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Volumn 7, Issue 4, 1997, Pages 557-565

Protein kinase C and phospholipase C: Bilayer interactions and regulation

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOLIPASE C; PROTEIN KINASE C;

EID: 0030755311     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80122-4     Document Type: Article
Times cited : (65)

References (69)
  • 1
    • 0028986998 scopus 로고
    • 2 hydrolysis and regulation of phospholipase C isozymes
    • 2 hydrolysis and regulation of phospholipase C isozymes. Curr Opin Cell Biol. 7:1995;183-189.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 183-189
    • Lee, S.B.1    Rhee, S.G.2
  • 2
    • 0030987070 scopus 로고    scopus 로고
    • Regulation of protein kinase C
    • of special interest. Lipid regulation of protein kinase C is put into context with its other regulatory mechanisms - protein phosphorylation and subcellular localization.
    • Newton AC. Regulation of protein kinase C. of special interest Curr Opin Cell Biol. 9:1997;161-167 Lipid regulation of protein kinase C is put into context with its other regulatory mechanisms - protein phosphorylation and subcellular localization.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 161-167
    • Newton, A.C.1
  • 3
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • Nishizuka Y. Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 9:1995;484-496.
    • (1995) FASEB J , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 4
    • 0029996139 scopus 로고    scopus 로고
    • Signal transduction through lipid second messengers
    • Spiegel S, Foster D, Kolesnick R. Signal transduction through lipid second messengers. Curr Opin Cell Biol. 8:1996;159-167.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 159-167
    • Spiegel, S.1    Foster, D.2    Kolesnick, R.3
  • 5
    • 0029157058 scopus 로고
    • Pleckstrin homology domains: A fact file
    • Saraste M, Hyvonen M. Pleckstrin homology domains: a fact file. Curr Opin Struct Biol. 5:1995;403-408.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 403-408
    • Saraste, M.1    Hyvonen, M.2
  • 6
    • 0029939448 scopus 로고    scopus 로고
    • PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surfaces
    • of special interest. The functions of different surfaces of PH and PTB domains in binding different ligands are discussed.
    • Lemmon MA, Ferguson KM, Schlessinger J. PH domains: diverse sequences with a common fold recruit signaling molecules to the cell surfaces. of special interest Cell. 85:1996;621-624 The functions of different surfaces of PH and PTB domains in binding different ligands are discussed.
    • (1996) Cell , vol.85 , pp. 621-624
    • Lemmon, M.A.1    Ferguson, K.M.2    Schlessinger, J.3
  • 7
    • 0027310309 scopus 로고
    • Proteolytic fragments of phosphoinositide-specific phospholipase C-δ1. Catalytic and membrane binding properties
    • Cifuentes ME, Honkanen L, Rebecchi MJ. Proteolytic fragments of phosphoinositide-specific phospholipase C-δ1. Catalytic and membrane binding properties. J Biol Chem. 268:1993;11586-11593.
    • (1993) J Biol Chem , vol.268 , pp. 11586-11593
    • Cifuentes, M.E.1    Honkanen, L.2    Rebecchi, M.J.3
  • 8
    • 0028787055 scopus 로고
    • The pleckstrin homology domain of phospholipase C-δ1 binds with high affinity to phosphatidylinositol 4,5-bisphosphate in bilayer membranes
    • Garcia P, Gupta R, Shah S, Morris AJ, Rudge SA, Scarlata S, Petrova V, McLaughlin S, Rebecchi MJ. The pleckstrin homology domain of phospholipase C-δ1 binds with high affinity to phosphatidylinositol 4,5-bisphosphate in bilayer membranes. Biochemistry. 34:1995;16228-16234.
    • (1995) Biochemistry , vol.34 , pp. 16228-16234
    • Garcia, P.1    Gupta, R.2    Shah, S.3    Morris, A.J.4    Rudge, S.A.5    Scarlata, S.6    Petrova, V.7    McLaughlin, S.8    Rebecchi, M.J.9
  • 10
    • 0028874438 scopus 로고
    • Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain
    • Lemmon MA, Ferguson KM, O'Brien R, Sigler PB, Schlessinger J. Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain. Proc Natl Acad Sci USA. 92:1995;10472-10476.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10472-10476
    • Lemmon, M.A.1    Ferguson, K.M.2    O'Brien, R.3    Sigler, P.B.4    Schlessinger, J.5
  • 11
    • 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. Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell. 83:1995;1037-1046.
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 12
    • 0031050299 scopus 로고    scopus 로고
    • Taxonomy and function of C1 protein kinase C homology domains
    • of special interest. The C1 domain (formerly known as the 'cys1 and cys2', 'zinc butterfly', 'zinc finger' or 'cysteine-rich domain' among other terms) nomenclature is standardized. The domains are considered as a structural family with diverse functions, enumerated and subdivided into those that bind phorbol ester (typical) and those that do not (atypical).
    • Hurley JH, Newton AC, Parker PJ, Blumberg PM, Nishizuka Y. Taxonomy and function of C1 protein kinase C homology domains. of special interest Protein Sci. 6:1997;477-480 The C1 domain (formerly known as the 'cys1 and cys2', 'zinc butterfly', 'zinc finger' or 'cysteine-rich domain' among other terms) nomenclature is standardized. The domains are considered as a structural family with diverse functions, enumerated and subdivided into those that bind phorbol ester (typical) and those that do not (atypical).
    • (1997) Protein Sci , vol.6 , pp. 477-480
    • Hurley, J.H.1    Newton, A.C.2    Parker, P.J.3    Blumberg, P.M.4    Nishizuka, Y.5
  • 13
    • 0028979464 scopus 로고
    • Crystal structure of the Cys2 activator-binding domain of protein kinase C δ in complex with phorbol ester
    • Zhang G, Kazanietz MG, Blumberg PM, Hurley JH. Crystal structure of the Cys2 activator-binding domain of protein kinase C δ in complex with phorbol ester. Cell. 81:1995;917-924.
    • (1995) Cell , vol.81 , pp. 917-924
    • Zhang, G.1    Kazanietz, M.G.2    Blumberg, P.M.3    Hurley, J.H.4
  • 14
    • 0028310840 scopus 로고
    • Zinc finger domains and phorbol ester pharmacophore: Analysis of binding to mutated form of protein kinase Cζ and the vav and c-raf proto-oncogene products
    • Kazanietz MG, Bustelo XR, Barbacid M, Kolch W, Mischak H, Wong G, Pettit GR, Bruns JD, Blumberg PM. Zinc finger domains and phorbol ester pharmacophore: analysis of binding to mutated form of protein kinase Cζ and the vav and c-raf proto-oncogene products. J Biol Chem. 269:1994;11590-11594.
    • (1994) J Biol Chem , vol.269 , pp. 11590-11594
    • Kazanietz, M.G.1    Bustelo, X.R.2    Barbacid, M.3    Kolch, W.4    Mischak, H.5    Wong, G.6    Pettit, G.R.7    Bruns, J.D.8    Blumberg, P.M.9
  • 15
    • 0029102822 scopus 로고
    • Residues in the second cysteine-rich region of protein kinase C δ relevant to phorbol ester binding as revealed by site-directed mutagenesis
    • Kazanietz MG, Wang S, Milne GWA, Lewin NE, Lui HL, Blumberg PM. Residues in the second cysteine-rich region of protein kinase C δ relevant to phorbol ester binding as revealed by site-directed mutagenesis. J Biol Chem. 270:1995;21852-21859.
    • (1995) J Biol Chem , vol.270 , pp. 21852-21859
    • Kazanietz, M.G.1    Wang, S.2    Milne, G.W.A.3    Lewin, N.E.4    Lui, H.L.5    Blumberg, P.M.6
  • 16
    • 0029757119 scopus 로고    scopus 로고
    • The solution structure of the Raf-1 cysteine-rich domain: A novel Ras and phospholipid binding site
    • of special interest. The first structure of an atypical C1 domain explains why the atypical C1 domains do not bind phorbol ester or diacylglycerol. One wall of the binding groove is torn away as compared with a typical C1 domain.
    • Mott HR, Carpenter JW, Zhong S, Ghosh S, Bell RM, Campbell SL. The solution structure of the Raf-1 cysteine-rich domain: a novel Ras and phospholipid binding site. of special interest Proc Natl Acad Sci USA. 93:1996;8312-8317 The first structure of an atypical C1 domain explains why the atypical C1 domains do not bind phorbol ester or diacylglycerol. One wall of the binding groove is torn away as compared with a typical C1 domain.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8312-8317
    • Mott, H.R.1    Carpenter, J.W.2    Zhong, S.3    Ghosh, S.4    Bell, R.M.5    Campbell, S.L.6
  • 17
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: Structural and functional diversity
    • of special interest. An invaluable compilation of the vast amount of information available on the full range of C2 domains and C2 domain containing proteins.
    • Nalefski EA, Falke JJ. The C2 domain calcium-binding motif: structural and functional diversity. of special interest Protein Sci. 5:1996;2375-2390 An invaluable compilation of the vast amount of information available on the full range of C2 domains and C2 domain containing proteins.
    • (1996) Protein Sci , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 19
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase C δ
    • of outstanding interest. The structure of rat phosphoinositide-specific phospholipase C δ1, containing the EF-hand, catalytic, and C2 domains but with the PH domain removed, is reported. The catalytic domain resembles that of bacterial phosphatidylinositol-specific phospholipase C, and the C2 domain is a topologically permuted cousin of the synaptotagmin I C2 domain. All three domains interact via extensive contact surfaces.
    • Essen LO, Perisic O, Cheung R, Katan M, Williams RL. Crystal structure of a mammalian phosphoinositide-specific phospholipase C δ of outstanding interest Nature. 380:1996;595-602 The structure of rat phosphoinositide-specific phospholipase C δ1, containing the EF-hand, catalytic, and C2 domains but with the PH domain removed, is reported. The catalytic domain resembles that of bacterial phosphatidylinositol-specific phospholipase C, and the C2 domain is a topologically permuted cousin of the synaptotagmin I C2 domain. All three domains interact via extensive contact surfaces.
    • (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
    • 0030967642 scopus 로고    scopus 로고
    • Similarity between C2 domain jaws and immunoglobulin CDRs
    • of special interest. The immunoglobulin fold has cropped up almost everywhere else in cell biology, and now we know that C2 domains are Ig folds. The occurrence of this fold in intracellular signal transduction is rationalized in terms of its unique suitability as a scaffold for generating diverse molecular recognition surfaces.
    • Grobler JA, Hurley JH. Similarity between C2 domain jaws and immunoglobulin CDRs. of special interest Nat Struct Biol. 4:1997;261-262 The immunoglobulin fold has cropped up almost everywhere else in cell biology, and now we know that C2 domains are Ig folds. The occurrence of this fold in intracellular signal transduction is rationalized in terms of its unique suitability as a scaffold for generating diverse molecular recognition surfaces.
    • (1997) Nat Struct Biol , vol.4 , pp. 261-262
    • Grobler, J.A.1    Hurley, J.H.2
  • 21
    • 0029772577 scopus 로고    scopus 로고
    • C2 domain conformational changes in phospholipase C δ
    • 2+ activation of protein kinase C and other C2 domain containing proteins. The C2 domain jaws are implicated in function by this conformational change and by the docking of phospholipase C δ1 to a bilayer model.
    • 2+ activation of protein kinase C and other C2 domain containing proteins. The C2 domain jaws are implicated in function by this conformational change and by the docking of phospholipase C δ1 to a bilayer model.
    • (1996) Nat Struct Biol , vol.3 , pp. 788-795
    • Grobler, J.A.1    Essen, L.O.2    Williams, R.L.3    Hurley, J.H.4
  • 22
    • 0029666292 scopus 로고    scopus 로고
    • 2+-binding motif in C2 domains of synaptotagmin and protein kinase C
    • 2+ ions to the C2 domains of protein kinase C βII and synaptotagmin I. Some resonances disappear in the aposynaptotagmin I spectrum, indicating changes in dynamics or average conformation, or both.
    • 2+ ions to the C2 domains of protein kinase C βII and synaptotagmin I. Some resonances disappear in the aposynaptotagmin I spectrum, indicating changes in dynamics or average conformation, or both.
    • (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
  • 23
    • 0028356989 scopus 로고
    • Characterization of the calcium-binding site that regulates association of protein kinase C with phospholipid bilayers
    • Mosior M, Epand RM. Characterization of the calcium-binding site that regulates association of protein kinase C with phospholipid bilayers. J Biol Chem. 269:1994;13798-13805.
    • (1994) J Biol Chem , vol.269 , pp. 13798-13805
    • Mosior, M.1    Epand, R.M.2
  • 24
    • 0028172171 scopus 로고
    • 2+-dependent conformational change in synaptotagmin I
    • 2+-dependent conformational change in synaptotagmin I. J Biol Chem. 269:1994;28547-28550.
    • (1994) J Biol Chem , vol.269 , pp. 28547-28550
    • Davletov, B.A.1    Sudhof, T.C.2
  • 25
    • 0031016185 scopus 로고    scopus 로고
    • Structural mapping of the catalytic mechanism for a mammalian phosphoinositide-specific phospholipase C
    • Essen L-O, Perisic O, Katan M, Wu Y, Roberts MF, Williams RL. Structural mapping of the catalytic mechanism for a mammalian phosphoinositide-specific phospholipase C. Biochemistry. 36:1997;1704-1718.
    • (1997) Biochemistry , vol.36 , pp. 1704-1718
    • Essen, L.-O.1    Perisic, O.2    Katan, M.3    Wu, Y.4    Roberts, M.F.5    Williams, R.L.6
  • 26
    • 0029121937 scopus 로고
    • Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol
    • Heinz DW, Ryan M, Bullock TL, Griffith OH. Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol. EMBO J. 14:1995;3855-3863.
    • (1995) EMBO J , vol.14 , pp. 3855-3863
    • Heinz, D.W.1    Ryan, M.2    Bullock, T.L.3    Griffith, O.H.4
  • 27
    • 0027232834 scopus 로고
    • Interaction of proteins with lipid headgroups: Lessons from protein kinase C
    • Newton AC. Interaction of proteins with lipid headgroups: lessons from protein kinase C. Annu Rev Biophys Biomol Struct. 22:1993;1-25.
    • (1993) Annu Rev Biophys Biomol Struct , vol.22 , pp. 1-25
    • Newton, A.C.1
  • 28
    • 0030586160 scopus 로고    scopus 로고
    • The effects of non-lamellar forming lipids on membrane protein - lipid interactions
    • of special interest. This paper presents a thoughtful argument that curvature stress is an important factor in protein - bilayer interactions.
    • Stubbs CD, Slater SJ. The effects of non-lamellar forming lipids on membrane protein - lipid interactions. of special interest Chem Phys Lipids. 81:1996;185-195 This paper presents a thoughtful argument that curvature stress is an important factor in protein - bilayer interactions.
    • (1996) Chem Phys Lipids , vol.81 , pp. 185-195
    • Stubbs, C.D.1    Slater, S.J.2
  • 29
    • 0027092982 scopus 로고
    • Phosphoinositide-specific phospholipase C-δ1: Effect of monolayer surface pressure and electrostatic surface potentials on activity
    • Rebecchi M, Boguslavsky V, Boguslavsky L, McLaughlin S. Phosphoinositide-specific phospholipase C-δ1: effect of monolayer surface pressure and electrostatic surface potentials on activity. Biochemistry. 31:1992;12748-12753.
    • (1992) Biochemistry , vol.31 , pp. 12748-12753
    • Rebecchi, M.1    Boguslavsky, V.2    Boguslavsky, L.3    McLaughlin, S.4
  • 31
    • 0029130345 scopus 로고
    • Lipid signaling enzymes and surface dilution kinetics
    • Carman GM, Deems RA, Dennis EA. Lipid signaling enzymes and surface dilution kinetics. J Biol Chem. 270:1995;18711-18714.
    • (1995) J Biol Chem , vol.270 , pp. 18711-18714
    • Carman, G.M.1    Deems, R.A.2    Dennis, E.A.3
  • 32
    • 0030062076 scopus 로고    scopus 로고
    • Calcium-independent binding to interfacial phorbol esters causes protein kinase C to associate with membranes in the absence of acidic lipids
    • of outstanding interest. This ambitious attempt to formulate the membrane binding of protein kinase C in terms of a rigorous model of linked equilibria puts the classical activation scheme into a new perspective. Binding experiments and mathematical modeling show that the requirement of protein kinase C for one type of activator can be bypassed in the presence of a large excess of another activator.
    • Mosior M, Newton AC. Calcium-independent binding to interfacial phorbol esters causes protein kinase C to associate with membranes in the absence of acidic lipids. of outstanding interest Biochemistry. 35:1996;1612-1623 This ambitious attempt to formulate the membrane binding of protein kinase C in terms of a rigorous model of linked equilibria puts the classical activation scheme into a new perspective. Binding experiments and mathematical modeling show that the requirement of protein kinase C for one type of activator can be bypassed in the presence of a large excess of another activator.
    • (1996) Biochemistry , vol.35 , pp. 1612-1623
    • Mosior, M.1    Newton, A.C.2
  • 33
    • 0028203902 scopus 로고
    • Effect of monolayer surface pressure on the activities of phosphoinositide-specific phospholipase C-β1, γ1, and δ1
    • Boguslavsky V, Rebecchi M, Morris AJ, Jhon DY, Rhee SG, McLaughlin S. Effect of monolayer surface pressure on the activities of phosphoinositide-specific phospholipase C-β1, γ1, and δ1. Biochemistry. 33:1994;3032-3037.
    • (1994) Biochemistry , vol.33 , pp. 3032-3037
    • Boguslavsky, V.1    Rebecchi, M.2    Morris, A.J.3    Jhon, D.Y.4    Rhee, S.G.5    McLaughlin, S.6
  • 34
    • 0031050619 scopus 로고    scopus 로고
    • Dependence of the activity of phospholipase Cβ on surface pressure and surface composition in phospholipid monolayers and its implications for their regulation
    • James SR, Paterson A, Harden TK, Demel RA, Downes CP. Dependence of the activity of phospholipase Cβ on surface pressure and surface composition in phospholipid monolayers and its implications for their regulation. Biochemistry. 36:1997;848-855.
    • (1997) Biochemistry , vol.36 , pp. 848-855
    • James, S.R.1    Paterson, A.2    Harden, T.K.3    Demel, R.A.4    Downes, C.P.5
  • 35
    • 0023747140 scopus 로고
    • Association of protein kinase C with phospholipid monolayers: Two-stage irreversible binding
    • Bazzi MD, Nelsestuen GL. Association of protein kinase C with phospholipid monolayers: two-stage irreversible binding. Biochemistry. 27:1988;6776-6783.
    • (1988) Biochemistry , vol.27 , pp. 6776-6783
    • Bazzi, M.D.1    Nelsestuen, G.L.2
  • 37
    • 0026729365 scopus 로고
    • Effect of phospholipid unsaturation on protein kinase C activation
    • Bolen EJ, Sando JJ. Effect of phospholipid unsaturation on protein kinase C activation. Biochemistry. 31:1992;5945-5951.
    • (1992) Biochemistry , vol.31 , pp. 5945-5951
    • Bolen, E.J.1    Sando, J.J.2
  • 38
    • 0028840703 scopus 로고
    • Role of phospholipids containing docosahexaenoyl chains in modulating the activity of protein kinase C
    • Giorgione J, Epand RM, Buda C, Farkas T. Role of phospholipids containing docosahexaenoyl chains in modulating the activity of protein kinase C. Proc Natl Acad Sci USA. 92:1995;9767-9770.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9767-9770
    • Giorgione, J.1    Epand, R.M.2    Buda, C.3    Farkas, T.4
  • 39
    • 0028075333 scopus 로고
    • The modulation of protein kinase C activity by membrane lipid bilayer structure
    • Slater SJ, Kelly MB, Taddeo FJ, Ho C, Rugin E, Stubbs CD. The modulation of protein kinase C activity by membrane lipid bilayer structure. J Biol Chem. 269:1994;4866-4871.
    • (1994) J Biol Chem , vol.269 , pp. 4866-4871
    • Slater, S.J.1    Kelly, M.B.2    Taddeo, F.J.3    Ho, C.4    Rugin, E.5    Stubbs, C.D.6
  • 40
    • 0029966229 scopus 로고    scopus 로고
    • Transbilayer inhibition of protein kinase C by the lipophosphoglycan from Leishmania donovani
    • Giorgione JR, Turco SJ, Epand RM. Transbilayer inhibition of protein kinase C by the lipophosphoglycan from Leishmania donovani. Proc Natl Acad Sci USA. 93:1996;11634-11639.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11634-11639
    • Giorgione, J.R.1    Turco, S.J.2    Epand, R.M.3
  • 41
    • 10244224044 scopus 로고    scopus 로고
    • Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol-4,5 bisphosphate in lateral domains
    • of outstanding interest. Microdomain formation induced by the MARCKS protein inhibits phospholipase C and is reversible by protein kinase C phosphorylation.
    • Glaser M, Wanaski S, Buser CA, Boguslavsky V, Rashidzada W, Morris A, Rebecchi M, Scarlata SF, Runnels LW, Prestwich GD, et al. Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol-4,5 bisphosphate in lateral domains. of outstanding interest J Biol Chem. 271:1996;26187-26193 Microdomain formation induced by the MARCKS protein inhibits phospholipase C and is reversible by protein kinase C phosphorylation.
    • (1996) J Biol Chem , vol.271 , pp. 26187-26193
    • Glaser, M.1    Wanaski, S.2    Buser, C.A.3    Boguslavsky, V.4    Rashidzada, W.5    Morris, A.6    Rebecchi, M.7    Scarlata, S.F.8    Runnels, L.W.9    Prestwich, G.D.10
  • 42
    • 0028952293 scopus 로고
    • Membrane domains containing phosphatidylserine and substrate can be important for the activation of protein kinase C
    • Yang L, Glaser M. Membrane domains containing phosphatidylserine and substrate can be important for the activation of protein kinase C. Biochemistry. 34:1995;1500-1506.
    • (1995) Biochemistry , vol.34 , pp. 1500-1506
    • Yang, L.1    Glaser, M.2
  • 43
    • 0029904712 scopus 로고    scopus 로고
    • Formation of membrane domains during the activation of protein kinase C
    • of outstanding interest. Fluorescence microscopy is used to directly observe protein kinase C colocalizing with membrane domains under activating conditions.
    • Yang L, Glaser M. Formation of membrane domains during the activation of protein kinase C. of outstanding interest Biochemistry. 35:1996;13966-13974 Fluorescence microscopy is used to directly observe protein kinase C colocalizing with membrane domains under activating conditions.
    • (1996) Biochemistry , vol.35 , pp. 13966-13974
    • Yang, L.1    Glaser, M.2
  • 44
    • 0029792683 scopus 로고    scopus 로고
    • Lipid lateral heterogeneity in phosphatidylcholine/phosphatidylserine/diacylglycerol vesicles and its influence on protein kinase C activation
    • of special interest. Microdomains and microdomain boundary formation monitored thermodynamically and correlated with protein kinase C activation.
    • Dibble ARG, Hinderliter AK, Sando JJ, Biltonen RL. Lipid lateral heterogeneity in phosphatidylcholine/phosphatidylserine/diacylglycerol vesicles and its influence on protein kinase C activation. of special interest Biophys J. 71:1996;1877-1890 Microdomains and microdomain boundary formation monitored thermodynamically and correlated with protein kinase C activation.
    • (1996) Biophys J , vol.71 , pp. 1877-1890
    • Dibble, A.R.G.1    Hinderliter, A.K.2    Sando, J.J.3    Biltonen, R.L.4
  • 45
    • 0030448583 scopus 로고    scopus 로고
    • Inhibition of phospholipase C-δ1 catalytic activity by sphingomyelin
    • of special interest. The biophysical basis for sphingomyelin inhibition of phospholipase C is explained by its this lipid's ability to stabilize the membrane interface against protein penetration.
    • Scarlata S, Gupta R, Garcia P, Keach H, Shah S, Kasireddy CR, Bittman R, Rebecchi MJ. Inhibition of phospholipase C-δ1 catalytic activity by sphingomyelin. of special interest Biochemistry. 35:1996;14882-14888 The biophysical basis for sphingomyelin inhibition of phospholipase C is explained by its this lipid's ability to stabilize the membrane interface against protein penetration.
    • (1996) Biochemistry , vol.35 , pp. 14882-14888
    • Scarlata, S.1    Gupta, R.2    Garcia, P.3    Keach, H.4    Shah, S.5    Kasireddy, C.R.6    Bittman, R.7    Rebecchi, M.J.8
  • 46
    • 0029038685 scopus 로고
    • Low affinity binding of phorbol esters to protein kinase C and its recombinant cysteine-rich region in the absence of phospholipids
    • Kazanietz MG, Barchi JJ, Omichinski JG, Blumberg PM. Low affinity binding of phorbol esters to protein kinase C and its recombinant cysteine-rich region in the absence of phospholipids. J Biol Chem. 270:1995;14679-14684.
    • (1995) J Biol Chem , vol.270 , pp. 14679-14684
    • Kazanietz, M.G.1    Barchi, J.J.2    Omichinski, J.G.3    Blumberg, P.M.4
  • 47
    • 0025265401 scopus 로고
    • Protein kinase C penetration into lipid bilayers
    • Brumfeld V, Lester DS. Protein kinase C penetration into lipid bilayers. Arch Biochem Biophys. 277:1990;318-323.
    • (1990) Arch Biochem Biophys , vol.277 , pp. 318-323
    • Brumfeld, V.1    Lester, D.S.2
  • 48
    • 0028843905 scopus 로고
    • Mechanism of interaction of protein kinase C with phorbol esters. Reversibility and nature of membrane association
    • Mosior M, Newton AC. Mechanism of interaction of protein kinase C with phorbol esters. Reversibility and nature of membrane association. J Biol Chem. 270:1995;25526-25533.
    • (1995) J Biol Chem , vol.270 , pp. 25526-25533
    • Mosior, M.1    Newton, A.C.2
  • 49
    • 0025914405 scopus 로고
    • Binding of peptides with basic residues to membranes containing acidic phospholipids
    • Kim J, Mosior M, Chung LA, Wu H, McLaughlin S. Binding of peptides with basic residues to membranes containing acidic phospholipids. Biophys J. 60:1991;135-148.
    • (1991) Biophys J , vol.60 , pp. 135-148
    • Kim, J.1    Mosior, M.2    Chung, L.A.3    Wu, H.4    McLaughlin, S.5
  • 51
    • 0028341564 scopus 로고
    • Phosphatidyl-L-serine is necessary for protein kinase C's high-affinity interaction with diacylglycerol-containing membranes
    • Newton AC, Keranen LM. Phosphatidyl-L-serine is necessary for protein kinase C's high-affinity interaction with diacylglycerol-containing membranes. Biochemistry. 33:1994;6651-6658.
    • (1994) Biochemistry , vol.33 , pp. 6651-6658
    • Newton, A.C.1    Keranen, L.M.2
  • 52
    • 0028292769 scopus 로고
    • Intrapeptide regulation of protein kinase C
    • Orr JW, Newton AC. Intrapeptide regulation of protein kinase C. J Biol Chem. 269:1994;8383-8387.
    • (1994) J Biol Chem , vol.269 , pp. 8383-8387
    • Orr, J.W.1    Newton, A.C.2
  • 53
    • 0031055195 scopus 로고    scopus 로고
    • Role of water in protein kinase C catalysis and its binding to membranes
    • Giorgione JR, Epand RM. Role of water in protein kinase C catalysis and its binding to membranes. Biochemistry. 36:1997;2230-2236.
    • (1997) Biochemistry , vol.36 , pp. 2230-2236
    • Giorgione, J.R.1    Epand, R.M.2
  • 54
    • 0029785953 scopus 로고    scopus 로고
    • Non-equivalent roles for the first and second zinc fingers of protein kinase Cδ
    • of outstanding interest. Site-directed mutagenesis is used to explain why protein kinase C has two C1 domains. The C1B, and not the C1A, domain is required for efficient translocation of transfected protein kinase to the plasma membrane. Future studies of the activation of purified proteins should be even more revealing.
    • Szallasi Z, Bogi K, Gohari S, Biro T, Acs P, Blumberg PM. Non-equivalent roles for the first and second zinc fingers of protein kinase Cδ of outstanding interest J Biol Chem. 271:1996;18299-18301 Site-directed mutagenesis is used to explain why protein kinase C has two C1 domains. The C1B, and not the C1A, domain is required for efficient translocation of transfected protein kinase to the plasma membrane. Future studies of the activation of purified proteins should be even more revealing.
    • (1996) J Biol Chem , vol.271 , pp. 18299-18301
    • Szallasi, Z.1    Bogi, K.2    Gohari, S.3    Biro, T.4    Acs, P.5    Blumberg, P.M.6
  • 55
    • 0029670030 scopus 로고    scopus 로고
    • Protein kinase C α contains two activator binding sites that bind phorbol esters and diacylglycerols with opposite affinities
    • Slater SJ, Ho C, Kelly MB, Larkin JD, Taddeo FJ, Yeager MD, Stubbs CD. Protein kinase C α contains two activator binding sites that bind phorbol esters and diacylglycerols with opposite affinities. J Biol Chem. 271:1996;4627-4631.
    • (1996) J Biol Chem , vol.271 , pp. 4627-4631
    • Slater, S.J.1    Ho, C.2    Kelly, M.B.3    Larkin, J.D.4    Taddeo, F.J.5    Yeager, M.D.6    Stubbs, C.D.7
  • 56
    • 0031014220 scopus 로고    scopus 로고
    • Cysteine-rich regions of protein kinase Cδ are functionally non-equivalent. Differences between cysteine-rich regions of non-calcium-dependent protein kinase Cδ and calcium-dependent protein kinase Cγ
    • Humm M, Quest AFG. Cysteine-rich regions of protein kinase Cδ are functionally non-equivalent. Differences between cysteine-rich regions of non-calcium-dependent protein kinase Cδ and calcium-dependent protein kinase Cγ FEBS Lett. 400:1997;226-232.
    • (1997) FEBS Lett , vol.400 , pp. 226-232
    • Humm, M.1    Quest, A.F.G.2
  • 57
    • 0029921355 scopus 로고    scopus 로고
    • Chemical specificity and physical properties of the lipid bilayer in the regulation of protein kinase C by anionic phospholipids: Evidence for the lack of a specific binding site for phosphatidylserine
    • Mosior M, Golini ES, Epand RM. Chemical specificity and physical properties of the lipid bilayer in the regulation of protein kinase C by anionic phospholipids: evidence for the lack of a specific binding site for phosphatidylserine. Proc Natl Acad Sci USA. 93:1996;1907-1912.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1907-1912
    • Mosior, M.1    Golini, E.S.2    Epand, R.M.3
  • 58
    • 0027460089 scopus 로고
    • 1 contains phosphatidylserine- And phorbol ester-dependent calcium binding activity
    • 1 contains phosphatidylserine- and phorbol ester-dependent calcium binding activity. J Biol Chem. 268:1993;3715-3719.
    • (1993) J Biol Chem , vol.268 , pp. 3715-3719
    • Luo, J.-H.1    Kahn, S.2    O'Driscoll, K.3    Weinstein, I.B.4
  • 59
    • 0028021161 scopus 로고
    • The regulatory region of protein kinase Cγ
    • Quest AFG, Bell RM. The regulatory region of protein kinase Cγ J Biol Chem. 269:1994;20000-20012.
    • (1994) J Biol Chem , vol.269 , pp. 20000-20012
    • Quest, A.F.G.1    Bell, R.M.2
  • 60
    • 0030053828 scopus 로고    scopus 로고
    • Expression and characterization of Aplysia protein kinase C: A negative regulatory role for the E region
    • Sossin WS, Fan X, Saberi F. Expression and characterization of Aplysia protein kinase C: a negative regulatory role for the E region. J Neurosci. 16:1996;10-18.
    • (1996) J Neurosci , vol.16 , pp. 10-18
    • Sossin, W.S.1    Fan, X.2    Saberi, F.3
  • 61
    • 0029039839 scopus 로고
    • A twist in the tale of lipolytic enzymes
    • Derewenda ZS. A twist in the tale of lipolytic enzymes. Nat Struct Biol. 2:1995;347-349.
    • (1995) Nat Struct Biol , vol.2 , pp. 347-349
    • Derewenda, Z.S.1
  • 66
    • 0027495890 scopus 로고
    • The regulation of phospholipase C-γ1 by phosphatidic acid
    • Jones GA, Carpenter G. The regulation of phospholipase C-γ1 by phosphatidic acid. J Biol Chem. 268:1993;20845-20850.
    • (1993) J Biol Chem , vol.268 , pp. 20845-20850
    • Jones, G.A.1    Carpenter, G.2
  • 67
    • 0029075004 scopus 로고
    • Kinetic analysis of phospholipase Cβ isoforms using phospholipid-detergent mixed micelles
    • James SR, Paterson A, Harden TK, Downes CP. Kinetic analysis of phospholipase Cβ isoforms using phospholipid-detergent mixed micelles. J Biol Chem. 270:1995;11872-11881.
    • (1995) J Biol Chem , vol.270 , pp. 11872-11881
    • James, S.R.1    Paterson, A.2    Harden, T.K.3    Downes, C.P.4
  • 68
    • 0029841118 scopus 로고    scopus 로고
    • The role of carboxyl-terminal basic amino acids in Gα-dependent activation, particulate association, and nuclear localization of phospholipase C-β1
    • Kim CG, Park D, Rhee SG. The role of carboxyl-terminal basic amino acids in Gα-dependent activation, particulate association, and nuclear localization of phospholipase C-β1. J Biol Chem. 271:1996;21187-21192.
    • (1996) J Biol Chem , vol.271 , pp. 21187-21192
    • Kim, C.G.1    Park, D.2    Rhee, S.G.3
  • 69
    • 0018788297 scopus 로고
    • The molecular structure of lecithin hydrates
    • Pascher I, Pearson RH. The molecular structure of lecithin hydrates. Nature. 281:1979;499-501.
    • (1979) Nature , vol.281 , pp. 499-501
    • Pascher, I.1    Pearson, R.H.2


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