메뉴 건너뛰기




Volumn 21, Issue 11, 2007, Pages 2637-2650

Direct binding and activation of protein kinase C isoforms by aldosterone and 17β-estradiol

Author keywords

[No Author keywords available]

Indexed keywords

ALDOSTERONE; ESTRADIOL; GLUTATHIONE TRANSFERASE; ISOPROTEIN; PHORBOL DIBUTYRATE; PROTEIN KINASE C; PROTEIN KINASE C ALPHA; PROTEIN KINASE C GAMMA;

EID: 35648946319     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2006-0559     Document Type: Article
Times cited : (41)

References (48)
  • 1
    • 0023052241 scopus 로고
    • Studies and perspectives of protein kinase C
    • Nishizuka Y 1986 Studies and perspectives of protein kinase C. Science 233:305-312
    • (1986) Science , vol.233 , pp. 305-312
    • Nishizuka, Y.1
  • 2
    • 0023764824 scopus 로고
    • The molecular heterogeneity of protein kinase C and its implications for cellular regulation
    • Nishizuka Y 1988 The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature 334:661-665
    • (1988) Nature , vol.334 , pp. 661-665
    • Nishizuka, Y.1
  • 3
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • Nishizuka Y 1995 Protein kinase C and lipid signaling for sustained cellular responses. FASEB J 9:484-496
    • (1995) FASEB J , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 4
    • 0023814294 scopus 로고
    • The heterogeneity and differential expression of multiple species of the protein kinase C family
    • Nishizuka Y 1988 The heterogeneity and differential expression of multiple species of the protein kinase C family. Biofactors 1:17-20
    • (1988) Biofactors , vol.1 , pp. 17-20
    • Nishizuka, Y.1
  • 5
    • 0030987070 scopus 로고    scopus 로고
    • Regulation of protein kinase C
    • Newton AC 1997 Regulation of protein kinase C. Curr Opin Cell Biol 9:161-167
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 161-167
    • Newton, A.C.1
  • 6
    • 0025270739 scopus 로고
    • Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C
    • Perin MS, Fried VA, Mignery GA, Jahn R, Sudhof TC 1990 Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C. Nature 345:260-263
    • (1990) Nature , vol.345 , pp. 260-263
    • Perin, M.S.1    Fried, V.A.2    Mignery, G.A.3    Jahn, R.4    Sudhof, T.C.5
  • 7
    • 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 1995 C2 region-derived peptides inhibit translocation and function of β protein kinase C in vivo. J Biol Chem 270:24180-24187
    • (1995) J Biol Chem , vol.270 , pp. 24180-24187
    • Ron, D.1    Luo, J.2    Mochly-Rosen, D.3
  • 8
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function, and regulation
    • Newton AC 1995 Protein kinase C: structure, function, and regulation. J Biol Chem 270:28495-28498
    • (1995) J Biol Chem , vol.270 , pp. 28495-28498
    • Newton, A.C.1
  • 9
    • 0028938152 scopus 로고
    • Localization of protein kinases by anchoring proteins: A theme in signal transduction
    • Mochly-Rosen D 1995 Localization of protein kinases by anchoring proteins: a theme in signal transduction. Science 268:247-251
    • (1995) Science , vol.268 , pp. 247-251
    • Mochly-Rosen, D.1
  • 10
    • 0027292678 scopus 로고
    • Phorbol ester-induced myeloid differentiation is mediated by protein kinase C-α and -δ and not by protein kinase C-βII, -ε, -ζ, and -η
    • Mischak H, Pierce JH, Goodnight J, Kazanietz MG, Blumberg PM, Mushinski JF 1993 Phorbol ester-induced myeloid differentiation is mediated by protein kinase C-α and -δ and not by protein kinase C-βII, -ε, -ζ, and -η. J Biol Chem 268:20110-20115
    • (1993) J Biol Chem , vol.268 , pp. 20110-20115
    • Mischak, H.1    Pierce, J.H.2    Goodnight, J.3    Kazanietz, M.G.4    Blumberg, P.M.5    Mushinski, J.F.6
  • 11
    • 0034957480 scopus 로고    scopus 로고
    • Nuclear hormone receptors and expression
    • Aranda A, Pascual A 2001 Nuclear hormone receptors and expression. Physiol Rev 81:1269-1304
    • (2001) Physiol Rev , vol.81 , pp. 1269-1304
    • Aranda, A.1    Pascual, A.2
  • 12
    • 15744393640 scopus 로고    scopus 로고
    • Regulation of signal transduction pathways by estrogen and progesterone
    • Edwards DP 2005 Regulation of signal transduction pathways by estrogen and progesterone. Annu Rev Physiol 67:337-376
    • (2005) Annu Rev Physiol , vol.67 , pp. 337-376
    • Edwards, D.P.1
  • 14
    • 0345874610 scopus 로고    scopus 로고
    • Steroid-hormone rapid actions, membrane receptors and a conformational ensemble model
    • Norman AW, Mizwicki MT, Norman DPG 2004 Steroid-hormone rapid actions, membrane receptors and a conformational ensemble model. Nat Rev Drug Discov 3:27-41
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 27-41
    • Norman, A.W.1    Mizwicki, M.T.2    Norman, D.P.G.3
  • 15
    • 23744447497 scopus 로고    scopus 로고
    • Integration of the extra-nuclear and nuclear actions of estrogen
    • Levin ER 2005 Integration of the extra-nuclear and nuclear actions of estrogen. Mol Endocrinol 19:1951-1959
    • (2005) Mol Endocrinol , vol.19 , pp. 1951-1959
    • Levin, E.R.1
  • 16
  • 17
    • 33747841976 scopus 로고    scopus 로고
    • Nature of functional estrogen receptors at the plasma membrane
    • Pedram A, Razandi M, Levin ER 2006 Nature of functional estrogen receptors at the plasma membrane. Mol Endocrinol 20:1996-2009
    • (2006) Mol Endocrinol , vol.20 , pp. 1996-2009
    • Pedram, A.1    Razandi, M.2    Levin, E.R.3
  • 18
    • 12344307170 scopus 로고    scopus 로고
    • Identity of an estrogen membrane receptor coupled to a G-protein in human breast cancer cells
    • Thomas P, Pang Y, Filardo EJ, Dong J 2004 Identity of an estrogen membrane receptor coupled to a G-protein in human breast cancer cells. Endocrinology 146:624-632
    • (2004) Endocrinology , vol.146 , pp. 624-632
    • Thomas, P.1    Pang, Y.2    Filardo, E.J.3    Dong, J.4
  • 22
    • 0034703616 scopus 로고    scopus 로고
    • The role of atypical and conventional PKC in dehydroepiandrosterone-induced glucose uptake and dexamethasone-induced insulin resistance
    • Kajita K, Ishizuka T, Miura A, Ishizawa M, Kanoh Y, Yasuda K 2000 The role of atypical and conventional PKC in dehydroepiandrosterone-induced glucose uptake and dexamethasone-induced insulin resistance. Biochem Biophys Res Commun 277:361-367
    • (2000) Biochem Biophys Res Commun , vol.277 , pp. 361-367
    • Kajita, K.1    Ishizuka, T.2    Miura, A.3    Ishizawa, M.4    Kanoh, Y.5    Yasuda, K.6
  • 25
    • 0026062945 scopus 로고
    • Protein kinase C contains two phorbol ester binding domains
    • Burns DJ, Bell RM 1991 Protein kinase C contains two phorbol ester binding domains. J Biol Chem 266:18330-18338
    • (1991) J Biol Chem , vol.266 , pp. 18330-18338
    • Burns, D.J.1    Bell, R.M.2
  • 26
    • 0029785953 scopus 로고    scopus 로고
    • Non-equivalent roles for the first and second zinc fingers of protein kinase Cδ. Effect of their mutation on phorbol ester-induced translocation in NIH 3T3 cells
    • Szallasi Z, Bogi K, Gohari S, Biro T, Acs P, Blumberg PM 1996 Non-equivalent roles for the first and second zinc fingers of protein kinase Cδ. Effect of their mutation on phorbol ester-induced translocation in NIH 3T3 cells. J Biol Chem 271:18299-18301
    • (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
  • 27
    • 0343692517 scopus 로고    scopus 로고
    • Differential selectivity of ligands for the C1a and C1b phorbol ester binding domains of protein kinase Cδ: Possible correlation with tumor-promoting activity
    • Bogi K, Lorenzo PS, Szallasi Z, Acs P, Wagner GS, Blumberg PM 1998 Differential selectivity of ligands for the C1a and C1b phorbol ester binding domains of protein kinase Cδ: possible correlation with tumor-promoting activity. Cancer Res 58:1423-1428
    • (1998) Cancer Res , vol.58 , pp. 1423-1428
    • Bogi, K.1    Lorenzo, P.S.2    Szallasi, Z.3    Acs, P.4    Wagner, G.S.5    Blumberg, P.M.6
  • 28
    • 0029670030 scopus 로고    scopus 로고
    • Protein kinase Cα 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 1996 Protein kinase Cα contains two activator binding sites that bind phorbol esters and diacylglycerols with opposite affinities. J Biol Chem 271:4627-4631
    • (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
  • 29
    • 0031014220 scopus 로고    scopus 로고
    • Hunn M, Quest AF 1997 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 400:226-232
    • Hunn M, Quest AF 1997 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 400:226-232
  • 30
    • 0028021161 scopus 로고
    • The regulatory region of protein kinase Cγ. Studies of phorbol ester binding to individual and combined functional segments expressed as glutathione S-transferase fusion proteins indicate a complex mechanism of regulation by phospholipids, phorbol esters, and divalent cations
    • Quest AF, Bell RM 1994 The regulatory region of protein kinase Cγ. Studies of phorbol ester binding to individual and combined functional segments expressed as glutathione S-transferase fusion proteins indicate a complex mechanism of regulation by phospholipids, phorbol esters, and divalent cations. J Biol Chem 269:20000-20012
    • (1994) J Biol Chem , vol.269 , pp. 20000-20012
    • Quest, A.F.1    Bell, R.M.2
  • 31
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: Structural and functional diversity
    • Nalefski EA, Falke JJ 1996 The C2 domain calcium-binding motif: structural and functional diversity. Protein Sci 5:2375-2390
    • (1996) Protein Sci , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 32
    • 0030034251 scopus 로고    scopus 로고
    • Extending the C2 domain family: C2s in PKCs δ, ε, η, θ, phospholipases, GAPs, and perforin
    • Ponting CP, Parker PJ 1996 Extending the C2 domain family: C2s in PKCs δ, ε, η, θ, phospholipases, GAPs, and perforin. Protein Sci 5:162-166
    • (1996) Protein Sci , vol.5 , pp. 162-166
    • Ponting, C.P.1    Parker, P.J.2
  • 33
    • 0037518192 scopus 로고    scopus 로고
    • 2+/phosphatidylserine binding region of the C2 domain in the translocation of PKCα to the plasma membrane
    • 2+/phosphatidylserine binding region of the C2 domain in the translocation of PKCα to the plasma membrane. J Biol Chem 278:10282-10290
    • (2003) J Biol Chem , vol.278 , pp. 10282-10290
    • Bolsover, S.R.1    Gomez-Fernandez, J.C.2    Corbalan-Garcia, S.3
  • 35
    • 0034698126 scopus 로고    scopus 로고
    • Direct interaction of all-trans-retinoic acid with protein kinase C (PKC). Implications for PKC signaling and cancer therapy
    • Radominska-Pandya A, Chen G, Czernik PJ, Little JM, Samokyszyn VM, Carter CA, Nowak G 2000 Direct interaction of all-trans-retinoic acid with protein kinase C (PKC). Implications for PKC signaling and cancer therapy. J Biol Chem 275:22324-22330
    • (2000) J Biol Chem , vol.275 , pp. 22324-22330
    • Radominska-Pandya, A.1    Chen, G.2    Czernik, P.J.3    Little, J.M.4    Samokyszyn, V.M.5    Carter, C.A.6    Nowak, G.7
  • 38
    • 0032555778 scopus 로고    scopus 로고
    • Protein kinase C: A paradigm for regulation of protein function by two membrane-targeting modules
    • Newton AC, Johnson JE 1998 Protein kinase C: a paradigm for regulation of protein function by two membrane-targeting modules. Biochim Biophys Acta 1376:155-172
    • (1998) Biochim Biophys Acta , vol.1376 , pp. 155-172
    • Newton, A.C.1    Johnson, J.E.2
  • 39
    • 0034651539 scopus 로고    scopus 로고
    • Multiple pathways control protein kinase C phosphorylation
    • Parekh DB, Ziegler W, Parker PJ 2000 Multiple pathways control protein kinase C phosphorylation. EMBO J 19:496-503
    • (2000) EMBO J , vol.19 , pp. 496-503
    • Parekh, D.B.1    Ziegler, W.2    Parker, P.J.3
  • 40
    • 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 1998 Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. Science 281:2042-2045
    • (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
  • 41
    • 0032585532 scopus 로고    scopus 로고
    • Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1)
    • Dutil EM, Toker A, Newton AC 1998 Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1). Curr Biol 8:1366-1375
    • (1998) Curr Biol , vol.8 , pp. 1366-1375
    • Dutil, E.M.1    Toker, A.2    Newton, A.C.3
  • 42
    • 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 2000 Regulation of receptor-mediated protein kinase C membrane trafficking by autophosphorylation. J Biol Chem 275:17024-17034
    • (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
  • 43
    • 0029615509 scopus 로고
    • Protein kinase C is regulated in vivo by three functionally distinct phosphorylations
    • Keranen LM, Dutil EM, Newton AC 1995 Protein kinase C is regulated in vivo by three functionally distinct phosphorylations. Curr Biol 5:1394-1403
    • (1995) Curr Biol , vol.5 , pp. 1394-1403
    • Keranen, L.M.1    Dutil, E.M.2    Newton, A.C.3
  • 44
    • 35649008093 scopus 로고    scopus 로고
    • Protein kinase C isoforms act as specific receptors for rapid responses to estradiol and aldosterone
    • Watson, CS, ed, 1st ed. Boston: Kluwer Academic Publishers;
    • Harvey BJ, Doolan CM 2003 Protein kinase C isoforms act as specific receptors for rapid responses to estradiol and aldosterone. In: Watson, CS, ed. The identities of membrane steroid receptors. 1st ed. Boston: Kluwer Academic Publishers; 177-185
    • (2003) The identities of membrane steroid receptors , pp. 177-185
    • Harvey, B.J.1    Doolan, C.M.2
  • 45
    • 34548302026 scopus 로고    scopus 로고
    • Female gender-specific inhibition of KCNQ1 channels and chloride secretion by 17β-estradiol in rat distal colonic crypts
    • O'Mahony F, Alzamora R, Betts V, LaPaix F, Carter D, Irnaten M, Harvey BJ 2007 Female gender-specific inhibition of KCNQ1 channels and chloride secretion by 17β-estradiol in rat distal colonic crypts. J Biol Chem 282:24563-24573
    • (2007) J Biol Chem , vol.282 , pp. 24563-24573
    • O'Mahony, F.1    Alzamora, R.2    Betts, V.3    LaPaix, F.4    Carter, D.5    Irnaten, M.6    Harvey, B.J.7
  • 46
    • 0022341259 scopus 로고
    • Activation of protein kinase C by Triton X-100 mixed micelles containing diacylglycerol and phosphatidylserine
    • Hannun YA, Loomis CR, Bell RM 1995 Activation of protein kinase C by Triton X-100 mixed micelles containing diacylglycerol and phosphatidylserine. J Biol Chem 260:10039-10043
    • (1995) J Biol Chem , vol.260 , pp. 10039-10043
    • Hannun, Y.A.1    Loomis, C.R.2    Bell, R.M.3
  • 47
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton RM, Hunt HD, Ho SN, Pullen JK, Pease LR 1989 Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77:61-68
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 48
    • 0028167842 scopus 로고
    • Binding of [26-3H]bryostatin 1 and analogs to calcium-dependent and calcium-independent protein kinase C isozymes
    • Kazanietz MG, Lewin NE, Gao F, Pettit GR, Blumberg PM 1994 Binding of [26-3H]bryostatin 1 and analogs to calcium-dependent and calcium-independent protein kinase C isozymes. Mol Pharmacol 46:374-379
    • (1994) Mol Pharmacol , vol.46 , pp. 374-379
    • Kazanietz, M.G.1    Lewin, N.E.2    Gao, F.3    Pettit, G.R.4    Blumberg, P.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.