
    • Falke, J.J.1    Drake, S.K.2    Hazard, A.L.3    Peersen, O.B.4
  • 36
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    • Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB. 1995. Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell 83:1037-1046.
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 37
    • 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, Mikoshiba K. 1994. Inositol-1,3,4.5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II. J Biol Chem 269:29206-29211.
    • (1994) J Biol Chem , vol.269 , pp. 29206-29211
    • Fukuda, M.1    Aruga, J.2    Niinobe, M.3    Aimoto, S.4    Mikoshiba, K.5
  • 38
  • 39
    • 0028221291 scopus 로고
    • + channels
    • + channels. FASEB J 8:522-528.
    • (1994) FASEB J , vol.8 , pp. 522-528
    • Garty, H.1
  • 40
    • 0026588783 scopus 로고
    • A putative Ras GTPase activating protein acts as a negative regulator of signaling by the sevenless receptor tyrosine kinase
    • Gaul U, Mardon G, Rubin GM. 1992. A putative Ras GTPase activating protein acts as a negative regulator of signaling by the sevenless receptor tyrosine kinase. Cell 68:1007-1019
    • (1992) Cell , vol.68 , pp. 1007-1019
    • Gaul, U.1    Mardon, G.2    Rubin, G.M.3
  • 41
    • 0028987698 scopus 로고
    • 2+-dependent phospholipid binding (CaLB) domain within p120 GAP, a GTPase-activating protein for p21 ras
    • 2+-dependent phospholipid binding (CaLB) domain within p120 GAP, a GTPase-activating protein for p21 ras. Biochem J 307:487-491.
    • (1995) Biochem J , vol.307 , pp. 487-491
    • Gawler, D.J.1    Zhang, L.-J.2    Moran, M.F.3
  • 42
    • 0028901758 scopus 로고
    • CaLB: A 43 amino acid calcium-dependent membrane/phospholipid binding domain in p120 Ras GTPase-activating protein
    • Gawler DJ, Zhang L-J, Reedijk M, Tung PS, Moran MF. 1995b CaLB: A 43 amino acid calcium-dependent membrane/phospholipid binding domain in p120 Ras GTPase-activating protein. Oncogens 10:817-825.
    • (1995) Oncogens , vol.10 , pp. 817-825
    • Gawler, D.J.1    Zhang, L.-J.2    Reedijk, M.3    Tung, P.S.4    Moran, M.F.5
  • 45
    • 0026753013 scopus 로고
    • 2 from rat kidney: Divalent metaldependent trapping of enzyme on product-containing vesicles
    • 2 from rat kidney: Divalent metaldependent trapping of enzyme on product-containing vesicles. Biochemistry 31:3814-3824.
    • (1992) Biochemistry , vol.31 , pp. 3814-3824
    • Ghomashchi, F.1    Schuttel, S.2    Jain, M.K.3    Gelb, M.H.4
  • 46
    • 0029020361 scopus 로고
    • 2 from cytosol to nuclear envelope in rat basophilic leukemia cells stimulated with calcium ionophore or IgE/antigen
    • 2 from cytosol to nuclear envelope in rat basophilic leukemia cells stimulated with calcium ionophore or IgE/antigen J Biol Chem 270:15359-15367.
    • (1995) J Biol Chem , vol.270 , pp. 15359-15367
    • Glover, S.1    Bayburt, T.2    Jonas, M.3    Chi, E.4    Gelb, M.H.5
  • 48
    • 0029564902 scopus 로고
    • Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family
    • Hammond SM, Altshuller YM, Sung T-C, Rudge SA, Rose K, Engebrecht J, Morris AJ, Frohman MA. 1995. Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family. J Biol Chem 270:29640-29643.
    • (1995) J Biol Chem , vol.270 , pp. 29640-29643
    • Hammond, S.M.1    Altshuller, Y.M.2    Sung, T.-C.3    Rudge, S.A.4    Rose, K.5    Engebrecht, J.6    Morris, A.J.7    Frohman, M.A.8
  • 49
    • 0021811764 scopus 로고
    • Structural organization of the bcr gene and its role in the Ph′ translocation
    • Heisterkamp N, Stam K, Groffen J, de Klein A, Grosveld G. 1985. Structural organization of the bcr gene and its role in the Ph′ translocation. Nature 315:758-761.
    • (1985) Nature , vol.315 , pp. 758-761
    • Heisterkamp, N.1    Stam, K.2    Groffen, J.3    De Klein, A.4    Grosveld, G.5
  • 50
    • 0025200830 scopus 로고
    • Characterization of VPS34, a gene required for vacuolar protein sorting and vacuole segregation in Saccharomyces cerevisiae
    • Herman PK, Emr SD. 1990. Characterization of VPS34, a gene required for vacuolar protein sorting and vacuole segregation in Saccharomyces cerevisiae. Mol Cell Biol 10:6742-6754.
    • (1990) Mol Cell Biol , vol.10 , pp. 6742-6754
    • Herman, P.K.1    Emr, S.D.2
  • 52
    • 0028831959 scopus 로고
    • The rsp5-domain is shared by proteins of diverse functions
    • Hofmann K, Bucher P. 1995. The rsp5-domain is shared by proteins of diverse functions. FEBS Lett 358:153-157.
    • (1995) FEBS Lett , vol.358 , pp. 153-157
    • Hofmann, K.1    Bucher, P.2
  • 53
    • 0027361002 scopus 로고
    • Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85
    • Hu P, Skolnik EY, Schlessinger J. 1993. Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85. Mol Cell Biol 13:7677-7688.
    • (1993) Mol Cell Biol , vol.13 , pp. 7677-7688
    • Hu, P.1    Skolnik, E.Y.2    Schlessinger, J.3
  • 54
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protease ligase
    • Huibregste JM, Scheffner M, Beaudenon S, Howley PM. 1995. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protease ligase. Proc Natl Acad Sci USA 92:2563-2567.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2563-2567
    • Huibregste, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 55
    • 0028865692 scopus 로고
    • A novel phosphatidylserine-binding peptide motif defined by an anti-idiotypic monoclonal antibody
    • Igarashi K, Kaneda M, Yamaji A, Saido TC, Kikkawa U, Ono Y, Inoue K, Umeda M. 1995 A novel phosphatidylserine-binding peptide motif defined by an anti-idiotypic monoclonal antibody. J Biol Chem 270:29075-29078.
    • (1995) J Biol Chem , vol.270 , pp. 29075-29078
    • Igarashi, K.1    Kaneda, M.2    Yamaji, A.3    Saido, T.C.4    Kikkawa, U.5    Ono, Y.6    Inoue, K.7    Umeda, M.8
  • 56
    • 0030032040 scopus 로고    scopus 로고
    • Calcium-binding and conformational response in EF-hand proteins
    • Ikura M. 1996. Calcium-binding and conformational response in EF-hand proteins. Trends Biochem Sci 21:14-17.
    • (1996) Trends Biochem Sci , vol.21 , pp. 14-17
    • Ikura, M.1
  • 57
    • 0028216869 scopus 로고
    • Synaptic vesicles and exocytosis
    • Jahn R, Südhof TC. 1994. Synaptic vesicles and exocytosis Annu Rev Neurosci 17:219-246.
    • (1994) Annu Rev Neurosci , vol.17 , pp. 219-246
    • Jahn, R.1    Südhof, T.C.2
  • 59
    • 0029189946 scopus 로고    scopus 로고
    • Calcium-binding proteins. 1. EF-hands
    • Kawasaki K, Kretsinger RH. 1996. Calcium-binding proteins. 1. EF-hands. Protein Profile 2:305-490.
    • (1996) Protein Profile , vol.2 , pp. 305-490
    • Kawasaki, K.1    Kretsinger, R.H.2
  • 60
    • 0029917101 scopus 로고    scopus 로고
    • Localization of synaptotagmin-binding domains on syntaxin
    • Kee Y, Scheller RH 1996 Localization of synaptotagmin-binding domains on syntaxin J Neurosci 16:1975-1981.
    • (1996) J Neurosci , vol.16 , pp. 1975-1981
    • Kee, Y.1    Scheller, R.H.2
  • 61
    • 0029257397 scopus 로고
    • Synaptotagmin is just a calcium sensor
    • Kelly RB. 1995. Synaptotagmin is just a calcium sensor. Curr Biol 5:257-259.
    • (1995) Curr Biol , vol.5 , pp. 257-259
    • Kelly, R.B.1
  • 64
    • 0026763128 scopus 로고
    • Identification of a set of genes with developmentally down-regulated expression in the mouse brain
    • Kumar S, Tomooka Y, Noda M. 1992. Identification of a set of genes with developmentally down-regulated expression in the mouse brain. Biochem Biophys Res Commun 185:1155-1161.
    • (1992) Biochem Biophys Res Commun , vol.185 , pp. 1155-1161
    • Kumar, S.1    Tomooka, Y.2    Noda, M.3
  • 65
    • 0001275961 scopus 로고    scopus 로고
    • Molecular cloning, splice variants, expression, and purification of phospholipase C-δ4
    • Lee SB, Rhee SG. 1996. Molecular cloning, splice variants, expression, and purification of phospholipase C-δ4 J Biol Chem 271:25-31.
    • (1996) J Biol Chem , vol.271 , pp. 25-31
    • Lee, S.B.1    Rhee, S.G.2
  • 66
    • 0029939448 scopus 로고    scopus 로고
    • PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface
    • Lemmon, MA, Ferguson KM, Schlessinger J. 1996. PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface. Cell 85:621-624.
    • (1996) Cell , vol.85 , pp. 621-624
    • Lemmon, M.A.1    Ferguson, K.M.2    Schlessinger, J.3
  • 67
    • 0025300349 scopus 로고
    • A candidate protein kinase C gene. PKC1, is required for the S cerevisiae cell cycle
    • Levin DE, Fields FO, Kunisawa R, Bishop JM, Thorner J. 1990. A candidate protein kinase C gene. PKC1, is required for the S cerevisiae cell cycle. Cell 62:213-224.
    • (1990) Cell , vol.62 , pp. 213-224
    • Levin, D.E.1    Fields, F.O.2    Kunisawa, R.3    Bishop, J.M.4    Thorner, J.5
  • 74
    • 0029612196 scopus 로고
    • A family of phosphoinositide 3-kinases in Drosophila identifies a new mediator of signal transduction
    • MacDougall LK, Domin J, Waterfield MD. 1995. A family of phosphoinositide 3-kinases in Drosophila identifies a new mediator of signal transduction. Curr Biol 5:1410-1415.
    • (1995) Curr Biol , vol.5 , pp. 1410-1415
    • MacDougall, L.K.1    Domin, J.2    Waterfield, M.D.3
  • 76
    • 0026053020 scopus 로고
    • A phorbol ester/diacylglycerol-binding protein encoded by the unc-13 gene of Caenorhabditis elegans
    • Maruyama IN, Brenner S. 1991. A phorbol ester/diacylglycerol-binding protein encoded by the unc-13 gene of Caenorhabditis elegans Proc Natl Acad Sci USA 85:5729-5733.
    • (1991) Proc Natl Acad Sci USA , vol.85 , pp. 5729-5733
    • Maruyama, I.N.1    Brenner, S.2
  • 77
    • 0026032349 scopus 로고
    • A second gene product of the inositol-phospholipid-specific phospholipase Cδ subclass
    • Meldrum E, Kriz RW, Totty N, Parker PJ. 1991. A second gene product of the inositol-phospholipid-specific phospholipase Cδ subclass. Eur J Biochem 196:159-165.
    • (1991) Eur J Biochem , vol.196 , pp. 159-165
    • Meldrum, E.1    Kriz, R.W.2    Totty, N.3    Parker, P.J.4
  • 78
    • 0028938152 scopus 로고
    • Localization of protein kinases by anchoring proteins: A theme in signal transduction
    • Mochly-Rosen D. 1995. Localization of protein kinases by anchoring proteins: A theme in signal transduction. Science 268:247-251.
    • (1995) Science , vol.268 , pp. 247-251
    • Mochly-Rosen, D.1
  • 79
    • 0026733246 scopus 로고
    • p65 fragments, homologous to the C2 region of protein kinase C, bind to the intracellular receptors for protein kinase C
    • Mochly-Rosen D, Miller KG, Scheller RH, Khaner H, Lopez J, Smith BL. 1992. p65 fragments, homologous to the C2 region of protein kinase C, bind to the intracellular receptors for protein kinase C. Biochemistry 31:8120-8124.
    • (1992) Biochemistry , vol.31 , pp. 8120-8124
    • Mochly-Rosen, D.1    Miller, K.G.2    Scheller, R.H.3    Khaner, H.4    Lopez, J.5    Smith, B.L.6
  • 80
    • 0028260527 scopus 로고
    • A novel protein kinase with leucine zipper-like sequences: Its catalytic domain is highly homologous to that of protein kinase C
    • Mukai H, Ono Y. 1994. A novel protein kinase with leucine zipper-like sequences: Its catalytic domain is highly homologous to that of protein kinase C. Biochem Biophys Res Commun 199:897-904.
    • (1994) Biochem Biophys Res Commun , vol.199 , pp. 897-904
    • Mukai, H.1    Ono, Y.2
  • 82
    • 0029364428 scopus 로고
    • Seeing two domains
    • Newton AC. 1995a. Seeing two domains. Curr Biol 5:973-976.
    • (1995) Curr Biol , vol.5 , pp. 973-976
    • Newton, A.C.1
  • 83
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function, and regulation
    • Newton AC. 1995b. Protein kinase C: Structure, function, and regulation. J Biol Chem 270:28495-28498.
    • (1995) J Biol Chem , vol.270 , pp. 28495-28498
    • Newton, A.C.1
  • 84
    • 0028643566 scopus 로고
    • Synaptotagmin is an inositol polyphosphate binding protein: Isolation and characterization as an Ins1,3,4,5-P4 binding protein
    • Niinobe M, Yamaguchi Y, Fukuda M, Mikoshiba K. 1994. Synaptotagmin is an inositol polyphosphate binding protein: Isolation and characterization as an Ins1,3,4,5-P4 binding protein. Biochem Biophys Res Commun 205:1036-1042
    • (1994) Biochem Biophys Res Commun , vol.205 , pp. 1036-1042
    • Niinobe, M.1    Yamaguchi, Y.2    Fukuda, M.3    Mikoshiba, K.4
  • 85
    • 0023764824 scopus 로고
    • The molecular heterogeneity of protein kinase C and its implications for cellular regulation
    • Nishizuka Y. 1988. The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature 334:661-665.
    • (1988) Nature , vol.334 , pp. 661-665
    • Nishizuka, Y.1
  • 86
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka Y. 1992. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C Science 258:607-614.
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 87
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signalling for sustained cellular responses
    • Nishizuka Y. 1995. Protein kinase C and lipid signalling for sustained cellular responses. FASEB J 9:484-496.
    • (1995) FASEB J , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 88
    • 0028829555 scopus 로고
    • A downstream target of RHO1 small GTP-binding protein is PKC1, a homolog of protein kinase C, which leads to activation of the MAP kinase cascade in Saccharomyces cerevisiae
    • Nonaka H, Tanaka K, Hirano H, Fujiwara T, Kohno H, Umikawa M, Mino A, Takai Y. 1995. A downstream target of RHO1 small GTP-binding protein is PKC1, a homolog of protein kinase C, which leads to activation of the MAP kinase cascade in Saccharomyces cerevisiae. EMBO J 14:5931-5938
    • (1995) EMBO J , vol.14 , pp. 5931-5938
    • Nonaka, H.1    Tanaka, K.2    Hirano, H.3    Fujiwara, T.4    Kohno, H.5    Umikawa, M.6    Mino, A.7    Takai, Y.8
  • 89
    • 0027319325 scopus 로고
    • Synaptic function is impaired but not eliminated in C. elegans mutants lacking synaptotagmin
    • Nonet ML, Grundahl K, Meyer BJ, Rand JB. 1993. Synaptic function is impaired but not eliminated in C. elegans mutants lacking synaptotagmin. Cell 73:1291-1305.
    • (1993) Cell , vol.73 , pp. 1291-1305
    • Nonet, M.L.1    Grundahl, K.2    Meyer, B.J.3    Rand, J.B.4
  • 93
    • 0029078831 scopus 로고
    • Expression, purification and characterization of the ubiquitous protein kinase C-related kinase 1
    • Palmer RH, Parker PJ. 1995. Expression, purification and characterization of the ubiquitous protein kinase C-related kinase 1. Biochem J 309:315-320.
    • (1995) Biochem J , vol.309 , pp. 315-320
    • Palmer, R.H.1    Parker, P.J.2
  • 94
    • 0028815490 scopus 로고
    • Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family
    • Palmer RH, Ridden J, Parker PJ. 1995. Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family. Eur J Biochem 227:344-351.
    • (1995) Eur J Biochem , vol.227 , pp. 344-351
    • Palmer, R.H.1    Ridden, J.2    Parker, P.J.3
  • 97
    • 0029320454 scopus 로고
    • PI 3-kinase puts GTP on the Rac
    • Parker PJ, 1995. PI 3-kinase puts GTP on the Rac. Curr Biol 5:577-579.
    • (1995) Curr Biol , vol.5 , pp. 577-579
    • Parker, P.J.1
  • 98
    • 0026484261 scopus 로고
    • SH2 and SH3 domains: From structure to function
    • Pawson T, Gish GD, 1992. SH2 and SH3 domains: From structure to function. Cell 71:359-362.
    • (1992) Cell , vol.71 , pp. 359-362
    • Pawson, T.1    Gish, G.D.2
  • 99
    • 0025270739 scopus 로고
    • Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C
    • Perin MS, Fried VA, Mignery GA, Jahn R, Südhof TC. 1990. Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C. Nature 345:260-263.
    • (1990) Nature , vol.345 , pp. 260-263
    • Perin, M.S.1    Fried, V.A.2    Mignery, G.A.3    Jahn, R.4    Südhof, T.C.5
  • 101
    • 0030034251 scopus 로고    scopus 로고
    • Extending the C2 domain family: C2s in PKCs δ, ∈, η, θ, phospholipases, GAPs, and perforin
    • Ponting CP, Parker PJ 1996. Extending the C2 domain family: C2s in PKCs δ, ∈, η, θ, phospholipases, GAPs, and perforin. Prorein Sci 5:162-166.
    • (1996) Prorein Sci , vol.5 , pp. 162-166
    • Ponting, C.P.1    Parker, P.J.2
  • 102
    • 0027200551 scopus 로고
    • Subcellular localization of prostaglandin endoperoxide synthase-2 in murine 3T3 cells
    • Regier MK, DeWitt DL, Schindler MS, Smith WL. 1993. Subcellular localization of prostaglandin endoperoxide synthase-2 in murine 3T3 cells. Arch Biochem Biophys 301:439-444.
    • (1993) Arch Biochem Biophys , vol.301 , pp. 439-444
    • Regier, M.K.1    Dewitt, D.L.2    Schindler, M.S.3    Smith, W.L.4
  • 103
    • 0026654469 scopus 로고
    • Regulation of inositol phospholipid-specific phospholipase C isozymes
    • Rhee SG, Choi KD. 1992. Regulation of inositol phospholipid-specific phospholipase C isozymes. J Biol Chem 267:12393-12396
    • (1992) J Biol Chem , vol.267 , pp. 12393-12396
    • Rhee, S.G.1    Choi, K.D.2
  • 104
    • 0024403320 scopus 로고
    • Studies of inositol phospholipid-specific phospholipase C
    • Rhee SG, Suh P-G, Ryu S-H, Lee SY. 1989 Studies of inositol phospholipid-specific phospholipase C. Science 244:546-550.
    • (1989) Science , vol.244 , pp. 546-550
    • Rhee, S.G.1    Suh, P.-G.2    Ryu, S.-H.3    Lee, S.Y.4
  • 105
    • 0028801624 scopus 로고
    • An autoregulatory region in protein kinase C: The pseudoanchoring site
    • Ron D, Mochly-Rosen D. 1995. An autoregulatory region in protein kinase C: The pseudoanchoring site. Proc Natl Acad Sci USA 92:492-496.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 492-496
    • Ron, D.1    Mochly-Rosen, D.2
  • 107
    • 0027504763 scopus 로고
    • 2: Identification of regions required for membrane association and stimulation by guanine-nucleotide-binding protein βγ subunits
    • 2: Identification of regions required for membrane association and stimulation by guanine-nucleotide-binding protein βγ subunits. Eur J Biochem 217:1109-1115.
    • (1993) Eur J Biochem , vol.217 , pp. 1109-1115
    • Schnabel, P.1    Camps, M.2    Carozzi, A.3    Parker, P.J.4    Gierschik, P.5
  • 110
  • 111
    • 0028594078 scopus 로고
    • Rabphilin-3A is associated with synaptic vesicles through a vesicle protein in a manner independent of Rab3A
    • Shirataki H, Yamamoto T, Hagi S, Miura H, Oishi H, Jin-no Y, Senbonmatsu T, Takai Y. 1994. Rabphilin-3A is associated with synaptic vesicles through a vesicle protein in a manner independent of Rab3A J Biol Chem 269:32717-32720
    • (1994) J Biol Chem , vol.269 , pp. 32717-32720
    • Shirataki, H.1    Yamamoto, T.2    Hagi, S.3    Miura, H.4    Oishi, H.5    Jin-no, Y.6    Senbonmatsu, T.7    Takai, Y.8
  • 112
    • 0027276016 scopus 로고
    • 2+-independent protein kinase Cs contain an amino-terminal domain similar to the C2 consensus sequence
    • 2+-independent protein kinase Cs contain an amino-terminal domain similar to the C2 consensus sequence. Trends Biochem Sci 18:207-208.
    • (1993) Trends Biochem Sci , vol.18 , pp. 207-208
    • Sossin, W.S.1    Schwartz, J.H.2
  • 113
    • 0029935431 scopus 로고    scopus 로고
    • Rab3 reversibly recruits rabphilin to synaptic vesicles by a mechanism analogous to raf recruitment by ras
    • Stahl B, Chou JH, Li C, Südhof TC, Jahn R. 1996. Rab3 reversibly recruits rabphilin to synaptic vesicles by a mechanism analogous to raf recruitment by ras. EMBO J 15:1799-1809.
    • (1996) EMBO J , vol.15 , pp. 1799-1809
    • Stahl, B.1    Chou, J.H.2    Li, C.3    Südhof, T.C.4    Jahn, R.5
  • 115
    • 0027366440 scopus 로고
    • Agonist-stimulated synthesis of phosphatidylinositol(3,4,5)-trisphosphate
    • Stephens LR, Jackson TR, Hawkins PT. 1993. Agonist-stimulated synthesis of phosphatidylinositol(3,4,5)-trisphosphate. Biochim Biophys Acta 1179:27-75.
    • (1993) Biochim Biophys Acta , vol.1179 , pp. 27-75
    • Stephens, L.R.1    Jackson, T.R.2    Hawkins, P.T.3
  • 117
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle - A cascade of protein-protein interactions
    • Südhof TC. 1995. The synaptic vesicle cycle - A cascade of protein-protein interactions. Nature 375:645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 120
    • 0028783371 scopus 로고
    • 2+-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V
    • 2+-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V. Nat Struct Biol 2:968-974.
    • (1995) Nat Struct Biol , vol.2 , pp. 968-974
    • Swairjo, M.A.1    Concha, N.O.2    Kaetzel, J.R.3    Seaton, B.A.4
  • 121
    • 0027738827 scopus 로고
    • The human active breakpoint cluster region-related gene encodes a brain protein with homology to guanine nucleotide exchange proteins and GTPase-activating proteins
    • Tan E-C, Leung T, Manser E, Lim L. 1993. The human active breakpoint cluster region-related gene encodes a brain protein with homology to guanine nucleotide exchange proteins and GTPase-activating proteins. J Biol Chem 268:27291-27298.
    • (1993) J Biol Chem , vol.268 , pp. 27291-27298
    • Tan, E.-C.1    Leung, T.2    Manser, E.3    Lim, L.4
  • 122
    • 0029135419 scopus 로고
    • Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state
    • Tanaka T, Ames JB, Harvey TS, Stryer L, Ikura M. 1995. Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state. Nature 376:444-447.
    • (1995) Nature , vol.376 , pp. 444-447
    • Tanaka, T.1    Ames, J.B.2    Harvey, T.S.3    Stryer, L.4    Ikura, M.5
  • 124
    • 0024009008 scopus 로고
    • SCH9, a gene of Saccharomyces cerevisiae that encodes a protein distinct from, but functionally and structurally related to, cAMP-dependent protein kinase catalytic subunits
    • Toda T, Cameron S, Sass P, Wigler M. 1988. SCH9, a gene of Saccharomyces cerevisiae that encodes a protein distinct from, but functionally and structurally related to, cAMP-dependent protein kinase catalytic subunits. Genes Dev 2:517-527.
    • (1988) Genes Dev , vol.2 , pp. 517-527
    • Toda, T.1    Cameron, S.2    Sass, P.3    Wigler, M.4
  • 125
    • 0027212463 scopus 로고
    • Two novel protein kinase C-related genes of fission yeast are essential for viability and implicated in cell shape control
    • Toda T, Shimamiki M, Yanagida M. 1993. Two novel protein kinase C-related genes of fission yeast are essential for viability and implicated in cell shape control EMBO J 12:1987-1995.
    • (1993) EMBO J , vol.12 , pp. 1987-1995
    • Toda, T.1    Shimamiki, M.2    Yanagida, M.3
  • 127
    • 0028924622 scopus 로고
    • Phosphatidylserine decarboxylase 2 of Saccharomyces cerevisae
    • Trotter PJ, Pedretti J, Yates R, Voelker DR. 1995. Phosphatidylserine decarboxylase 2 of Saccharomyces cerevisae. J Biol Chem 270:6071-6080.
    • (1995) J Biol Chem , vol.270 , pp. 6071-6080
    • Trotter, P.J.1    Pedretti, J.2    Yates, R.3    Voelker, D.R.4
  • 132
    • 0027983786 scopus 로고
    • Cloning and expression of phosphatidylcholine-hydrolyzing phospholipase D from Ricinus communis L
    • Wang X, Xu L, Zheng L. 1994. Cloning and expression of phosphatidylcholine-hydrolyzing phospholipase D from Ricinus communis L J Biol Chem 269:20312-20317
    • (1994) J Biol Chem , vol.269 , pp. 20312-20317
    • Wang, X.1    Xu, L.2    Zheng, L.3
  • 133
    • 0027942615 scopus 로고
    • AtVPS34, a phosphatidylinositol 3-kinase of Arabidopsis thaliana, is an essential protein with homology to a calcium-dependent lipid banding domain
    • Welters P, Takegawa K, Emr SD, Chrispeels MJ. 1994. AtVPS34, a phosphatidylinositol 3-kinase of Arabidopsis thaliana, is an essential protein with homology to a calcium-dependent lipid banding domain Proc Natl Acad Sci USA 91:11398-11402.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11398-11402
    • Welters, P.1    Takegawa, K.2    Emr, S.D.3    Chrispeels, M.J.4
  • 135
    • 0027465720 scopus 로고
    • Identification of critical regions on phospholipase C-β1 required for activation by G-proteins
    • Wu D, Jiang H, Katz A, Simon MI. 1993. Identification of critical regions on phospholipase C-β1 required for activation by G-proteins. J Biol Chem 268:3704-3709.
    • (1993) J Biol Chem , vol.268 , pp. 3704-3709
    • Wu, D.1    Jiang, H.2    Katz, A.3    Simon, M.I.4
  • 139
    • 0028168590 scopus 로고
    • Synaptotagmin I is a high affinity receptor for clathrin AP-2: Implications for membrane recycling
    • Zhang JZ, Davletov BA, Südhof TC, Anderson RGW. 1994. Synaptotagmin I is a high affinity receptor for clathrin AP-2: Implications for membrane recycling. Cell 78:751-760.
    • (1994) Cell , vol.78 , pp. 751-760
    • Zhang, J.Z.1    Davletov, B.A.2    Südhof, T.C.3    Anderson, R.G.W.4


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