메뉴 건너뛰기




Volumn 1487, Issue 2-3, 2000, Pages 246-254

The C2 domain of protein kinase Cα is directly involved in the diacylglycerol-dependent binding of the C1 domain to the membrane

Author keywords

C1 domain; C2 domain; Calcium signalling; Phosphatidylserine; Protein kinase C

Indexed keywords

DIACYLGLYCEROL; PHOSPHATIDYLSERINE; PROTEIN KINASE C;

EID: 0042099466     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1388-1981(00)00099-8     Document Type: Article
Times cited : (30)

References (30)
  • 1
    • 0027435064 scopus 로고
    • The potential of protein kinase C as a target for anticancer treatment
    • Basu A. The potential of protein kinase C as a target for anticancer treatment. Pharmacol. Ther. 59:1993;257-280.
    • (1993) Pharmacol. Ther. , vol.59 , pp. 257-280
    • Basu, A.1
  • 2
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function and regulation
    • Newton A. Protein kinase C: structure, function and regulation. J. Biol. Chem. 270:1995;28495-28498.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28495-28498
    • Newton, A.1
  • 3
    • 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. 9:1995;484-496.
    • (1995) FASEB J. , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 4
    • 0032104245 scopus 로고    scopus 로고
    • The extended protein kinase C superfamily
    • Mellor H., Parker P.J. The extended protein kinase C superfamily. Biochem. J. 332:1998;281-292.
    • (1998) Biochem. J. , vol.332 , pp. 281-292
    • Mellor, H.1    Parker, P.J.2
  • 7
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: Structural and functional diversity
    • Nalefski E.A., Falke J.J. The C2 domain calcium-binding motif: structural and functional diversity. Protein Sci. 5:1996;2375-2390.
    • (1996) Protein Sci. , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 12
    • 0038233011 scopus 로고    scopus 로고
    • Determination of the calcium-binding sites of the C2 domain of protein kinase Cα that are critical for its translocation to the plasma membrane
    • Corbalan-Garcia S., Rodriguez-Alfaro J.A., Gomez-Fernandez J.C. Determination of the calcium-binding sites of the C2 domain of protein kinase Cα that are critical for its translocation to the plasma membrane. Biochem. J. 337:1999;513-521.
    • (1999) Biochem. J. , vol.337 , pp. 513-521
    • Corbalan-Garcia, S.1    Rodriguez-Alfaro, J.A.2    Gomez-Fernandez, J.C.3
  • 13
    • 0033538433 scopus 로고    scopus 로고
    • Interplay of C1 and C2 domains of protein kinase Cα in its membrane binding and activation
    • Medkova M., Cho W. Interplay of C1 and C2 domains of protein kinase Cα in its membrane binding and activation. J. Biol. Chem. 274:1999;19852-19861.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19852-19861
    • Medkova, M.1    Cho, W.2
  • 14
    • 0031458338 scopus 로고    scopus 로고
    • Regulation of protein kinase C βiI by its C2 domain
    • Edwards A.S., Newton A.C. Regulation of protein kinase C βII by its C2 domain. Biochemistry. 36:1997;15615-15623.
    • (1997) Biochemistry , vol.36 , pp. 15615-15623
    • Edwards, A.S.1    Newton, A.C.2
  • 15
    • 0032504259 scopus 로고    scopus 로고
    • Mutagenesis of the C2 domain of protein kinase Cα
    • Medkova M., Cho W. Mutagenesis of the C2 domain of protein kinase Cα J. Biol. Chem. 273:1998;17544-17552.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17544-17552
    • Medkova, M.1    Cho, W.2
  • 16
    • 0030755311 scopus 로고    scopus 로고
    • Protein kinase C and phospholipase C: Bilayer interactions and regulation
    • Hurley J.H., Grobler J.A. Protein kinase C and phospholipase C: bilayer interactions and regulation. Curr. Opin. Struct. Biol. 7:1997;557-565.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 557-565
    • Hurley, J.H.1    Grobler, J.A.2
  • 17
    • 0032555778 scopus 로고    scopus 로고
    • Protein kinase C: A paradigm for regulation of protein function by two membrane-targeting modules
    • Newton A.C., Johnson J.E. Protein kinase C: a paradigm for regulation of protein function by two membrane-targeting modules. Biochim. Biophys. Acta. 1376:1998;155-172.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 155-172
    • Newton, A.C.1    Johnson, J.E.2
  • 18
    • 0025912944 scopus 로고
    • Highly sequential binding of protein kinase C and related proteins to membranes
    • Bazzi M.D., Nelsestuen G.L. Highly sequential binding of protein kinase C and related proteins to membranes. Biochemistry. 30:1991;7970-7977.
    • (1991) Biochemistry , vol.30 , pp. 7970-7977
    • Bazzi, M.D.1    Nelsestuen, G.L.2
  • 19
    • 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. 272:1997;25959-25967.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25959-25967
    • Keranen, L.M.1    Newton, A.C.2
  • 20
    • 0032582525 scopus 로고    scopus 로고
    • Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals
    • Oancea E., Meyer T. Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals. Cell. 95:1998;307-318.
    • (1998) Cell , vol.95 , pp. 307-318
    • Oancea, E.1    Meyer, T.2
  • 22
    • 0025186708 scopus 로고
    • Differential transcriptional activation by Oct-1 and Oct-2: Interdependent activation domains induce Oct-2 phosphorylation
    • Tanaka M., Herr W. Differential transcriptional activation by Oct-1 and Oct-2: interdependent activation domains induce Oct-2 phosphorylation. Cell. 60:1990;375-386.
    • (1990) Cell , vol.60 , pp. 375-386
    • Tanaka, M.1    Herr, W.2
  • 23
    • 0017647917 scopus 로고
    • Transfer of purified herpes virus thymidine kinase gene to cultured mouse cells
    • Wigler M., Silverstein S., Lee L.S., Pellicer A., Cheng V.C., Axel R. Transfer of purified herpes virus thymidine kinase gene to cultured mouse cells. Cell. 11:1977;223-227.
    • (1977) Cell , vol.11 , pp. 223-227
    • Wigler, M.1    Silverstein, S.2    Lee, L.S.3    Pellicer, A.4    Cheng, V.C.5    Axel, R.6
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0344114246 scopus 로고
    • Specificity and mechanism of protein kinase C activation by sn-1,2-diacylglycerols
    • Ganong B.R., Loomis C.R., Hannun Y.A., Bell R.M. Specificity and mechanism of protein kinase C activation by sn-1,2-diacylglycerols. Proc. Natl. Acad. Sci. USA. 83:1986;1184-1188.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 1184-1188
    • Ganong, B.R.1    Loomis, C.R.2    Hannun, Y.A.3    Bell, R.M.4
  • 26
    • 0032498538 scopus 로고    scopus 로고
    • Green fluorescent protein (GFP)-tagged cysteine-rich domains from protein kinase C as fluorescent indicators for diacylglycerol signaling in living cells
    • Oancea E., Teruel M.N., Quest A.F.G., 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. 140:1998;485-498.
    • (1998) J. Cell Biol. , vol.140 , pp. 485-498
    • Oancea, E.1    Teruel, M.N.2    Quest, A.F.G.3    Meyer, T.4
  • 27
    • 0028062105 scopus 로고
    • In vivo regulation of protein kinase C by trans-phosphorylation followed by autophosphorylation
    • Dutil E.M., Keranen L.M., DePaoli-Roach A.A., Newton A.C. In vivo regulation of protein kinase C by trans-phosphorylation followed by autophosphorylation. J. Biol. Chem. 269:1994;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
  • 28
    • 0028979464 scopus 로고
    • Crystal structure of the cys2 activator-binding domain of protein kinase Cδ in complex with phorbol ester
    • Zhang G., Kazanietz M.G., Blumberg P.M., Hurley J.H. Crystal structure of the cys2 activator-binding domain of protein kinase Cδ in complex with phorbol ester. Cell. 81:1995;917-924.
    • (1995) Cell , vol.81 , pp. 917-924
    • Zhang, G.1    Kazanietz, M.G.2    Blumberg, P.M.3    Hurley, J.H.4
  • 29
    • 0029102822 scopus 로고
    • Residues in the second cystein-rich region of protein kinase C δ relevant to phorbol ester binding as revealed by site-directed mutagenesis
    • Kazanietz M.G., Wang S., Milne G.W.A., Lewin N.E., Liu H.L., Blumberg P.M. Residues in the second cystein-rich region of protein kinase C δ relevant to phorbol ester binding as revealed by site-directed mutagenesis. J. Biol. Chem. 270:1995;21852-21859.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21852-21859
    • Kazanietz, M.G.1    Wang, S.2    Milne, G.W.A.3    Lewin, N.E.4    Liu, H.L.5    Blumberg, P.M.6
  • 30
    • 0031014220 scopus 로고    scopus 로고
    • Cystein-rich regions of protein kinase C δ are functionally non-equivalent
    • Hunn M., Quest A.F.G. Cystein-rich regions of protein kinase C δ are functionally non-equivalent. FEBS Lett. 400:1997;226-232.
    • (1997) FEBS Lett. , vol.400 , pp. 226-232
    • Hunn, M.1    Quest, A.F.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.