메뉴 건너뛰기




Volumn 9, Issue 14, 1999, Pages 728-737

The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 0033565608     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(99)80332-7     Document Type: Article
Times cited : (125)

References (38)
  • 1
    • 0001285981 scopus 로고
    • Networking with protein kinases
    • Pelech SL: Networking with protein kinases. Curr Biol 1993, 3:513-515.
    • (1993) Curr Biol , vol.3 , pp. 513-515
    • Pelech, S.L.1
  • 2
    • 0027762616 scopus 로고
    • Autophosphorylation: A salient feature of protein kinases
    • Smith JA, Francis, SH, Corbin JD: Autophosphorylation: A salient feature of protein kinases. Mol Cell Biochem 1993, 127-128:51-70.
    • (1993) Mol Cell Biochem , vol.127-128 , pp. 51-70
    • Smith, J.A.1    Francis, S.H.2    Corbin, J.D.3
  • 3
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson LN, Noble MEM, Owen DJ: Active and inactive protein kinases: Structural basis for regulation. Cell 1996, 85:149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.M.2    Owen, D.J.3
  • 4
    • 0030898417 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways
    • Robinson MJ, Cobb MH: Mitogen-activated protein kinase pathways. Curr Opin Cell Biol 1997, 9:180-186.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 180-186
    • Robinson, M.J.1    Cobb, M.H.2
  • 5
    • 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 1995,5:1394-1403.
    • (1995) Curr Biol , vol.5 , pp. 1394-1403
    • Keranen, L.M.1    Dutil, E.M.2    Newton, A.C.3
  • 6
    • 0028802451 scopus 로고
    • The principal target of rapamycin-induced p70s6k inactivation is a novel phosphorylation site within a conserved hydrophobic domain
    • Pearson RB, Dennis PB, Han J-W, Williamson NA, Kozma SC, Wettenhall REH, Thomas G: The principal target of rapamycin-induced p70s6k inactivation is a novel phosphorylation site within a conserved hydrophobic domain. EMBO J 1995, 14:5279-5287.
    • (1995) EMBO J , vol.14 , pp. 5279-5287
    • Pearson, R.B.1    Dennis, P.B.2    Han, J.-W.3    Williamson, N.A.4    Kozma, S.C.5    Wettenhall, R.E.H.6    Thomas, G.7
  • 7
    • 0030875555 scopus 로고    scopus 로고
    • Phosphorylation at conserved carboxyl-terminal hydrophobic motif regulates the catalytic and regulatory domains of protein kinase C
    • Edwards AS, Newton AC: Phosphorylation at conserved carboxyl-terminal hydrophobic motif regulates the catalytic and regulatory domains of protein kinase C. J Biol Chem 1997, 272:18382-18390.
    • (1997) J Biol Chem , vol.272 , pp. 18382-18390
    • Edwards, A.S.1    Newton, A.C.2
  • 8
    • 0031021875 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase C alpha 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 alpha on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state. J Biol Chem 1997, 272:3544-3549.
    • (1997) J Biol Chem , vol.272 , pp. 3544-3549
    • Bornancin, F.1    Parker, P.J.2
  • 10
    • 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 1999, 274:6461-6468.
    • (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
  • 11
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signalling for sustained cellular responses
    • Nishizuka Y: Protein kinase C and lipid signalling for sustained cellular responses. FASEB J 1995, 9:484-496.
    • (1995) FASEB J , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 12
    • 0030987070 scopus 로고    scopus 로고
    • Regulation of protein kinase C
    • Newton AC: Regulation of protein kinase C. Curr Opin Cell Biol 1997, 9:161-167.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 161-167
    • Newton, A.C.1
  • 13
    • 0028062105 scopus 로고
    • In vivo regulation of protein kinase C by trans-phosphorylation followed by autophosphorylation
    • Dutil EM, Keranen LM, DePaoli-Roach AA, Newton AC: In vivo regulation of protein kinase C by trans-phosphorylation followed by autophosphorylation. J Biol Chem 1994, 269:29359-29362.
    • (1994) J Biol Chem , vol.269 , pp. 29359-29362
    • Dutil, E.M.1    Keranen, L.M.2    DePaoli-Roach, A.A.3    Newton, A.C.4
  • 14
    • 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: Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1). Curr Biol 1998, 8:1366-1375.
    • (1998) Curr Biol , vol.8 , pp. 1366-1375
    • Dutil, E.M.1    Toker, A.2    Newton, A.C.3
  • 17
    • 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 1998, 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
  • 18
    • 0027999633 scopus 로고
    • Requirement for negative charge on "activation loop" of protein kinase C
    • Orr JW, Newton AC: Requirement for negative charge on "activation loop" of protein kinase C. J Biol Chem 1994, 269:27715-27718.
    • (1994) J Biol Chem , vol.269 , pp. 27715-27718
    • Orr, J.W.1    Newton, A.C.2
  • 19
    • 0028108027 scopus 로고
    • Threonine-497 is a critical site for permissive activation of protein kinase Cα
    • Cazaubon S, Bornancin F, Parker PJ: Threonine-497 is a critical site for permissive activation of protein kinase Cα. Biochem J 1994, 301:443-448.
    • (1994) Biochem J , vol.301 , pp. 443-448
    • Cazaubon, S.1    Bornancin, F.2    Parker, P.J.3
  • 21
    • 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 1997, 272:25959-25967.
    • (1997) J Biol Chem , vol.272 , pp. 25959-25967
    • Keranen, L.M.1    Newton, A.C.2
  • 22
    • 0024515583 scopus 로고
    • Limited proteolysis of protein kinase C subspecies by calcium-dependent neutral protease (calpain)
    • Kishimoto A, Mikawa K, Hashimoto K, Yasuda I, Tanaka S-1, Tominaga M, et al.: Limited proteolysis of protein kinase C subspecies by calcium-dependent neutral protease (calpain). J Biol Chem 1989, 264:4088-4092.
    • (1989) J Biol Chem , vol.264 , pp. 4088-4092
    • Kishimoto, A.1    Mikawa, K.2    Hashimoto, K.3    Yasuda, I.4    Tanaka, S.-I.5    Tominaga, M.6
  • 23
    • 0025091986 scopus 로고
    • Differential sensitivity of protein kinase C isozymes to phospholipid-induced inactivation
    • Huang K-P, Huang FL: Differential sensitivity of protein kinase C isozymes to phospholipid-induced inactivation. J Biol Chem 1990, 265:738-744.
    • (1990) J Biol Chem , vol.265 , pp. 738-744
    • Huang, K.-P.1    Huang, F.L.2
  • 24
    • 0025863885 scopus 로고
    • The direct measurement of protein kinase C (PKC) activity in isolated membranes using a selective peptide substrate
    • Chakravarthy BR, Bussey A, Whitfield JF, Sikorska M, Williams RE, Durkin JP: The direct measurement of protein kinase C (PKC) activity in isolated membranes using a selective peptide substrate. Anal Biochem 1991, 196:144-150.
    • (1991) Anal Biochem , vol.196 , pp. 144-150
    • Chakravarthy, B.R.1    Bussey, A.2    Whitfield, J.F.3    Sikorska, M.4    Williams, R.E.5    Durkin, J.P.6
  • 25
    • 0023664669 scopus 로고
    • Protein kinase C autophosphorylates by an intrapeptide reaction
    • Newton AC, Koshland DE Jr: Protein kinase C autophosphorylates by an intrapeptide reaction. J Biol Chem 1987, 262:10185-10188.
    • (1987) J Biol Chem , vol.262 , pp. 10185-10188
    • Newton, A.C.1    Koshland D.E., Jr.2
  • 26
    • 0025004286 scopus 로고
    • Autophosphorylation of protein kinase C at three separated regions of its primary sequence
    • Flint AJ, Paladini RD, Koshland DE Jr: Autophosphorylation of protein kinase C at three separated regions of its primary sequence. Science 1990, 249:408-411.
    • (1990) Science , vol.249 , pp. 408-411
    • Flint, A.J.1    Paladini, R.D.2    Koshland D.E., Jr.3
  • 27
    • 0023654062 scopus 로고
    • Domain structure and phosphorylation of protein kinase C
    • Mochly-Rosen D, Koshland DE Jr: domain structure and phosphorylation of protein kinase C. J Biol Chem 1987, 262:2291-2297.
    • (1987) J Biol Chem , vol.262 , pp. 2291-2297
    • Mochly-Rosen, D.1    Koshland D.E., Jr.2
  • 28
    • 0026478887 scopus 로고
    • Autophosphorylation of protein kinase C may require a high order of protein-phospholipid aggregates
    • Bazzi MD, Nelsestuen GL: Autophosphorylation of protein kinase C may require a high order of protein-phospholipid aggregates. J Biol Chem 1992, 267:22891-22896.
    • (1992) J Biol Chem , vol.267 , pp. 22891-22896
    • Bazzi, M.D.1    Nelsestuen, G.L.2
  • 30
    • 0343852701 scopus 로고    scopus 로고
    • Conformational stability of pGEX-expressed Schistosoma japonicum glutathione S-transferase: A detoxification enzyme and fusion-protein affinity tag
    • Kaplan W, Hüsler P, Klump H, Erhardt J, Sluis-Cremer N, Dirr H: Conformational stability of pGEX-expressed Schistosoma japonicum glutathione S-transferase: A detoxification enzyme and fusion-protein affinity tag. Prot Sci 1997, 6:399-406.
    • (1997) Prot Sci , vol.6 , pp. 399-406
    • Kaplan, W.1    Hüsler, P.2    Klump, H.3    Erhardt, J.4    Sluis-Cremer, N.5    Dirr, H.6
  • 32
    • 0032053709 scopus 로고    scopus 로고
    • Mechanisms and consequences of activation of protein kinase B/Akt
    • Downward J: Mechanisms and consequences of activation of protein kinase B/Akt. Curr Opin Cell Biol 1998, 10:262-267.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 262-267
    • Downward, J.1
  • 33
    • 0031127305 scopus 로고    scopus 로고
    • Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα
    • Alessi DR, James SR, Downes CP, Holmes AB, Gaffney PRJ, Reese CB, Cohen P: Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα. Curr Biol 1997, 7:261-269.
    • (1997) Curr Biol , vol.7 , pp. 261-269
    • Alessi, D.R.1    James, S.R.2    Downes, C.P.3    Holmes, A.B.4    Gaffney, P.R.J.5    Reese, C.B.6    Cohen, P.7
  • 34
    • 0033594480 scopus 로고    scopus 로고
    • PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2
    • Balendran A, Casamayor A, Deak M, Paterson A, Gaffney P, Currie R, et al.: PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2. Curr Biol 1999, 9:393-404.
    • (1999) Curr Biol , vol.9 , pp. 393-404
    • Balendran, A.1    Casamayor, A.2    Deak, M.3    Paterson, A.4    Gaffney, P.5    Currie, R.6
  • 35
    • 0033551234 scopus 로고    scopus 로고
    • Protein phosphatase 2A interacts with the 70-kDa S6 kinase and is activated by inhibition of FKBP12-rapamycin-associated protein
    • Peterson RT, Desai BN, Hardwick JS, Schreiber SL: Protein phosphatase 2A interacts with the 70-kDa S6 kinase and is activated by inhibition of FKBP12-rapamycin-associated protein. Proc Natl Acad Sci USA 1999, 96:4438-4442.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4438-4442
    • Peterson, R.T.1    Desai, B.N.2    Hardwick, J.S.3    Schreiber, S.L.4
  • 37
    • 0026741799 scopus 로고
    • Reversible exposure of the pseudosubstrate domain of protein kinase C by phosphatidylserine and diacylglycerol
    • Orr JW, Keranen LM, Newton AC: Reversible exposure of the pseudosubstrate domain of protein kinase C by phosphatidylserine and diacylglycerol. J Biol Chem 1992, 267:15263-15266.
    • (1992) J Biol Chem , vol.267 , pp. 15263-15266
    • Orr, J.W.1    Keranen, L.M.2    Newton, A.C.3
  • 38
    • 0027849713 scopus 로고
    • Purification of glutathione-S-transferase fusion proteins
    • Smith DB: Purification of glutathione-S-transferase fusion proteins. Methods Mol Cell Biol 1993, 4:220-229.
    • (1993) Methods Mol Cell Biol , vol.4 , pp. 220-229
    • Smith, D.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.