메뉴 건너뛰기




Volumn 88, Issue 4, 2008, Pages 1341-1378

Structural basis of protein kinase C isoform function

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CASPASE; PROTEIN KINASE C; PROTEIN KINASE C ALPHA; PROTEIN KINASE C BETA; PROTEIN KINASE C DELTA; PROTEIN KINASE C EPSILON; PROTEIN KINASE C ETA; PROTEIN KINASE C GAMMA; PROTEIN KINASE C IOTA; PROTEIN KINASE C LAMBDA; PROTEIN KINASE C THETA; PROTEIN KINASE C ZETA; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; RECEPTOR FOR ACTIVATED C KINASE 1; RECEPTOR FOR ACTIVATED C KINASE 2; SERINE; THREONINE; TYROSINE; UNCLASSIFIED DRUG; ISOENZYME;

EID: 55949109631     PISSN: 00319333     EISSN: 15221210     Source Type: Journal    
DOI: 10.1152/physrev.00034.2007     Document Type: Review
Times cited : (707)

References (239)
  • 1
    • 0342657745 scopus 로고    scopus 로고
    • Effect of a tyrosine 155 to phenylalanine mutation of protein kinase C-δ on the proliferative and tumorigenic properties of NIH 3T3 fibroblasts
    • Acs P, Beheshti M, Szallasi Z, Li L, Yuspa SH, Blumberg PM. Effect of a tyrosine 155 to phenylalanine mutation of protein kinase C-δ on the proliferative and tumorigenic properties of NIH 3T3 fibroblasts. Carcinogenesis 21: 887-891, 2000.
    • (2000) Carcinogenesis , vol.21 , pp. 887-891
    • Acs, P.1    Beheshti, M.2    Szallasi, Z.3    Li, L.4    Yuspa, S.H.5    Blumberg, P.M.6
  • 2
    • 0031052014 scopus 로고    scopus 로고
    • The protein kinase C inhibitors Ro 318220 and GF 109203X are equally potent inhibitors of MAPKAP kinase-1β (Rsk-2) and p70 S6 kinase
    • Alessi DR. The protein kinase C inhibitors Ro 318220 and GF 109203X are equally potent inhibitors of MAPKAP kinase-1β (Rsk-2) and p70 S6 kinase. FEBS Lett 402: 121-123, 1997.
    • (1997) FEBS Lett , vol.402 , pp. 121-123
    • Alessi, D.R.1
  • 3
    • 0344443708 scopus 로고    scopus 로고
    • Activation mechanisms of conventional protein kinase C isoforms are determined by the ligand affinity and conformational flexibility of their C1 domains
    • Ananthanarayanan B, Stahelin RV, Digman MA, Cho W. Activation mechanisms of conventional protein kinase C isoforms are determined by the ligand affinity and conformational flexibility of their C1 domains. J Biol Chem 278: 46886-46894, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 46886-46894
    • Ananthanarayanan, B.1    Stahelin, R.V.2    Digman, M.A.3    Cho, W.4
  • 4
    • 0142073731 scopus 로고    scopus 로고
    • Interaction of fascin and protein kinase Cα: A novel intersection in cell adhesion and motility
    • Anilkumar N, Parsons M, Monk R, Ng T, Adams JC. Interaction of fascin and protein kinase Cα: a novel intersection in cell adhesion and motility. EMBO J 22: 5390-5402, 2003.
    • (2003) EMBO J , vol.22 , pp. 5390-5402
    • Anilkumar, N.1    Parsons, M.2    Monk, R.3    Ng, T.4    Adams, J.C.5
  • 6
    • 0037799269 scopus 로고    scopus 로고
    • Protein kinase C isoformspecific differences in the spatial-temporal regulation and decoding of metabotropic glutamate receptor1a-stimulated second messenger responses
    • Babwah AV, Dale LB, Ferguson SS. Protein kinase C isoformspecific differences in the spatial-temporal regulation and decoding of metabotropic glutamate receptor1a-stimulated second messenger responses. J Biol Chem 278: 5419-5426, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 5419-5426
    • Babwah, A.V.1    Dale, L.B.2    Ferguson, S.S.3
  • 7
    • 0037177860 scopus 로고    scopus 로고
    • Ping P. Nitric oxide induces nitration of PKCε, facilitating PKCε translocation via enhanced PKCε-RACK2 interactions: A novel mechanism of NO-triggered activation of PKC
    • Balafanova Z, Bolli R, Zhang J, Zheng Y, Pass JM, Bhatnagar A, Tang XL, Wang O, Cardwell E, Ping P. Nitric oxide induces nitration of PKCε, facilitating PKCε translocation via enhanced PKCε-RACK2 interactions: a novel mechanism of NO-triggered activation of PKC. J Biol Chem 277: 15021-15027, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 15021-15027
    • Balafanova, Z.1    Bolli, R.2    Zhang, J.3    Zheng, Y.4    Pass, J.M.5    Bhatnagar, A.6    Tang, X.L.7    Wang, O.8    Cardwell, E.9
  • 8
    • 0037066740 scopus 로고    scopus 로고
    • Molecular dynamics characterization of the C2 domain of protein kinase Cβ
    • Banci L, Cavallaro G, Kheifets V, Mochly-Rosen D. Molecular dynamics characterization of the C2 domain of protein kinase Cβ. J Biol Chem 277: 12988-12997, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 12988-12997
    • Banci, L.1    Cavallaro, G.2    Kheifets, V.3    Mochly-Rosen, D.4
  • 9
    • 0036829593 scopus 로고    scopus 로고
    • Proteolytic activation of protein kinase C-ε by caspase-mediated processing and transduction of antiapoptotic signals
    • Basu A, Lu D, Sun B, Moor AN, Akkaraju GR, Huang J. Proteolytic activation of protein kinase C-ε by caspase-mediated processing and transduction of antiapoptotic signals. J Biol Chem 277: 41850-41856, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 41850-41856
    • Basu, A.1    Lu, D.2    Sun, B.3    Moor, A.N.4    Akkaraju, G.R.5    Huang, J.6
  • 10
    • 0346732281 scopus 로고    scopus 로고
    • cPKC-dependent sequestration of membrane-recycling components in a subset of recycling endosomes
    • Becker KP, Hannun YA. cPKC-dependent sequestration of membrane-recycling components in a subset of recycling endosomes. J Biol Chem 278: 52747-52754, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 52747-52754
    • Becker, K.P.1    Hannun, Y.A.2
  • 11
    • 3142654821 scopus 로고    scopus 로고
    • Isoenzyme-specific translocation of PKC-βII and not PKCβI to a juxtanuclear subset of recycling endosomes: Involvement of phospholipase D
    • Becker KP, Hannun YA. Isoenzyme-specific translocation of PKC-βII and not PKCβI to a juxtanuclear subset of recycling endosomes: involvement of phospholipase D. J Biol Chem 279: 28251-28256, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 28251-28256
    • Becker, K.P.1    Hannun, Y.A.2
  • 14
    • 0036132855 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of protein kinase Cδ is essential for its apoptotic effect in response to etoposide
    • Blass M, Kronfeld I, Kazimirsky G, Blumberg PM, Brodie C. Tyrosine phosphorylation of protein kinase Cδ is essential for its apoptotic effect in response to etoposide. Mol Cell Biol 22: 182-195, 2002.
    • (2002) Mol Cell Biol , vol.22 , pp. 182-195
    • Blass, M.1    Kronfeld, I.2    Kazimirsky, G.3    Blumberg, P.M.4    Brodie, C.5
  • 15
    • 0030001021 scopus 로고    scopus 로고
    • Protein kinase C βII specifically binds to and is activated by F-actin
    • Blobe GC, Stribling DS, Fabbro D, Stabel S, Hannun YA. Protein kinase C βII specifically binds to and is activated by F-actin. J Biol Chem 271: 15823-15830, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 15823-15830
    • Blobe, G.C.1    Stribling, D.S.2    Fabbro, D.3    Stabel, S.4    Hannun, Y.A.5
  • 16
    • 0030250879 scopus 로고    scopus 로고
    • Phosphorylation of threonine 638 critically controls the dephosphorylation and inactivation of protein kinase Cα
    • Bornancin F, Parker PJ. Phosphorylation of threonine 638 critically controls the dephosphorylation and inactivation of protein kinase Cα. Curr Biol 6: 1114-1123, 1996.
    • (1996) Curr Biol , vol.6 , pp. 1114-1123
    • Bornancin, F.1    Parker, P.J.2
  • 17
    • 0031021875 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase C-α on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state
    • Bornancin F, Parker PJ. Phosphorylation of protein kinase C-α on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state. J Biol Chem 272: 3544-3549, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 3544-3549
    • Bornancin, F.1    Parker, P.J.2
  • 18
    • 0034634596 scopus 로고    scopus 로고
    • Ceramide directly activates protein kinase C-ζ to regulate a stress-activated protein kinase signaling complex
    • Bourbon NA, Yun J, Kester M. Ceramide directly activates protein kinase C-ζ to regulate a stress-activated protein kinase signaling complex. J Biol Chem 275: 35617-35623, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 35617-35623
    • Bourbon, N.A.1    Yun, J.2    Kester, M.3
  • 19
    • 33947522817 scopus 로고    scopus 로고
    • Peptides derived from the C2 domain of protein kinase Cε modulate εPKC activity and identify potential protein-protein interaction surfaces
    • Brandman R, Disatnik MH, Churchill E, Mochly-Rosen D. Peptides derived from the C2 domain of protein kinase Cε modulate εPKC activity and identify potential protein-protein interaction surfaces. J Biol Chem 282: 4113-4123, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 4113-4123
    • Brandman, R.1    Disatnik, M.H.2    Churchill, E.3    Mochly-Rosen, D.4
  • 20
    • 14844285356 scopus 로고    scopus 로고
    • Analysis by fluorescence resonance energy transfer of the interaction between ligands and protein kinase Cδ in the intact cell
    • Braun DC, Garfield SH, Blumberg PM. Analysis by fluorescence resonance energy transfer of the interaction between ligands and protein kinase Cδ in the intact cell. J Biol Chem 280: 8164-8171, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 8164-8171
    • Braun, D.C.1    Garfield, S.H.2    Blumberg, P.M.3
  • 21
    • 33644685637 scopus 로고    scopus 로고
    • The role of protein kinase C in cerebral ischemic and reperfusion injury
    • Bright R, Mochly-Rosen D. The role of protein kinase C in cerebral ischemic and reperfusion injury. Stroke 36: 2781-2790, 2005.
    • (2005) Stroke , vol.36 , pp. 2781-2790
    • Bright, R.1    Mochly-Rosen, D.2
  • 22
    • 0037687332 scopus 로고    scopus 로고
    • Phosphorylation or glutamic acid substitution at protein kinase C sites on cardiac troponin I differentially depress myofilament tension and shortening velocity
    • Burkart EM, Sumandea MP, Kobayashi T, Nili M, Martin AF, Homsher E, Solaro RJ. Phosphorylation or glutamic acid substitution at protein kinase C sites on cardiac troponin I differentially depress myofilament tension and shortening velocity. J Biol Chem 278: 11265-11272, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 11265-11272
    • Burkart, E.M.1    Sumandea, M.P.2    Kobayashi, T.3    Nili, M.4    Martin, A.F.5    Homsher, E.6    Solaro, R.J.7
  • 23
    • 0031888577 scopus 로고    scopus 로고
    • Physiological phosphorylation of protein kinase A at Thr-197 is by a protein kinase A kinase
    • Cauthron RD, Carter KB, Liauw S, Steinberg RA. Physiological phosphorylation of protein kinase A at Thr-197 is by a protein kinase A kinase. Mol Cell Biol 18: 1416-1423, 1998.
    • (1998) Mol Cell Biol , vol.18 , pp. 1416-1423
    • Cauthron, R.D.1    Carter, K.B.2    Liauw, S.3    Steinberg, R.A.4
  • 25
    • 16344395930 scopus 로고    scopus 로고
    • 2 in pulmonary endothelium: Involvement of a pertussis toxin sensitive protein
    • 2 in pulmonary endothelium: involvement of a pertussis toxin sensitive protein. Biochemistry 44: 5246-5257, 2005.
    • (2005) Biochemistry , vol.44 , pp. 5246-5257
    • Chakraborti, T.1    Das, S.2    Chakraborti, S.3
  • 28
    • 1042266629 scopus 로고    scopus 로고
    • Centrosomal anchoring of protein kinase CβII by pericentrin controls microtubule organization, spindle function, cytokinesis
    • Chen D, Purohit A, Halilovic E, Doxsey SJ, Newton AC. Centrosomal anchoring of protein kinase CβII by pericentrin controls microtubule organization, spindle function, cytokinesis. J Biol Chem 279: 4829-4839, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 4829-4839
    • Chen, D.1    Purohit, A.2    Halilovic, E.3    Doxsey, S.J.4    Newton, A.C.5
  • 30
    • 38849142607 scopus 로고    scopus 로고
    • A critical role of protein kinase Cδ activation loop phosphorylation in formyl-methionyl- leucyl-phenylalanine-induced phosphorylation of p47phox and rapid activation of nicotinamide adenine dinucleotide phosphate oxidase
    • Cheng N, He R, Tian J, Dinauer MC, Ye RD. A critical role of protein kinase Cδ activation loop phosphorylation in formyl-methionyl- leucyl-phenylalanine-induced phosphorylation of p47phox and rapid activation of nicotinamide adenine dinucleotide phosphate oxidase. J Immunol 179: 7720-7728, 2007.
    • (2007) J Immunol , vol.179 , pp. 7720-7728
    • Cheng, N.1    He, R.2    Tian, J.3    Dinauer, M.C.4    Ye, R.D.5
  • 31
    • 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: 32407-32410, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 32407-32410
    • Cho, W.1
  • 32
    • 34250896107 scopus 로고    scopus 로고
    • Noradrenaline and endothelin activate diacylglycerol kinases in caveolae/rafts of rat mesenteric arteries
    • Clarke CJ, Ohanian V, Ohanian J. Noradrenaline and endothelin activate diacylglycerol kinases in caveolae/rafts of rat mesenteric arteries. Am J Physiol Heart Circ Physiol 292: H2248-H2256, 2007.
    • (2007) Am J Physiol Heart Circ Physiol , vol.292
    • Clarke, C.J.1    Ohanian, V.2    Ohanian, J.3
  • 33
    • 0034775233 scopus 로고    scopus 로고
    • Death by protein kinase C inhibitor
    • Clerk A. Death by protein kinase C inhibitor. J Mol Cell Cardiol 33: 1773-1776, 2001.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 1773-1776
    • Clerk, A.1
  • 36
    • 33750334731 scopus 로고    scopus 로고
    • Diacylglycerol kinase δ regulates protein kinase C and epidermal growth factor receptor signaling
    • Crotty T, Cai J, Sakane F, Taketomi A, Prescott SM, Topham MK. Diacylglycerol kinase δ regulates protein kinase C and epidermal growth factor receptor signaling. Proc Natl Acad Sci USA 103: 15485-15490, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 15485-15490
    • Crotty, T.1    Cai, J.2    Sakane, F.3    Taketomi, A.4    Prescott, S.M.5    Topham, M.K.6
  • 37
    • 0030670399 scopus 로고    scopus 로고
    • The coatomer protein β′-COP, a selective binding protein (RACK) for protein kinase C
    • Csukai M, Chen CH, De Matteis MA, Mochly-Rosen D. The coatomer protein β′-COP, a selective binding protein (RACK) for protein kinase C. J Biol Chem 272: 29200-29206, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 29200-29206
    • Csukai, M.1    Chen, C.H.2    De Matteis, M.A.3    Mochly-Rosen, D.4
  • 38
    • 0030795091 scopus 로고    scopus 로고
    • Caspase-3-mediated cleavage of protein kinase Cθ in induction of apoptosis
    • Datta R, Kojima H, Yoshida K, Kufe D. Caspase-3-mediated cleavage of protein kinase Cθ in induction of apoptosis. J Biol Chem 272: 20317-20320, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 20317-20320
    • Datta, R.1    Kojima, H.2    Yoshida, K.3    Kufe, D.4
  • 39
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies SP, Reddy H, Caivano M, Cohen P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem J 351: 95-105, 2000.
    • (2000) Biochem J , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 40
    • 0030946258 scopus 로고    scopus 로고
    • Regulated binding of the protein kinase C substrate GAP-43 to the V0/C2 region of protein kinase C-δ
    • Dekker LV, Parker PJ. Regulated binding of the protein kinase C substrate GAP-43 to the V0/C2 region of protein kinase C-δ. J Biol Chem 272: 12747-12753, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 12747-12753
    • Dekker, L.V.1    Parker, P.J.2
  • 42
    • 0038107575 scopus 로고    scopus 로고
    • Cutting edge: A chemical genetic system for the analysis of kinases regulating T cell development
    • Denzel A, Hare KJ, Zhang C, Shokat K, Jenkinson EJ, Anderson G, Hayday A. Cutting edge: a chemical genetic system for the analysis of kinases regulating T cell development. J Immunol 171: 519-523, 2003.
    • (2003) J Immunol , vol.171 , pp. 519-523
    • Denzel, A.1    Hare, K.J.2    Zhang, C.3    Shokat, K.4    Jenkinson, E.J.5    Anderson, G.6    Hayday, A.7
  • 43
    • 0037110732 scopus 로고    scopus 로고
    • Nuclear import of PKCδ is required for apoptosis: Identification of a novel nuclear import sequence
    • DeVries TA, Neville MC, Reyland ME. Nuclear import of PKCδ is required for apoptosis: identification of a novel nuclear import sequence. EMBO J 21: 6050-6060, 2002.
    • (2002) EMBO J , vol.21 , pp. 6050-6060
    • DeVries, T.A.1    Neville, M.C.2    Reyland, M.E.3
  • 44
    • 0028289497 scopus 로고
    • Localization of protein kinase C isozymes in cardiac myocytes
    • Disatnik MH, Buraggi G, Mochly-Rosen D. Localization of protein kinase C isozymes in cardiac myocytes. Exp Cell Res 210: 287-297, 1994.
    • (1994) Exp Cell Res , vol.210 , pp. 287-297
    • Disatnik, M.H.1    Buraggi, G.2    Mochly-Rosen, D.3
  • 45
    • 0842302372 scopus 로고    scopus 로고
    • Phosphorylation of serine 262 in the gap junction protein connexin-43 regulates DNA synthesis in cell-cell contact forming cardiomyocytes
    • Doble BW, Dang X, Ping P, Fandrich RR, Nickel BE, Jin Y, Cattini PA, Kardami E. Phosphorylation of serine 262 in the gap junction protein connexin-43 regulates DNA synthesis in cell-cell contact forming cardiomyocytes. J Cell Sci 117: 507-514, 2004.
    • (2004) J Cell Sci , vol.117 , pp. 507-514
    • Doble, B.W.1    Dang, X.2    Ping, P.3    Fandrich, R.R.4    Nickel, B.E.5    Jin, Y.6    Cattini, P.A.7    Kardami, E.8
  • 46
    • 0033621884 scopus 로고    scopus 로고
    • The ε subtype of protein kinase C is required for cardiomyocyte connexin-43 phosphorylation
    • Doble BW, Ping P, Kardami E. The ε subtype of protein kinase C is required for cardiomyocyte connexin-43 phosphorylation. Circ Res 86: 293-301, 2000.
    • (2000) Circ Res , vol.86 , pp. 293-301
    • Doble, B.W.1    Ping, P.2    Kardami, E.3
  • 47
    • 33847746323 scopus 로고    scopus 로고
    • A single residue in the C1 domain sensitizes novel protein kinase C isoforms to cellular diacylglycerol production
    • Dries DR, Gallegos LL, Newton AC. A single residue in the C1 domain sensitizes novel protein kinase C isoforms to cellular diacylglycerol production. J Biol Chem 282: 826-830, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 826-830
    • Dries, D.R.1    Gallegos, L.L.2    Newton, A.C.3
  • 48
    • 0032585532 scopus 로고    scopus 로고
    • Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1
    • Dutil EM, Toker A, Newton AC. Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1. Curr Biol 8: 1366-1375, 1998.
    • (1998) Curr Biol , vol.8 , pp. 1366-1375
    • Dutil, E.M.1    Toker, A.2    Newton, A.C.3
  • 49
    • 0033525860 scopus 로고    scopus 로고
    • Carboxyl-terminal phosphorylation regulates the function and subcellular localization of protein kinase C-βII
    • Edwards AS, Faux MC, Scott JD, Newton AC. Carboxyl-terminal phosphorylation regulates the function and subcellular localization of protein kinase C-βII. J Biol Chem 274: 6461-6468, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 6461-6468
    • Edwards, A.S.1    Faux, M.C.2    Scott, J.D.3    Newton, A.C.4
  • 50
    • 0030875555 scopus 로고    scopus 로고
    • Phosphorylation at conserved carboxylterminal hydrophobic motif regulates the catalytic and regulatory domains of protein kinase C
    • Edwards AS, Newton AC. Phosphorylation at conserved carboxylterminal hydrophobic motif regulates the catalytic and regulatory domains of protein kinase C. J Biol Chem 272: 18382-18390, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 18382-18390
    • Edwards, A.S.1    Newton, A.C.2
  • 51
    • 0031458338 scopus 로고    scopus 로고
    • Regulation of protein kinase C βII by its C2 domain
    • Edwards AS, Newton AC. Regulation of protein kinase C βII by its C2 domain. Biochemistry 36: 15615-15623, 1997.
    • (1997) Biochemistry , vol.36 , pp. 15615-15623
    • Edwards, A.S.1    Newton, A.C.2
  • 53
    • 33845327489 scopus 로고    scopus 로고
    • The gatekeeper residue controls autoactivation of ERK2 via a pathway of intramolecular connectivity
    • Emrick MA, Lee T, Starkey PJ, Mumby MC, Resing KA, Ahn NG. The gatekeeper residue controls autoactivation of ERK2 via a pathway of intramolecular connectivity. Proc Natl Acad Sci USA 103: 18101-18106, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18101-18106
    • Emrick, M.A.1    Lee, T.2    Starkey, P.J.3    Mumby, M.C.4    Resing, K.A.5    Ahn, N.G.6
  • 55
    • 0034595645 scopus 로고    scopus 로고
    • Regulation of receptor-mediated protein kinase C membrane trafficking by autophosphorylation
    • Feng X, Becker KP, Stribling SD, Peters KG, Hannun YA. Regulation of receptor-mediated protein kinase C membrane trafficking by autophosphorylation. J Biol Chem 275: 17024-17034, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 17024-17034
    • Feng, X.1    Becker, K.P.2    Stribling, S.D.3    Peters, K.G.4    Hannun, Y.A.5
  • 56
    • 0032500506 scopus 로고    scopus 로고
    • An essential role for autophosphorylation in the dissociation of activated protein kinase C from the plasma membrane
    • Feng X, Hannun YA. An essential role for autophosphorylation in the dissociation of activated protein kinase C from the plasma membrane. J Biol Chem 273: 26870-26874, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 26870-26874
    • Feng, X.1    Hannun, Y.A.2
  • 58
    • 0033574277 scopus 로고    scopus 로고
    • Cleavage of ζPKC but not λιPKC by caspase-3 during UV-induced apoptos
    • Frutos S, Moscat J, Diaz-Meco MT. Cleavage of ζPKC but not λιPKC by caspase-3 during UV-induced apoptos. J Biol Chem 274: 10765-10770, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 10765-10770
    • Frutos, S.1    Moscat, J.2    Diaz-Meco, M.T.3
  • 59
    • 33750072605 scopus 로고    scopus 로고
    • Targeting protein kinase C activity reporter to discrete intracellular regions reveals spatiotemporal differences in agonist-dependent signaling
    • Gallegos LL, Kunkel MT, Newton AC. Targeting protein kinase C activity reporter to discrete intracellular regions reveals spatiotemporal differences in agonist-dependent signaling. J Biol Chem 281: 30947-30956, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 30947-30956
    • Gallegos, L.L.1    Kunkel, M.T.2    Newton, A.C.3
  • 60
    • 0037200043 scopus 로고    scopus 로고
    • The turn motif is a phosphorylation switch that regulates the binding of Hsp70 to protein kinase C
    • Gao T, Newton AC. The turn motif is a phosphorylation switch that regulates the binding of Hsp70 to protein kinase C. J Biol Chem 277: 31585-31592, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 31585-31592
    • Gao, T.1    Newton, A.C.2
  • 61
    • 33845944580 scopus 로고    scopus 로고
    • Invariant leu preceding turn motif phosphorylation site controls the interaction of protein kinase C with hsp70
    • Gao T, Newton AC. Invariant leu preceding turn motif phosphorylation site controls the interaction of protein kinase C with hsp70. J Biol Chem 281: 32461-32468, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 32461-32468
    • Gao, T.1    Newton, A.C.2
  • 62
    • 0035380478 scopus 로고    scopus 로고
    • The carboxyl terminus of protein kinase C provides a switch to regulate its interaction with the phosphoinositide- dependent kinase, PDK-1
    • Gao T, Toker A, Newton AC. The carboxyl terminus of protein kinase C provides a switch to regulate its interaction with the phosphoinositide- dependent kinase, PDK-1. J Biol Chem 276: 19588-19596, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 19588-19596
    • Gao, T.1    Toker, A.2    Newton, A.C.3
  • 63
    • 0032143922 scopus 로고    scopus 로고
    • The broad specificity of dominant inhibitory protein kinase C mutants infers a common step in phosphorylation
    • Garcia-Paramio P, Cabrerizo Y, Bornancin F, Parker PJ. The broad specificity of dominant inhibitory protein kinase C mutants infers a common step in phosphorylation. Biochem J 333: 631-636, 1998.
    • (1998) Biochem J , vol.333 , pp. 631-636
    • Garcia-Paramio, P.1    Cabrerizo, Y.2    Bornancin, F.3    Parker, P.J.4
  • 64
    • 33644981789 scopus 로고    scopus 로고
    • Increased membrane affinity of the C1 domain of protein kinase Cδ compensates for the lack of involvement of its C2 domain in membrane recruitment
    • Giorgione JR, Lin JH, McCammon JA, Newton AC. Increased membrane affinity of the C1 domain of protein kinase Cδ compensates for the lack of involvement of its C2 domain in membrane recruitment. J Biol Chem 281: 1660-1669, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 1660-1669
    • Giorgione, J.R.1    Lin, J.H.2    McCammon, J.A.3    Newton, A.C.4
  • 65
    • 0032493823 scopus 로고    scopus 로고
    • Mapping of a molecular determinant for protein kinase C-βII isozyme function
    • Gökmen-Polar Y, Fields AP. Mapping of a molecular determinant for protein kinase C-βII isozyme function. J Biol Chem 273: 20261-20266, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 20261-20266
    • Gökmen-Polar, Y.1    Fields, A.P.2
  • 66
    • 0031464009 scopus 로고    scopus 로고
    • The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src
    • Gonfloni S, Williams JC, Hattula K, Weijland A, Wierenga RK, Superti-Furga G. The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src. EMBO J 16: 7261-7271, 1997.
    • (1997) EMBO J , vol.16 , pp. 7261-7271
    • Gonfloni, S.1    Williams, J.C.2    Hattula, K.3    Weijland, A.4    Wierenga, R.K.5    Superti-Furga, G.6
  • 67
    • 0028833510 scopus 로고
    • Protein kinase C (PKC)-induced PKC down-regulation: Association with up-regulation of vesicle traffic
    • Goode NT, Hajibagheri N, Parker PJ. Protein kinase C (PKC)-induced PKC down-regulation: association with up-regulation of vesicle traffic. J Biol Chem 270: 2669-2673, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 2669-2673
    • Goode, N.T.1    Hajibagheri, N.2    Parker, P.J.3
  • 68
    • 0028900634 scopus 로고
    • Immunocytochemical localization of eight protein kinase C isozymes overexpressed in NIH 3T3 fibroblasts. Isoform-specific association with microfilaments, Golgi, endoplasmic reticulum, nuclear and cell membranes
    • Goodnight JA, Mischak H, Kolch W, Mushinski JF. Immunocytochemical localization of eight protein kinase C isozymes overexpressed in NIH 3T3 fibroblasts. Isoform-specific association with microfilaments, Golgi, endoplasmic reticulum, nuclear and cell membranes. J Biol Chem 270: 9991-10001, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 9991-10001
    • Goodnight, J.A.1    Mischak, H.2    Kolch, W.3    Mushinski, J.F.4
  • 69
    • 0034190297 scopus 로고    scopus 로고
    • Protein kinase C signaling and oxidative stress
    • Gopalakrishna R, Jaken S. Protein kinase C signaling and oxidative stress. Free Radic Biol Med 28: 1349-1361, 2000.
    • (2000) Free Radic Biol Med , vol.28 , pp. 1349-1361
    • Gopalakrishna, R.1    Jaken, S.2
  • 70
    • 0942298111 scopus 로고    scopus 로고
    • Preservation of base-line hemodynamic function and loss of inducible cardioprotection in adult mice lacking protein kinase C-ε
    • Gray MO, Zhou HZ, Schafhalter-Zoppoth I, Zhu P, Mochly-Rosen D, Messing RO. Preservation of base-line hemodynamic function and loss of inducible cardioprotection in adult mice lacking protein kinase C-ε. J Biol Chem 279: 3596-3604, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 3596-3604
    • Gray, M.O.1    Zhou, H.Z.2    Schafhalter-Zoppoth, I.3    Zhu, P.4    Mochly-Rosen, D.5    Messing, R.O.6
  • 71
    • 33947603008 scopus 로고    scopus 로고
    • Protein kinase C and other diacylglycerol effectors in cancer
    • Griner EM, Kazanietz MG. Protein kinase C and other diacylglycerol effectors in cancer. Nat Rev Cancer 7: 281-294, 2007.
    • (2007) Nat Rev Cancer , vol.7 , pp. 281-294
    • Griner, E.M.1    Kazanietz, M.G.2
  • 72
    • 33751570046 scopus 로고    scopus 로고
    • Structure of the catalytic domain of human protein kinase C βII complexed with a bisindolylmaleimide inhibitor
    • Grodsky N, Li Y, Bouzida D, Love R, Jensen J, Nodes B, Nonomiya J, Grant S. Structure of the catalytic domain of human protein kinase C βII complexed with a bisindolylmaleimide inhibitor. Biochemistry 45: 13970-13981, 2006.
    • (2006) Biochemistry , vol.45 , pp. 13970-13981
    • Grodsky, N.1    Li, Y.2    Bouzida, D.3    Love, R.4    Jensen, J.5    Nodes, B.6    Nonomiya, J.7    Grant, S.8
  • 74
    • 0030891426 scopus 로고    scopus 로고
    • Importance of the A-helix of the catalytic subunit of cAMP-dependent protein kinase for stability and for orienting subdomains at the cleft interface
    • Herberg FW, Zimmermann B, McGlone M, Taylor SS. Importance of the A-helix of the catalytic subunit of cAMP-dependent protein kinase for stability and for orienting subdomains at the cleft interface. Protein Sci 6: 569-579, 1997.
    • (1997) Protein Sci , vol.6 , pp. 569-579
    • Herberg, F.W.1    Zimmermann, B.2    McGlone, M.3    Taylor, S.S.4
  • 75
    • 0028447767 scopus 로고
    • Solution structure of a cysteine rich domain of rat protein kinase C
    • Hommel U, Zurini M, Luyten M. Solution structure of a cysteine rich domain of rat protein kinase C. Nat Struct Biol 1: 383-387, 1994.
    • (1994) Nat Struct Biol , vol.1 , pp. 383-387
    • Hommel, U.1    Zurini, M.2    Luyten, M.3
  • 76
    • 0037462741 scopus 로고    scopus 로고
    • Mechanisms of regulation of phospholipase D1 by protein kinase Cα
    • Hu T, Exton JH. Mechanisms of regulation of phospholipase D1 by protein kinase Cα. J Biol Chem 278: 2348-2355, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 2348-2355
    • Hu, T.1    Exton, J.H.2
  • 77
    • 4143050486 scopus 로고    scopus 로고
    • Protein kinase Cα translocates to the perinuclear region to activate phospholipase D1
    • Hu T, Exton JH. Protein kinase Cα translocates to the perinuclear region to activate phospholipase D1. J Biol Chem 279: 35702-35708, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 35702-35708
    • Hu, T.1    Exton, J.H.2
  • 78
    • 0033887478 scopus 로고    scopus 로고
    • Signaling and subcellular targeting by membrane-binding domains
    • Hurley JH, Misra S. Signaling and subcellular targeting by membrane-binding domains. Annu Rev Biophys Biomol Struct 29: 49-79, 2000.
    • (2000) Annu Rev Biophys Biomol Struct , vol.29 , pp. 49-79
    • Hurley, J.H.1    Misra, S.2
  • 79
    • 0032514649 scopus 로고    scopus 로고
    • Selective ceramide binding to protein kinase C-α and -δ isoenzymes in renal mesangial cells
    • Huwiler A, Fabbro D, Pfeilschifter J. Selective ceramide binding to protein kinase C-α and -δ isoenzymes in renal mesangial cells. Biochemistry 37: 14556-14562, 1998.
    • (1998) Biochemistry , vol.37 , pp. 14556-14562
    • Huwiler, A.1    Fabbro, D.2    Pfeilschifter, J.3
  • 80
    • 33746822924 scopus 로고    scopus 로고
    • Dynamic sequestration of the recycling compartment by classical protein kinase C
    • Idkowiak-Baldys J, Becker KP, Kitatani K, Hannun YA. Dynamic sequestration of the recycling compartment by classical protein kinase C. J Biol Chem 281: 22321-22331, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 22321-22331
    • Idkowiak-Baldys, J.1    Becker, K.P.2    Kitatani, K.3    Hannun, Y.A.4
  • 81
    • 4744364185 scopus 로고    scopus 로고
    • The plasma membrane translocation of diacylglycerol kinase δ1 is negatively regulated by conventional protein kinase C-dependent phosphorylation at Ser-22 and Ser-26 within the pleckstrin homology domain
    • Imai S, Kai M, Yamada K, Kanoh H, Sakane F. The plasma membrane translocation of diacylglycerol kinase δ1 is negatively regulated by conventional protein kinase C-dependent phosphorylation at Ser-22 and Ser-26 within the pleckstrin homology domain. Biochem J 382: 957-966, 2004.
    • (2004) Biochem J , vol.382 , pp. 957-966
    • Imai, S.1    Kai, M.2    Yamada, K.3    Kanoh, H.4    Sakane, F.5
  • 82
    • 27844444696 scopus 로고    scopus 로고
    • PKCε-mediated phosphorylation of vimentin controls integrin recycling and motility
    • Ivaska J, Vuoriluoto K, Huovinen T, Izawa I, Inagaki M, Parker PJ. PKCε-mediated phosphorylation of vimentin controls integrin recycling and motility. EMBO J 24: 3834-3845, 2005.
    • (2005) EMBO J , vol.24 , pp. 3834-3845
    • Ivaska, J.1    Vuoriluoto, K.2    Huovinen, T.3    Izawa, I.4    Inagaki, M.5    Parker, P.J.6
  • 83
    • 0037099313 scopus 로고    scopus 로고
    • PKC-ε controls the traffic of β1-integrins in motile cells
    • Ivaska J, Whelan RD, Watson R, Parker PJ. PKC-ε controls the traffic of β1-integrins in motile cells. EMBO J 21: 3608-3619, 2002.
    • (2002) EMBO J , vol.21 , pp. 3608-3619
    • Ivaska, J.1    Whelan, R.D.2    Watson, R.3    Parker, P.J.4
  • 84
    • 23644439447 scopus 로고    scopus 로고
    • Catalytic independent functions of a protein kinase as revealed by a kinase-dead mutant: Study of the Lys72His mutant of cAMP-dependent kinase
    • Iyer GH, Garrod S, Woods VL Jr, Taylor SS. Catalytic independent functions of a protein kinase as revealed by a kinase-dead mutant: study of the Lys72His mutant of cAMP-dependent kinase. J Mol Biol 351: 1110-1122, 2005.
    • (2005) J Mol Biol , vol.351 , pp. 1110-1122
    • Iyer, G.H.1    Garrod, S.2    Woods Jr, V.L.3    Taylor, S.S.4
  • 85
    • 15744399873 scopus 로고    scopus 로고
    • Consequences of lysine 72 mutation on the phosphorylation and activation state of cAMP-dependent kinase
    • Iyer GH, Moore MJ, Taylor SS. Consequences of lysine 72 mutation on the phosphorylation and activation state of cAMP-dependent kinase. J Biol Chem 280: 8800-8807, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 8800-8807
    • Iyer, G.H.1    Moore, M.J.2    Taylor, S.S.3
  • 87
    • 0029745535 scopus 로고    scopus 로고
    • A protein kinase C translocation inhibitor as an isozyme-selective antagonist of cardiac function
    • Johnson JA, Gray MO, Chen CH, Mochly-Rosen D. A protein kinase C translocation inhibitor as an isozyme-selective antagonist of cardiac function. J Biol Chem 271: 24962-24966, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 24962-24966
    • Johnson, J.A.1    Gray, M.O.2    Chen, C.H.3    Mochly-Rosen, D.4
  • 88
    • 0344443675 scopus 로고    scopus 로고
    • The simultaneous production of phosphatidic acid and diacylglycerol is essential for the translocation of protein kinase Cε to the plasma membrane in RBL-2H3 cells
    • Jose Lopez-Andreo M, Gomez-Fernandez JC, Corbalan-Garcia S. The simultaneous production of phosphatidic acid and diacylglycerol is essential for the translocation of protein kinase Cε to the plasma membrane in RBL-2H3 cells. Mol Biol Cell 14: 4885-4895, 2003.
    • (2003) Mol Biol Cell , vol.14 , pp. 4885-4895
    • Jose Lopez-Andreo, M.1    Gomez-Fernandez, J.C.2    Corbalan-Garcia, S.3
  • 89
    • 0037023769 scopus 로고    scopus 로고
    • Src family kinases phosphorylate protein kinase C-δ on tyrosine residues and modify the neoplastic phenotype of skin keratinocytes
    • Joseloff E, Cataisson C, Aamodt H, Ocheni H, Blumberg P, Kraker AJ, Yuspa SH. Src family kinases phosphorylate protein kinase C-δ on tyrosine residues and modify the neoplastic phenotype of skin keratinocytes. J Biol Chem 277: 12318-12323, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 12318-12323
    • Joseloff, E.1    Cataisson, C.2    Aamodt, H.3    Ocheni, H.4    Blumberg, P.5    Kraker, A.J.6    Yuspa, S.H.7
  • 90
    • 1842582001 scopus 로고    scopus 로고
    • Ceramide-induced apoptosis by translocation, phosphorylation, activation of protein kinase Cδ in the Golgi complex
    • Kajimoto T, Shirai Y, Sakai N, Yamamoto T, Matsuzaki H, Kikkawa U, Saito N. Ceramide-induced apoptosis by translocation, phosphorylation, activation of protein kinase Cδ in the Golgi complex. J Biol Chem 279: 12668-12676, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 12668-12676
    • Kajimoto, T.1    Shirai, Y.2    Sakai, N.3    Yamamoto, T.4    Matsuzaki, H.5    Kikkawa, U.6    Saito, N.7
  • 91
    • 0037124093 scopus 로고    scopus 로고
    • Importance of C1B domain for lipid messenger-induced targeting of protein kinase C
    • Kashiwagi K, Shirai Y, Kuriyama M, Sakai N, Saito N. Importance of C1B domain for lipid messenger-induced targeting of protein kinase C. J Biol Chem 277: 18037-18045, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 18037-18045
    • Kashiwagi, K.1    Shirai, Y.2    Kuriyama, M.3    Sakai, N.4    Saito, N.5
  • 93
    • 0036209077 scopus 로고    scopus 로고
    • Novel "nonkinase" phorbol ester receptors: The C1 domain connection
    • Kazanietz MG. Novel "nonkinase" phorbol ester receptors: the C1 domain connection. Mol Pharmacol 61: 759-767, 2002.
    • (2002) Mol Pharmacol , vol.61 , pp. 759-767
    • Kazanietz, M.G.1
  • 94
    • 0029615509 scopus 로고
    • Protein kinase C is regulated in vivo by three functionally distinct phosphorylations
    • Keranen LM, Dutil EM, Newton AC. Protein kinase C is regulated in vivo by three functionally distinct phosphorylations. Curr Biol 5: 1394-1403, 1995.
    • (1995) Curr Biol , vol.5 , pp. 1394-1403
    • Keranen, L.M.1    Dutil, E.M.2    Newton, A.C.3
  • 95
    • 0030611049 scopus 로고    scopus 로고
    • 2+ differentially regulates conventional protein kinase Cs′ membrane interaction and activation
    • 2+ differentially regulates conventional protein kinase Cs′ membrane interaction and activation. J Biol Chem 272: 25959-25967, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 25959-25967
    • Keranen, L.M.1    Newton, A.C.2
  • 96
    • 33747372839 scopus 로고    scopus 로고
    • Protein kinase Cδ-annexin V interaction: A required step in δPKC translocation and function
    • Kheifets V, Bright R, Inagaki K, Schechtman D, Mochly-Rosen D. Protein kinase Cδ-annexin V interaction: a required step in δPKC translocation and function. J Biol Chem 281: 23218-23226, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 23218-23226
    • Kheifets, V.1    Bright, R.2    Inagaki, K.3    Schechtman, D.4    Mochly-Rosen, D.5
  • 97
    • 34547122771 scopus 로고    scopus 로고
    • Mechanism of inhibition of sequestration of protein kinase C-α/βII by ceramide: Roles of ceramide-activated protein phosphatases and phosphorylation/ dephosphorylation of protein kinase C-α/β II on threonine 638/641
    • Kitatani K, Idkowiak-Baldys J, Hannun YA. Mechanism of inhibition of sequestration of protein kinase C-α/βII by ceramide: roles of ceramide-activated protein phosphatases and phosphorylation/ dephosphorylation of protein kinase C-α/β II on threonine 638/641. J Biol Chem 282: 20647-20656, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 20647-20656
    • Kitatani, K.1    Idkowiak-Baldys, J.2    Hannun, Y.A.3
  • 101
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton DR, Zheng JH, Ten Eyck LF, Xuong NH, Taylor SS, Sowadski JM. Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253: 414-420, 1991.
    • (1991) Science , vol.253 , pp. 414-420
    • Knighton, D.R.1    Zheng, J.H.2    Ten Eyck, L.F.3    Xuong, N.H.4    Taylor, S.S.5    Sowadski, J.M.6
  • 104
    • 0034634651 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase Cδ on distinct tyrosine residues regulates specific cellular functions
    • Kronfeld I, Kazimirsky G, Lorenzo PS, Garfield SH, Blumberg PM, Brodie C. Phosphorylation of protein kinase Cδ on distinct tyrosine residues regulates specific cellular functions. J Biol Chem 275: 35491-35498, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 35491-35498
    • Kronfeld, I.1    Kazimirsky, G.2    Lorenzo, P.S.3    Garfield, S.H.4    Blumberg, P.M.5    Brodie, C.6
  • 105
    • 0035907396 scopus 로고    scopus 로고
    • Targeting of the c-Abl tyrosine kinase to mitochondria in the necrotic cell death response to oxidative stress
    • Kumar S, Bharti A, Mishra NC, Raina D, Kharbanda S, Saxena S, Kufe D. Targeting of the c-Abl tyrosine kinase to mitochondria in the necrotic cell death response to oxidative stress. J Biol Chem 276: 17281-17285, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 17281-17285
    • Kumar, S.1    Bharti, A.2    Mishra, N.C.3    Raina, D.4    Kharbanda, S.5    Saxena, S.6    Kufe, D.7
  • 106
    • 0032566691 scopus 로고    scopus 로고
    • Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1
    • Le Good JA, Ziegler WH, Parekh DB, Alessi DR, Cohen P, Parker PJ. Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. Science 281: 2042-2045, 1998.
    • (1998) Science , vol.281 , pp. 2042-2045
    • Le Good, J.A.1    Ziegler, W.H.2    Parekh, D.B.3    Alessi, D.R.4    Cohen, P.5    Parker, P.J.6
  • 107
    • 33644858992 scopus 로고    scopus 로고
    • Regulation of p53 by activated protein kinase C-δ during nitric oxide-induced dopaminergic cell death
    • Lee SJ, Kim DC, Choi BH, Ha H, Kim KT. Regulation of p53 by activated protein kinase C-δ during nitric oxide-induced dopaminergic cell death. J Biol Chem 281: 2215-2224, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 2215-2224
    • Lee, S.J.1    Kim, D.C.2    Choi, B.H.3    Ha, H.4    Kim, K.T.5
  • 108
    • 0028986620 scopus 로고
    • Protein kinase C-ε is localized to the Golgi via its zinc-finger domain and modulates Golgi function
    • Lehel C, Olah Z, Jakab G, Anderson WB. Protein kinase C-ε is localized to the Golgi via its zinc-finger domain and modulates Golgi function. Proc Natl Acad Sci USA 92: 1406-1410, 1995.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1406-1410
    • Lehel, C.1    Olah, Z.2    Jakab, G.3    Anderson, W.B.4
  • 109
    • 0034892413 scopus 로고    scopus 로고
    • Rottlerin-independent attenuation of pervanadate-induced tyrosine phosphorylation events by protein kinase C-δ in hemopoietic cells
    • Leitges M, Elis W, Gimborn K, Huber M. Rottlerin-independent attenuation of pervanadate-induced tyrosine phosphorylation events by protein kinase C-δ in hemopoietic cells. Lab Invest 81: 1087-1095, 2001.
    • (2001) Lab Invest , vol.81 , pp. 1087-1095
    • Leitges, M.1    Elis, W.2    Gimborn, K.3    Huber, M.4
  • 112
    • 0030870169 scopus 로고    scopus 로고
    • Identification of serine 643 of protein kinase C-δ as an important autophosphorylation site for its enzymatic activity
    • Li W, Zhang J, Bottaro DP, Pierce JH. Identification of serine 643 of protein kinase C-δ as an important autophosphorylation site for its enzymatic activity. J Biol Chem 272: 24550-24555, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 24550-24555
    • Li, W.1    Zhang, J.2    Bottaro, D.P.3    Pierce, J.H.4
  • 114
    • 34347358526 scopus 로고    scopus 로고
    • Protein kinase C-γ mutations in the C1B domain cause caspase-3-linked apoptosis in lens epithelial cells through gap junctions
    • Lin D, Shanks D, Prakash O, Takemoto DJ. Protein kinase C-γ mutations in the C1B domain cause caspase-3-linked apoptosis in lens epithelial cells through gap junctions. Exp Eye Res 85: 113-122, 2007.
    • (2007) Exp Eye Res , vol.85 , pp. 113-122
    • Lin, D.1    Shanks, D.2    Prakash, O.3    Takemoto, D.J.4
  • 115
    • 17144369501 scopus 로고    scopus 로고
    • Oxidative activation of protein kinase Cγ through the C1 domain. Effects on gap junctions
    • Lin D, Takemoto DJ. Oxidative activation of protein kinase Cγ through the C1 domain. Effects on gap junctions. J Biol Chem 280: 13682-13693, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 13682-13693
    • Lin, D.1    Takemoto, D.J.2
  • 116
    • 0344420042 scopus 로고    scopus 로고
    • Protein kinase Cγ regulation of gap junction activity through caveolin-1-containing lipid rafts
    • Lin D, Zhou J, Zelenka PS, Takemoto DJ. Protein kinase Cγ regulation of gap junction activity through caveolin-1-containing lipid rafts. Invest Ophthalmol Vis Sci 44: 5259-5268, 2003.
    • (2003) Invest Ophthalmol Vis Sci , vol.44 , pp. 5259-5268
    • Lin, D.1    Zhou, J.2    Zelenka, P.S.3    Takemoto, D.J.4
  • 117
    • 34147127371 scopus 로고    scopus 로고
    • Comparison of the PKCα and the PKCε C1b domains: Identification of residues critical for PKCε-mediated neurite induction
    • Ling M, Sunesson L, Larsson C. Comparison of the PKCα and the PKCε C1b domains: identification of residues critical for PKCε-mediated neurite induction. J Mol Biol 368: 951-965, 2007.
    • (2007) J Mol Biol , vol.368 , pp. 951-965
    • Ling, M.1    Sunesson, L.2    Larsson, C.3
  • 118
    • 24044470631 scopus 로고    scopus 로고
    • Identification of conserved amino acids N-terminal of the PKC-ε C1b domain crucial for protein kinase C-ε-mediated induction of neurite outgrowth
    • Ling M, Troller U, Zeidman R, Stensman H, Schultz A, Larsson C. Identification of conserved amino acids N-terminal of the PKC-ε C1b domain crucial for protein kinase C-ε-mediated induction of neurite outgrowth. J Biol Chem 280: 17910-17919, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 17910-17919
    • Ling, M.1    Troller, U.2    Zeidman, R.3    Stensman, H.4    Schultz, A.5    Larsson, C.6
  • 119
    • 33750358316 scopus 로고    scopus 로고
    • Atypical protein kinase C in glucose metabolism
    • Liu XJ, He AB, Chang YS, Fang FD. Atypical protein kinase C in glucose metabolism. Cell Signal 18: 2071-2076, 2006.
    • (2006) Cell Signal , vol.18 , pp. 2071-2076
    • Liu, X.J.1    He, A.B.2    Chang, Y.S.3    Fang, F.D.4
  • 120
    • 33744960493 scopus 로고    scopus 로고
    • Independence of protein kinase C-δ activity from activation loop phosphorylation: Structural basis and altered functions in cells
    • Liu Y, Belkina NV, Graham C, Shaw S. Independence of protein kinase C-δ activity from activation loop phosphorylation: structural basis and altered functions in cells. J Biol Chem 281: 12102-12111, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 12102-12111
    • Liu, Y.1    Belkina, N.V.2    Graham, C.3    Shaw, S.4
  • 121
    • 0037081849 scopus 로고    scopus 로고
    • Phosphorylation of the protein kinase C-θ activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor-B induction
    • Liu Y, Graham C, Li A, Fisher RJ, Shaw S. Phosphorylation of the protein kinase C-θ activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor-B induction. Biochem J 361: 255-265, 2002.
    • (2002) Biochem J , vol.361 , pp. 255-265
    • Liu, Y.1    Graham, C.2    Li, A.3    Fisher, R.J.4    Shaw, S.5
  • 122
    • 0034602963 scopus 로고    scopus 로고
    • Regulation of protein kinase Cθ function during T cell activation by Lck-mediated tyrosine phosphorylation
    • Liu Y, Witte S, Liu YC, Doyle M, Elly C, Altman A. Regulation of protein kinase Cθ function during T cell activation by Lck-mediated tyrosine phosphorylation. J Biol Chem 275: 3603-3609, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 3603-3609
    • Liu, Y.1    Witte, S.2    Liu, Y.C.3    Doyle, M.4    Elly, C.5    Altman, A.6
  • 125
    • 34548425994 scopus 로고    scopus 로고
    • The phosphorylation of tyrosine 332 is necessary for the caspase 3-dependent cleavage of PKCδ and the regulation of cell apoptosis
    • Lu W, Lee HK, Xiang C, Finniss S, Brodie C. The phosphorylation of tyrosine 332 is necessary for the caspase 3-dependent cleavage of PKCδ and the regulation of cell apoptosis. Cell Signal 19: 2165-2173, 2007.
    • (2007) Cell Signal , vol.19 , pp. 2165-2173
    • Lu, W.1    Lee, H.K.2    Xiang, C.3    Finniss, S.4    Brodie, C.5
  • 126
    • 0037451177 scopus 로고    scopus 로고
    • Association of diacylglycerol kinase-ζ with protein kinase C-α: Spatial regulation of diacylglycerol signaling
    • Luo B, Prescott SM, Topham MK. Association of diacylglycerol kinase-ζ with protein kinase C-α: spatial regulation of diacylglycerol signaling. J Cell Biol 160: 929-937, 2003.
    • (2003) J Cell Biol , vol.160 , pp. 929-937
    • Luo, B.1    Prescott, S.M.2    Topham, M.K.3
  • 127
    • 0141994860 scopus 로고    scopus 로고
    • Protein kinase C-α phosphorylates and negatively regulates diacylglycerol kinase-ζ
    • Luo B, Prescott SM, Topham MK. Protein kinase C-α phosphorylates and negatively regulates diacylglycerol kinase-ζ. J Biol Chem 278: 39542-39547, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 39542-39547
    • Luo, B.1    Prescott, S.M.2    Topham, M.K.3
  • 128
    • 0034958672 scopus 로고    scopus 로고
    • Localization, anchoring, functions of protein kinase C isozymes in the heart
    • Mackay K, Mochly-Rosen D. Localization, anchoring, functions of protein kinase C isozymes in the heart. J Mol Cell Cardiol 33: 1301-1307, 2001.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 1301-1307
    • Mackay, K.1    Mochly-Rosen, D.2
  • 129
    • 0035503293 scopus 로고    scopus 로고
    • Recruitment of protein kinase D to the trans-Golgi network via the first cysteine-rich domain
    • Maeda Y, Beznoussenko GV, Van Lint J, Mironov AA, Malhotra V. Recruitment of protein kinase D to the trans-Golgi network via the first cysteine-rich domain. EMBO J 20: 5982-5990, 2001.
    • (2001) EMBO J , vol.20 , pp. 5982-5990
    • Maeda, Y.1    Beznoussenko, G.V.2    Van Lint, J.3    Mironov, A.A.4    Malhotra, V.5
  • 131
    • 0032504259 scopus 로고    scopus 로고
    • 2+ ligands and membrane binding residues
    • 2+ ligands and membrane binding residues. J Biol Chem 273: 17544-17552, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 17544-17552
    • Medkova, M.1    Cho, W.2
  • 132
    • 34547118860 scopus 로고    scopus 로고
    • Mechanism of diacylglycerol-induced membrane targeting and activation of protein kinase Cθ
    • Melowic HR, Stahelin RV, Blatner NR, Tian W, Hayashi K, Altman A, Cho W. Mechanism of diacylglycerol-induced membrane targeting and activation of protein kinase Cθ. J Biol Chem 282: 21467-21476, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 21467-21476
    • Melowic, H.R.1    Stahelin, R.V.2    Blatner, N.R.3    Tian, W.4    Hayashi, K.5    Altman, A.6    Cho, W.7
  • 133
    • 24644488646 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human atypical protein kinase Cι reveals interaction mode of phosphorylation site in turn motif
    • Messerschmidt A, Macieira S, Velarde M, Badeker M, Benda C, Jestel A, Brandstetter H, Neuefeind T, Blaesse M. Crystal structure of the catalytic domain of human atypical protein kinase Cι reveals interaction mode of phosphorylation site in turn motif. J Mol Biol 352: 918-931, 2005.
    • (2005) J Mol Biol , vol.352 , pp. 918-931
    • Messerschmidt, A.1    Macieira, S.2    Velarde, M.3    Badeker, M.4    Benda, C.5    Jestel, A.6    Brandstetter, H.7    Neuefeind, T.8    Blaesse, M.9
  • 135
    • 0030734628 scopus 로고    scopus 로고
    • The proteolytic cleavage of protein kinase C isotypes, which generates kinase and regulatory fragments, correlates with Fas-mediated and 12-O-tetradecanoylphorbol-13-acetate-induced apoptosis
    • Mizuno K, Noda K, Araki T, Imaoka T, Kobayashi Y, Akita Y, Shimonaka M, Kishi S, Ohno S. The proteolytic cleavage of protein kinase C isotypes, which generates kinase and regulatory fragments, correlates with Fas-mediated and 12-O-tetradecanoylphorbol-13-acetate-induced apoptosis. Eur J Biochem 250: 7-18, 1997.
    • (1997) Eur J Biochem , vol.250 , pp. 7-18
    • Mizuno, K.1    Noda, K.2    Araki, T.3    Imaoka, T.4    Kobayashi, Y.5    Akita, Y.6    Shimonaka, M.7    Kishi, S.8    Ohno, S.9
  • 136
    • 0037033032 scopus 로고    scopus 로고
    • Phosphorylation of the catalytic subunit of protein kinase A. Autophosphorylation versus phosphorylation by phosphoinositide-dependent kinase-1
    • Moore MJ, Kanter JR, Jones KC, Taylor SS. Phosphorylation of the catalytic subunit of protein kinase A. Autophosphorylation versus phosphorylation by phosphoinositide-dependent kinase-1. J Biol Chem 277: 47878-47884, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 47878-47884
    • Moore, M.J.1    Kanter, J.R.2    Jones, K.C.3    Taylor, S.S.4
  • 138
    • 33747886310 scopus 로고    scopus 로고
    • Cell signaling and function organized by PB1 domain interactions
    • Moscat J, Diaz-Meco MT, Albert A, Campuzano S. Cell signaling and function organized by PB1 domain interactions. Mol Cell 23: 631-640, 2006.
    • (2006) Mol Cell , vol.23 , pp. 631-640
    • Moscat, J.1    Diaz-Meco, M.T.2    Albert, A.3    Campuzano, S.4
  • 139
    • 33645960166 scopus 로고    scopus 로고
    • PKCζ at the crossroad of NF-κB and Jak1/Stat6 signaling pathways
    • Moscat J, Rennert P, Diaz-Meco MT. PKCζ at the crossroad of NF-κB and Jak1/Stat6 signaling pathways. Cell Death Differ 13: 702-711, 2006.
    • (2006) Cell Death Differ , vol.13 , pp. 702-711
    • Moscat, J.1    Rennert, P.2    Diaz-Meco, M.T.3
  • 140
    • 0029003788 scopus 로고
    • PKC-ζ is a molecular switch in signal transduction of TNF-α, bifunctionally regulated by ceramide and arachidonic acid
    • Muller G, Ayoub M, Storz P, Rennecke J, Fabbro D, Pfizenmaier K. PKC-ζ is a molecular switch in signal transduction of TNF-α, bifunctionally regulated by ceramide and arachidonic acid. EMBO J 14: 1961-1969, 1995.
    • (1995) EMBO J , vol.14 , pp. 1961-1969
    • Muller, G.1    Ayoub, M.2    Storz, P.3    Rennecke, J.4    Fabbro, D.5    Pfizenmaier, K.6
  • 141
    • 0032555778 scopus 로고    scopus 로고
    • Protein kinase C: A paradigm for regulation of protein function by two membrane-targeting modules
    • Newton AC, Johnson JE. Protein kinase C: a paradigm for regulation of protein function by two membrane-targeting modules. Biochim Biophys Acta 1376: 155-172, 1998.
    • (1998) Biochim Biophys Acta , vol.1376 , pp. 155-172
    • Newton, A.C.1    Johnson, J.E.2
  • 143
    • 10644277781 scopus 로고    scopus 로고
    • Inhibition of gap junction activity through the release of the C1B domain of protein kinase Cγ from 14-3-3: Identification of PKCγ-binding sites
    • Nguyen TA, Takemoto LJ, Takemoto DJ. Inhibition of gap junction activity through the release of the C1B domain of protein kinase Cγ from 14-3-3: identification of PKCγ-binding sites. J Biol Chem 279: 52714-52725, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 52714-52725
    • Nguyen, T.A.1    Takemoto, L.J.2    Takemoto, D.J.3
  • 144
    • 0032498538 scopus 로고    scopus 로고
    • Oancea E, Teruel MN, Quest AF, Meyer T. Green fluorescent protein (GFP)-tagged cysteine-rich domains from protein kinase C as fluorescent indicators for diacylglycerol signaling in living cells. J Cell Biol 140: 485-498, 1998.
    • Oancea E, Teruel MN, Quest AF, Meyer T. Green fluorescent protein (GFP)-tagged cysteine-rich domains from protein kinase C as fluorescent indicators for diacylglycerol signaling in living cells. J Cell Biol 140: 485-498, 1998.
  • 146
    • 0031035528 scopus 로고    scopus 로고
    • Chk1 is a wee1 kinase in the G2 DNA damage checkpoint inhibiting cdc2 by Y15 phosphorylation
    • O'Connell MJ, Raleigh JM, Verkade HM, Nurse P. Chk1 is a wee1 kinase in the G2 DNA damage checkpoint inhibiting cdc2 by Y15 phosphorylation. EMBO J 16: 545-554, 1997.
    • (1997) EMBO J , vol.16 , pp. 545-554
    • O'Connell, M.J.1    Raleigh, J.M.2    Verkade, H.M.3    Nurse, P.4
  • 148
    • 0031455589 scopus 로고    scopus 로고
    • Caveolin interaction with protein kinase C: Isoenzyme-dependent regulation of kinase activity by the caveolin scaffolding domain peptide
    • Oka N, Yamamoto M, Schwencke C, Kawabe JI, Ebina T, Ohno S, Couet J, Lisanti MP, Ishikawa Y. Caveolin interaction with protein kinase C: isoenzyme-dependent regulation of kinase activity by the caveolin scaffolding domain peptide. J Biol Chem 272: 33416-33421, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 33416-33421
    • Oka, N.1    Yamamoto, M.2    Schwencke, C.3    Kawabe, J.I.4    Ebina, T.5    Ohno, S.6    Couet, J.7    Lisanti, M.P.8    Ishikawa, Y.9
  • 149
    • 21244479797 scopus 로고    scopus 로고
    • Roles of tyrosine phosphorylation and cleavage of PKCδ in its protective effect against trail-induced apoptosis
    • Okhrimenko H, Lu W, Jiang C, Ju D, Blumberg PM, Gomel R, Kazimirsky G, Brodie C. Roles of tyrosine phosphorylation and cleavage of PKCδ in its protective effect against trail-induced apoptosis. J Biol Chem 280: 23643-23652, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 23643-23652
    • Okhrimenko, H.1    Lu, W.2    Jiang, C.3    Ju, D.4    Blumberg, P.M.5    Gomel, R.6    Kazimirsky, G.7    Brodie, C.8
  • 152
    • 0033520995 scopus 로고    scopus 로고
    • Mammalian TOR controls one of two kinase pathways acting upon nPKCδ and nPKCε
    • Parekh D, Ziegler W, Yonezawa K, Hara K, Parker PJ. Mammalian TOR controls one of two kinase pathways acting upon nPKCδ and nPKCε. J Biol Chem 274: 34758-34764, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 34758-34764
    • Parekh, D.1    Ziegler, W.2    Yonezawa, K.3    Hara, K.4    Parker, P.J.5
  • 153
    • 0034651539 scopus 로고    scopus 로고
    • Multiple pathways control protein kinase C phosphorylation
    • Parekh DB, Ziegler W, Parker PJ. Multiple pathways control protein kinase C phosphorylation. EMBO J 19: 496-503, 2000
    • (2000) EMBO J , vol.19 , pp. 496-503
    • Parekh, D.B.1    Ziegler, W.2    Parker, P.J.3
  • 155
    • 0035918217 scopus 로고    scopus 로고
    • Nuclear import and export signals enable rapid nucleocytoplasmic shuttling of the atypical protein kinase C-λ
    • Perander M, Bjorkoy G, Johansen T. Nuclear import and export signals enable rapid nucleocytoplasmic shuttling of the atypical protein kinase C-λ. J Biol Chem 276: 13015-13024, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 13015-13024
    • Perander, M.1    Bjorkoy, G.2    Johansen, T.3
  • 157
    • 0032500583 scopus 로고    scopus 로고
    • Molecular analysis of the interactions between protein kinase C- and filamentous actin
    • Prekeris R, Hernandez RM, Mayhew MW, White MK, Terrian DM. Molecular analysis of the interactions between protein kinase C- and filamentous actin. J Biol Chem 273: 26790-26798, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 26790-26798
    • Prekeris, R.1    Hernandez, R.M.2    Mayhew, M.W.3    White, M.K.4    Terrian, D.M.5
  • 158
    • 0030042104 scopus 로고    scopus 로고
    • Identification and localization of an actin-binding motif that is unique to the epsilon isoform of protein kinase C and participates in the regulation of synaptic function
    • Prekeris R, Mayhew MW, Cooper JB, Terrian DM. Identification and localization of an actin-binding motif that is unique to the epsilon isoform of protein kinase C and participates in the regulation of synaptic function. J Cell Biol 132: 77-90, 1996.
    • (1996) J Cell Biol , vol.132 , pp. 77-90
    • Prekeris, R.1    Mayhew, M.W.2    Cooper, J.B.3    Terrian, D.M.4
  • 159
    • 0033858056 scopus 로고    scopus 로고
    • Protein kinase Cα actively downregulates through caveolae-dependent traffic to an endosomal compartment
    • Prevostel C, Alice V, Joubert D, Parker PJ. Protein kinase Cα actively downregulates through caveolae-dependent traffic to an endosomal compartment. J Cell Sci 113: 2575-2584, 2000.
    • (2000) J Cell Sci , vol.113 , pp. 2575-2584
    • Prevostel, C.1    Alice, V.2    Joubert, D.3    Parker, P.J.4
  • 160
    • 33845946450 scopus 로고    scopus 로고
    • Effects on ligand interaction and membrane translocation of the positively charged arginine residues situated along the C1 domain binding cleft in the atypical protein kinase C isoforms
    • Pu Y, Peach ML, Garfield SH, Wincovitch S, Marquez VE, Blumberg PM. Effects on ligand interaction and membrane translocation of the positively charged arginine residues situated along the C1 domain binding cleft in the atypical protein kinase C isoforms. J Biol Chem 281: 33773-33788, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 33773-33788
    • Pu, Y.1    Peach, M.L.2    Garfield, S.H.3    Wincovitch, S.4    Marquez, V.E.5    Blumberg, P.M.6
  • 161
    • 0347287088 scopus 로고    scopus 로고
    • Targeting of PKCα and ε in the pituitary: A highly regulated mechanism involving a GD(E)E motif of the V3 region
    • Quittau-Prevostel C, Delaunay N, Collazos A, Vallentin A, Joubert D. Targeting of PKCα and ε in the pituitary: a highly regulated mechanism involving a GD(E)E motif of the V3 region. J Cell Sci 117: 63-72, 2004.
    • (2004) J Cell Sci , vol.117 , pp. 63-72
    • Quittau-Prevostel, C.1    Delaunay, N.2    Collazos, A.3    Vallentin, A.4    Joubert, D.5
  • 162
    • 34247245145 scopus 로고    scopus 로고
    • Activation loop phosphorylation-independent kinase activity of human protein kinase C-ζ
    • Ranganathan S, Wang Y, Kern FG, Qu Z, Li R. Activation loop phosphorylation-independent kinase activity of human protein kinase C-ζ. Proteins 67: 709-719, 2007.
    • (2007) Proteins , vol.67 , pp. 709-719
    • Ranganathan, S.1    Wang, Y.2    Kern, F.G.3    Qu, Z.4    Li, R.5
  • 163
    • 0037072483 scopus 로고    scopus 로고
    • p73β is regulated by protein kinase Cδ catalytic fragment generated in the apoptotic response to DNA damage
    • Ren J, Datta R, Shioya H, Li Y, Oki E, Biedermann V, Bharti A, Kufe D. p73β is regulated by protein kinase Cδ catalytic fragment generated in the apoptotic response to DNA damage. J Biol Chem 277: 33758-33765, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 33758-33765
    • Ren, J.1    Datta, R.2    Shioya, H.3    Li, Y.4    Oki, E.5    Biedermann, V.6    Bharti, A.7    Kufe, D.8
  • 164
    • 22044452299 scopus 로고    scopus 로고
    • Effects of bisindolylmaleimide PKC inhibitors on p90RSK activity in vitro and in adult ventricular myocytes
    • Roberts NA, Haworth RS, Avkiran M. Effects of bisindolylmaleimide PKC inhibitors on p90RSK activity in vitro and in adult ventricular myocytes. Br J Pharmacol 145: 477-489, 2005.
    • (2005) Br J Pharmacol , vol.145 , pp. 477-489
    • Roberts, N.A.1    Haworth, R.S.2    Avkiran, M.3
  • 165
    • 5144230416 scopus 로고    scopus 로고
    • Specificity of action of bisindolylmaleimide protein kinase C inhibitors: Do they inhibit the 70kDa ribosomal S6 kinase in cardiac myocytes?
    • Roberts NA, Marber MS, Avkiran M. Specificity of action of bisindolylmaleimide protein kinase C inhibitors: do they inhibit the 70kDa ribosomal S6 kinase in cardiac myocytes? Biochem Pharmacol 68: 1923-1928, 2004.
    • (2004) Biochem Pharmacol , vol.68 , pp. 1923-1928
    • Roberts, N.A.1    Marber, M.S.2    Avkiran, M.3
  • 167
    • 0028805699 scopus 로고
    • C2 region-derived peptides inhibit translocation and function of β-protein kinase C in vivo
    • Ron D, Luo J, Mochly-Rosen D. C2 region-derived peptides inhibit translocation and function of β-protein kinase C in vivo. J Biol Chem 270: 24180-24187, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 24180-24187
    • Ron, D.1    Luo, J.2    Mochly-Rosen, D.3
  • 168
    • 0028801624 scopus 로고
    • An autoregulatory region in protein kinase C: The pseudoanchoring site
    • Ron D, Mochly-Rosen D. An autoregulatory region in protein kinase C: The pseudoanchoring site. Proc Natl Acad Sci USA 92: 492-496, 1995.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 492-496
    • Ron, D.1    Mochly-Rosen, D.2
  • 169
    • 0036678472 scopus 로고    scopus 로고
    • Clinical resistance to the kinase inhibitor STI-571 in chronic myeloid leukemia by mutation of Tyr-253 in the Abl kinase domain P-loop
    • Roumiantsev S, Shah NP, Gorre ME, Nicoll J, Brasher BB, Sawyers CL, Van Etten RA. Clinical resistance to the kinase inhibitor STI-571 in chronic myeloid leukemia by mutation of Tyr-253 in the Abl kinase domain P-loop. Proc Natl Acad Sci USA 99: 10700-10705, 2002.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 10700-10705
    • Roumiantsev, S.1    Shah, N.P.2    Gorre, M.E.3    Nicoll, J.4    Brasher, B.B.5    Sawyers, C.L.6    Van Etten, R.A.7
  • 170
    • 34548183625 scopus 로고    scopus 로고
    • Protein kinase C and Src control PKCδ activation loop phosphorylation in cardiomyocytes
    • Rybin VO, Guo J, Gertsberg Z, Elouardighi H, Steinberg SF. Protein kinase C and Src control PKCδ activation loop phosphorylation in cardiomyocytes. J Biol Chem 282: 23631-23638, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 23631-23638
    • Rybin, V.O.1    Guo, J.2    Gertsberg, Z.3    Elouardighi, H.4    Steinberg, S.F.5
  • 172
    • 2442498430 scopus 로고    scopus 로고
    • Stimulus-specific differences in protein kinase C-δ localization and activation mechanisms in cardiomyocytes
    • Rybin VO, Guo J, Sabri A, Elouardighi H, Schaefer E, Steinberg SF. Stimulus-specific differences in protein kinase C-δ localization and activation mechanisms in cardiomyocytes. J Biol Chem 279: 19350-19361, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 19350-19361
    • Rybin, V.O.1    Guo, J.2    Sabri, A.3    Elouardighi, H.4    Schaefer, E.5    Steinberg, S.F.6
  • 173
    • 0037687307 scopus 로고    scopus 로고
    • Cross regulation of nPKC isoform function in cardiomyocytes: Role of PKCε in activation loop phosphorylations and PKCδ in hydrophobic motif phosphorylations
    • Rybin VO, Sabri A, Short J, Braz JC, Molkentin JD, Steinberg SF. Cross regulation of nPKC isoform function in cardiomyocytes: role of PKCε in activation loop phosphorylations and PKCδ in hydrophobic motif phosphorylations. J Biol Chem 278: 14555-14564, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 14555-14564
    • Rybin, V.O.1    Sabri, A.2    Short, J.3    Braz, J.C.4    Molkentin, J.D.5    Steinberg, S.F.6
  • 174
    • 33645460047 scopus 로고    scopus 로고
    • Immunoblotting PKCδ: A cautionary note from the bench
    • Rybin VO, Steinberg SF. Immunoblotting PKCδ: a cautionary note from the bench. Am J Physiol Cell Physiol 290: C750-C756, 2006.
    • (2006) Am J Physiol Cell Physiol , vol.290
    • Rybin, V.O.1    Steinberg, S.F.2
  • 175
    • 0033553417 scopus 로고    scopus 로고
    • Activated protein kinase C isoforms target to cardiomyocyte caveolae
    • Rybin VO, Xu X, Steinberg SF. Activated protein kinase C isoforms target to cardiomyocyte caveolae. Circ Res 84: 980-988, 1999.
    • (1999) Circ Res , vol.84 , pp. 980-988
    • Rybin, V.O.1    Xu, X.2    Steinberg, S.F.3
  • 176
    • 0141616595 scopus 로고    scopus 로고
    • Protein kinase C isoform-selective signals that lead to cardiac hypertrophy and the progression of heart failure
    • Sabri A, Steinberg SF. Protein kinase C isoform-selective signals that lead to cardiac hypertrophy and the progression of heart failure. Mol Cell Biochem 251: 97-101, 2003.
    • (2003) Mol Cell Biochem , vol.251 , pp. 97-101
    • Sabri, A.1    Steinberg, S.F.2
  • 177
    • 0034820345 scopus 로고    scopus 로고
    • Novel protein kinase C delta isoform insensitive to caspase-3
    • Sakurai Y, Onishi Y, Tanimoto Y, Kizaki H. Novel protein kinase C delta isoform insensitive to caspase-3. Biol Pharm Bull 24: 973-977, 2001.
    • (2001) Biol Pharm Bull , vol.24 , pp. 973-977
    • Sakurai, Y.1    Onishi, Y.2    Tanimoto, Y.3    Kizaki, H.4
  • 179
    • 34447540362 scopus 로고    scopus 로고
    • Identification of ChChd3 as a novel substrate of the cAMP-dependent protein kinase (PKA) using an analog-sensitive catalytic subunit
    • Schauble S, King CC, Darshi M, Koller A, Shah K, Taylor SS. Identification of ChChd3 as a novel substrate of the cAMP-dependent protein kinase (PKA) using an analog-sensitive catalytic subunit. J Biol Chem 282: 14952-14959, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 14952-14959
    • Schauble, S.1    King, C.C.2    Darshi, M.3    Koller, A.4    Shah, K.5    Taylor, S.S.6
  • 181
    • 0035474310 scopus 로고    scopus 로고
    • Adaptor proteins in protein kinase C-mediated signal transduction
    • Schechtman D, Mochly-Rosen D. Adaptor proteins in protein kinase C-mediated signal transduction. Oncogene 20: 6339-6347, 2001.
    • (2001) Oncogene , vol.20 , pp. 6339-6347
    • Schechtman, D.1    Mochly-Rosen, D.2
  • 182
    • 0037636466 scopus 로고    scopus 로고
    • The regulatory domain of protein kinase Cθ localises to the Golgi complex and induces apoptosis in neuroblastoma and Jurkat cells
    • Schultz A, Jonsson JI, Larsson C. The regulatory domain of protein kinase Cθ localises to the Golgi complex and induces apoptosis in neuroblastoma and Jurkat cells. Cell Death Differ 10: 662-675, 2003.
    • (2003) Cell Death Differ , vol.10 , pp. 662-675
    • Schultz, A.1    Jonsson, J.I.2    Larsson, C.3
  • 183
    • 3843145099 scopus 로고    scopus 로고
    • Identification of an amino acid residue in the protein kinase C C1b domain crucial for its localization to the Golgi network
    • Schultz A, Ling M, Larsson C. Identification of an amino acid residue in the protein kinase C C1b domain crucial for its localization to the Golgi network. J Biol Chem 279: 31750-31760, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 31750-31760
    • Schultz, A.1    Ling, M.2    Larsson, C.3
  • 184
    • 1542353445 scopus 로고    scopus 로고
    • A chemical genetic approach for the identification of direct substrates of protein kinases
    • Shah K, Shokat KM. A chemical genetic approach for the identification of direct substrates of protein kinases. Methods Mol Biol 233: 253-271, 2003.
    • (2003) Methods Mol Biol , vol.233 , pp. 253-271
    • Shah, K.1    Shokat, K.M.2
  • 185
    • 0029671455 scopus 로고    scopus 로고
    • Regulation of phospholipase D by protein kinase C is synergistic with ADP-ribosylation factor and independent of protein kinase activity
    • Singer WD, Brown HA, Jiang X, Sternweis PC. Regulation of phospholipase D by protein kinase C is synergistic with ADP-ribosylation factor and independent of protein kinase activity. J Biol Chem 271: 4504-4510, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 4504-4510
    • Singer, W.D.1    Brown, H.A.2    Jiang, X.3    Sternweis, P.C.4
  • 188
    • 0037195932 scopus 로고    scopus 로고
    • Lack of constitutive activity of the free kinase domain of protein kinase C-ζ. Dependence on transphosphorylation of the activation loop
    • Smith L, Smith JB. Lack of constitutive activity of the free kinase domain of protein kinase C-ζ. Dependence on transphosphorylation of the activation loop. J Biol Chem 277: 45866-45873, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 45866-45873
    • Smith, L.1    Smith, J.B.2
  • 189
    • 0035851112 scopus 로고    scopus 로고
    • Rottlerin is a mitochondrial uncoupler that decreases cellular ATP levels and indirectly blocks PKCδ tyrosine phosphorylation
    • Soltoff SP. Rottlerin is a mitochondrial uncoupler that decreases cellular ATP levels and indirectly blocks PKCδ tyrosine phosphorylation. J Biol Chem 276: 37986-37992, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 37986-37992
    • Soltoff, S.P.1
  • 190
    • 34548511124 scopus 로고    scopus 로고
    • Rottlerin: An inappropriate and ineffective inhibitor of PKCδ
    • Soltoff SP. Rottlerin: an inappropriate and ineffective inhibitor of PKCδ. Trends Pharmacol Sci 28: 453-458, 2007.
    • (2007) Trends Pharmacol Sci , vol.28 , pp. 453-458
    • Soltoff, S.P.1
  • 191
    • 0032474741 scopus 로고    scopus 로고
    • Tyrosine phosphorylation-dependent and -independent associations of protein kinase C-δ with Src family kinases in the RBL-2H3 mast cell line
    • Song JS, Swann PG, Szallasi Z, Blank U, Blumberg PM, Rivera J. Tyrosine phosphorylation-dependent and -independent associations of protein kinase C-δ with Src family kinases in the RBL-2H3 mast cell line. Oncogene 16: 3357-3368, 1998.
    • (1998) Oncogene , vol.16 , pp. 3357-3368
    • Song, J.S.1    Swann, P.G.2    Szallasi, Z.3    Blank, U.4    Blumberg, P.M.5    Rivera, J.6
  • 192
    • 0035976977 scopus 로고    scopus 로고
    • The phosphoinositidedependent kinase, PDK-1, phosphorylates conventional protein kinase C isozymes by a mechanism that is independent of phosphoinositide 3-kinase
    • Sonnenburg ED, Gao T, Newton AC. The phosphoinositidedependent kinase, PDK-1, phosphorylates conventional protein kinase C isozymes by a mechanism that is independent of phosphoinositide 3-kinase. J Biol Chem 276: 45289-45297, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 45289-45297
    • Sonnenburg, E.D.1    Gao, T.2    Newton, A.C.3
  • 194
    • 0034721863 scopus 로고    scopus 로고
    • Unique structural and functional properties of the ATP-binding domain of atypical protein kinase C-ι
    • Spitaler M, Villunger A, Grunicke H, Uberall F. Unique structural and functional properties of the ATP-binding domain of atypical protein kinase C-ι. J Biol Chem 275: 33289-33296, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 33289-33296
    • Spitaler, M.1    Villunger, A.2    Grunicke, H.3    Uberall, F.4
  • 195
    • 21244504606 scopus 로고    scopus 로고
    • Diacylglycerol-induced membrane targeting and activation of protein kinase Cε: Mechanistic differences between protein kinases Cδ and Cε
    • Stahelin RV, Digman MA, Medkova M, Ananthanarayanan B, Melowic HR, Rafter JD, Cho W. Diacylglycerol-induced membrane targeting and activation of protein kinase Cε: mechanistic differences between protein kinases Cδ and Cε. J Biol Chem 280: 19784-19793, 2005.
    • (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
  • 199
    • 0028898641 scopus 로고
    • PICK1: A perinuclear binding protein and substrate for protein kinase C isolated by the yeast two-hybrid system
    • Staudinger J, Zhou J, Burgess R, Elledge SJ, Olson EN. PICK1: a perinuclear binding protein and substrate for protein kinase C isolated by the yeast two-hybrid system. J Cell Biol 128: 263-271, 1995.
    • (1995) J Cell Biol , vol.128 , pp. 263-271
    • Staudinger, J.1    Zhou, J.2    Burgess, R.3    Elledge, S.J.4    Olson, E.N.5
  • 200
    • 0035839578 scopus 로고    scopus 로고
    • Binding specificity for RACK1 resides in the V5 region of βII protein kinase C
    • Stebbins EG, Mochly-Rosen D. Binding specificity for RACK1 resides in the V5 region of βII protein kinase C. J Biol Chem 276: 29644-29650, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 29644-29650
    • Stebbins, E.G.1    Mochly-Rosen, D.2
  • 201
    • 10944238407 scopus 로고    scopus 로고
    • Distinctive activation mechanisms and functions for protein kinase C-δ
    • Steinberg SF. Distinctive activation mechanisms and functions for protein kinase C-δ. Biochem J 384: 449-459, 2004.
    • (2004) Biochem J , vol.384 , pp. 449-459
    • Steinberg, S.F.1
  • 202
    • 17644380302 scopus 로고    scopus 로고
    • Cardiac hypertrophy served with protein kinase C-ε: δ isoform substitution available at additional cost
    • Steinberg SF, Sussman MA. Cardiac hypertrophy served with protein kinase C-ε: δ isoform substitution available at additional cost. Circ Res 96: 711-713, 2005.
    • (2005) Circ Res , vol.96 , pp. 711-713
    • Steinberg, S.F.1    Sussman, M.A.2
  • 203
    • 0030894024 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase Cδ at threonine 505 is not a prerequisite for enzymatic activity
    • Stempka L, Girod A, Muller HJ, Rincke G, Marks F, Gschwendt M, Bossemeyer D. Phosphorylation of protein kinase Cδ at threonine 505 is not a prerequisite for enzymatic activity. J Biol Chem 272: 6805-6811, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 6805-6811
    • Stempka, L.1    Girod, A.2    Muller, H.J.3    Rincke, G.4    Marks, F.5    Gschwendt, M.6    Bossemeyer, D.7
  • 204
    • 0344141205 scopus 로고    scopus 로고
    • Requirements of protein kinase C δ for catalytic function. Role of glutamic acid 500 and autophosphorylation on serine 643
    • Stempka L, Schnolzer M, Radke S, Rincke G, Marks F, Gschwendt M. Requirements of protein kinase C δ for catalytic function. Role of glutamic acid 500 and autophosphorylation on serine 643. J Biol Chem 274: 8886-8892, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 8886-8892
    • Stempka, L.1    Schnolzer, M.2    Radke, S.3    Rincke, G.4    Marks, F.5    Gschwendt, M.6
  • 205
    • 4644326204 scopus 로고    scopus 로고
    • Autophosphorylation suppresses whereas kinase inhibition augments the translocation of protein kinase Cα in response to diacylglycerol
    • Stensman H, Raghunath A, Larsson C. Autophosphorylation suppresses whereas kinase inhibition augments the translocation of protein kinase Cα in response to diacylglycerol. J Biol Chem 279: 40576-40583, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 40576-40583
    • Stensman, H.1    Raghunath, A.2    Larsson, C.3
  • 206
    • 57149083803 scopus 로고    scopus 로고
    • Sumandea M, Rybin VO, Wang C, Hinken A, Kobayashi T, Harleton E, Sievert G, Feinmark SJ, Balke CW, Solaro RJ, Steinberg SF. Tyrosine phosphorylation modifies PKCδ phosphorylation of cardiac troponin I. Mol Cell. In press.
    • Sumandea M, Rybin VO, Wang C, Hinken A, Kobayashi T, Harleton E, Sievert G, Feinmark SJ, Balke CW, Solaro RJ, Steinberg SF. Tyrosine phosphorylation modifies PKCδ phosphorylation of cardiac troponin I. Mol Cell. In press.
  • 207
    • 0034677930 scopus 로고    scopus 로고
    • Interaction between protein kinase Cδ and the c-Abl tyrosine kinase in the cellular response to oxidative stress
    • Sun X, Wu F, Datta R, Kharbanda S, Kufe D. Interaction between protein kinase Cδ and the c-Abl tyrosine kinase in the cellular response to oxidative stress. J Biol Chem 275: 7470-7473, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 7470-7473
    • Sun, X.1    Wu, F.2    Datta, R.3    Kharbanda, S.4    Kufe, D.5
  • 211
    • 0020404981 scopus 로고
    • Activation of the T24 bladder carcinoma transforming gene is linked to a single amino acid change
    • Taparowsky E, Suard Y, Fasano O, Shimizu K, Goldfarb M, Wigler M. Activation of the T24 bladder carcinoma transforming gene is linked to a single amino acid change. Nature 300: 762-765, 1982.
    • (1982) Nature , vol.300 , pp. 762-765
    • Taparowsky, E.1    Suard, Y.2    Fasano, O.3    Shimizu, K.4    Goldfarb, M.5    Wigler, M.6
  • 213
    • 0035032583 scopus 로고    scopus 로고
    • A single point mutation in the V3 region affects protein kinase Cα targeting and accumulation at cell-cell contacts
    • Vallentin A, Lo TC, Joubert D. A single point mutation in the V3 region affects protein kinase Cα targeting and accumulation at cell-cell contacts. Mol Cell Biol 21: 3351-3363, 2001.
    • (2001) Mol Cell Biol , vol.21 , pp. 3351-3363
    • Vallentin, A.1    Lo, T.C.2    Joubert, D.3
  • 217
    • 0037780971 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C
    • Violin JD, Zhang J, Tsien RY, Newton AC. A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C. J Cell Biol 161: 899-909, 2003.
    • (2003) J Cell Biol , vol.161 , pp. 899-909
    • Violin, J.D.1    Zhang, J.2    Tsien, R.Y.3    Newton, A.C.4
  • 218
    • 0034697324 scopus 로고    scopus 로고
    • The lipophilicity of phorbol esters as a critical factor in determining the pattern of translocation of protein kinase C delta fused to green fluorescent protein
    • Wang QJ, Fang TW, Fenick D, Garfield S, Bienfait B, Marquez VE, Blumberg PM. The lipophilicity of phorbol esters as a critical factor in determining the pattern of translocation of protein kinase C delta fused to green fluorescent protein. J Biol Chem 275: 12136-12146, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 12136-12146
    • Wang, Q.J.1    Fang, T.W.2    Fenick, D.3    Garfield, S.4    Bienfait, B.5    Marquez, V.E.6    Blumberg, P.M.7
  • 220
    • 0035669720 scopus 로고    scopus 로고
    • Protein kinase C and the development of diabetic vascular complications
    • Way KJ, Katai N, King GL. Protein kinase C and the development of diabetic vascular complications. Diabetes Med 18: 945-959, 2001.
    • (2001) Diabetes Med , vol.18 , pp. 945-959
    • Way, K.J.1    Katai, N.2    King, G.L.3
  • 221
    • 0036200364 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 256 facilitates nuclear import of atypical protein kinase C
    • White WO, Seibenhener ML, Wooten MW. Phosphorylation of tyrosine 256 facilitates nuclear import of atypical protein kinase C. J Cell Biochem 85: 42-53, 2002.
    • (2002) J Cell Biochem , vol.85 , pp. 42-53
    • White, W.O.1    Seibenhener, M.L.2    Wooten, M.W.3
  • 222
    • 0034176579 scopus 로고    scopus 로고
    • The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells
    • Williams MR, Arthur JS, Balendran A, van der KJ, Poli V, Cohen P, Alessi DR. The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells. Curr Biol 10: 439-448, 2000.
    • (2000) Curr Biol , vol.10 , pp. 439-448
    • Williams, M.R.1    Arthur, J.S.2    Balendran, A.3    van der, K.J.4    Poli, V.5    Cohen, P.6    Alessi, D.R.7
  • 223
    • 0023091019 scopus 로고
    • Elevated levels of diacylglycerol and decreased phorbol ester sensitivity in ras-transformed fibroblasts
    • Wolfman A, Macara IG. Elevated levels of diacylglycerol and decreased phorbol ester sensitivity in ras-transformed fibroblasts. Nature 325: 359-361, 1987.
    • (1987) Nature , vol.325 , pp. 359-361
    • Wolfman, A.1    Macara, I.G.2
  • 224
    • 0035193041 scopus 로고    scopus 로고
    • Nerve growth factor stimulates multisite tyrosine phosphorylation and activation of the atypical protein kinase C's via a src kinase pathway
    • Wooten MW, Vandenplas ML, Seibenhener ML, Geetha T, Diaz-Meco MT. Nerve growth factor stimulates multisite tyrosine phosphorylation and activation of the atypical protein kinase C's via a src kinase pathway. Mol Cell Biol 21: 8414-8427, 2001.
    • (2001) Mol Cell Biol , vol.21 , pp. 8414-8427
    • Wooten, M.W.1    Vandenplas, M.L.2    Seibenhener, M.L.3    Geetha, T.4    Diaz-Meco, M.T.5
  • 225
    • 0030764306 scopus 로고    scopus 로고
    • NMR structure of a protein kinase C-γ phorbol-binding domain and study of protein-lipid micelle interactions
    • Xu RX, Pawelczyk T, Xia TH, Brown SC. NMR structure of a protein kinase C-γ phorbol-binding domain and study of protein-lipid micelle interactions. Biochemistry 36: 10709-10717, 1997.
    • (1997) Biochemistry , vol.36 , pp. 10709-10717
    • Xu, R.X.1    Pawelczyk, T.2    Xia, T.H.3    Brown, S.C.4
  • 229
    • 0034776026 scopus 로고    scopus 로고
    • Chelerythrine rapidly induces apoptosis through generation of reactive oxygen species in cardiac myocytes
    • Yamamoto S, Seta K, Morisco C, Vatner SF, Sadoshima J. Chelerythrine rapidly induces apoptosis through generation of reactive oxygen species in cardiac myocytes. J Mol Cell Cardiol 33: 1829-1848, 2001.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 1829-1848
    • Yamamoto, S.1    Seta, K.2    Morisco, C.3    Vatner, S.F.4    Sadoshima, J.5
  • 230
    • 33750433553 scopus 로고    scopus 로고
    • Schmidt AM. Protein kinase C-β/early growth response-1 pathway: A key player in ischemia, atherosclerosis, restenosis
    • Yan SF, Harja E, Andrassy M, Fujita T, Schmidt AM. Protein kinase C-β/early growth response-1 pathway: a key player in ischemia, atherosclerosis, restenosis. J Am Coll Cardiol 48: A47-A55, 2006.
    • (2006) J Am Coll Cardiol , vol.48
    • Yan, S.F.1    Harja, E.2    Andrassy, M.3    Fujita, T.4
  • 231
    • 0036295728 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation
    • Yang J, Cron P, Thompson V, Good VM, Hess D, Hemmings BA, Barford D. Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation. Mol Cell 9: 1227-1240, 2002.
    • (2002) Mol Cell , vol.9 , pp. 1227-1240
    • Yang, J.1    Cron, P.2    Thompson, V.3    Good, V.M.4    Hess, D.5    Hemmings, B.A.6    Barford, D.7
  • 232
    • 12344334691 scopus 로고    scopus 로고
    • Allosteric network of cAMP-dependent protein kinase revealed by mutation of Tyr204 in the P+1 loop
    • Yang J, Garrod SM, Deal MS, Anand GS, Woods VL Jr, Taylor S. Allosteric network of cAMP-dependent protein kinase revealed by mutation of Tyr204 in the P+1 loop. J Mol Biol 346: 191-201, 2005.
    • (2005) J Mol Biol , vol.346 , pp. 191-201
    • Yang, J.1    Garrod, S.M.2    Deal, M.S.3    Anand, G.S.4    Woods Jr, V.L.5    Taylor, S.6
  • 234
    • 0038237433 scopus 로고    scopus 로고
    • Protein kinase Cδ is responsible for constitutive and DNA damage-induced phosphorylation of Rad9
    • Yoshida K, Wang HG, Miki Y, Kufe D. Protein kinase Cδ is responsible for constitutive and DNA damage-induced phosphorylation of Rad9. EMBO J 22: 1431-1441, 2003.
    • (2003) EMBO J , vol.22 , pp. 1431-1441
    • Yoshida, K.1    Wang, H.G.2    Miki, Y.3    Kufe, D.4
  • 235
    • 34249657837 scopus 로고    scopus 로고
    • Activation of acid sphingomyelinase by protein kinase Cδ-mediated phosphorylation
    • Zeidan YH, Hannun YA. Activation of acid sphingomyelinase by protein kinase Cδ-mediated phosphorylation. J Biol Chem 282: 11549-11561, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 11549-11561
    • Zeidan, Y.H.1    Hannun, Y.A.2
  • 236
    • 0033577576 scopus 로고    scopus 로고
    • PKCε, via its regulatory domain and independently of its catalytic domain, induces neurite-like processes in neuroblastoma cells
    • Zeidman R, Lofgren B, Pahlman S, Larsson C. PKCε, via its regulatory domain and independently of its catalytic domain, induces neurite-like processes in neuroblastoma cells. J Cell Biol 145: 713-726, 1999.
    • (1999) J Cell Biol , vol.145 , pp. 713-726
    • Zeidman, R.1    Lofgren, B.2    Pahlman, S.3    Larsson, C.4
  • 237
    • 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: 917-924, 1995.
    • (1995) Cell , vol.81 , pp. 917-924
    • Zhang, G.1    Kazanietz, M.G.2    Blumberg, P.M.3    Hurley, J.H.4
  • 238
    • 32144437233 scopus 로고    scopus 로고
    • The very C-terminus of protein kinase Cε is critical for the full catalytic competence but its hydrophobic motif is dispensable for the interaction with 3-phosphoinositide-dependent kinase-1
    • Zhu Y, Smith D, Verma C, Lim WG, Tan BJ, Armstrong JS, Zhou S, Chan E, Tan SL, Zhu YZ, Cheung NS, Duan W. The very C-terminus of protein kinase Cε is critical for the full catalytic competence but its hydrophobic motif is dispensable for the interaction with 3-phosphoinositide-dependent kinase-1. Cell Signal 18: 807-818, 2006.
    • (2006) Cell Signal , vol.18 , pp. 807-818
    • Zhu, Y.1    Smith, D.2    Verma, C.3    Lim, W.G.4    Tan, B.J.5    Armstrong, J.S.6    Zhou, S.7    Chan, E.8    Tan, S.L.9    Zhu, Y.Z.10    Cheung, N.S.11    Duan, W.12


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.