메뉴 건너뛰기




Volumn 287, Issue 24, 2012, Pages 20590-20602

Regulation of protein kinase C-related Protein Kinase 2 (PRK2) by an intermolecular PRK2-PRK2 interaction mediated by its N-terminal domain

Author keywords

[No Author keywords available]

Indexed keywords

3-PHOSPHOINOSITIDE-DEPENDENT KINASE 1; ACTIVATION LOOPS; C-TERMINAL REGIONS; CATALYTIC DOMAINS; DIMER FORMATION; GTPASES; KINASE ACTIVITY; LINKER REGION; N-TERMINAL DOMAINS; N-TERMINALS; PROSTATE CANCERS; PROTEIN KINASE; RHO FAMILY;

EID: 84862000521     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.327437     Document Type: Article
Times cited : (23)

References (56)
  • 1
    • 0027959781 scopus 로고
    • Identification of multiple, novel, protein kinase C-related gene products
    • DOI 10.1016/0014-5793(94)01202-4
    • Palmer, R. H., Ridden, J., and Parker, P. J. (1994) Identification of multiple, novel, protein kinase C-related gene products. FEBS Lett. 356, 5-8 (Pubitemid 24374020)
    • (1994) FEBS Letters , vol.356 , Issue.1 , pp. 5-8
    • Palmer, R.H.1
  • 2
    • 0021167007 scopus 로고
    • Phosphorylation of ribosomal protein S6 and a peptide analogue of S6 by a protease-activated kinase isolated from rat liver
    • DOI 10.1016/0014-5793(84)80740-1
    • Gabrielli, B., Wettenhall, R. E., Kemp, B. E., Quinn, M., and Bizonova, L. (1984) Phosphorylation of ribosomal protein S6 and a peptide analogue of S6 by a protease-activated kinase isolated from rat liver. FEBS Lett. 175, 219-226 (Pubitemid 14006541)
    • (1984) FEBS Letters , vol.175 , Issue.2 , pp. 219-226
    • Gabrielli, B.1    Wettenhall, R.E.H.2    Kemp, B.E.3
  • 3
    • 0028260527 scopus 로고
    • A novel protein kinase with leucine zipper-like sequences: Its catalytic domain is highly homologous to that of protein kinase C
    • DOI 10.1006/bbrc.1994.1313
    • Mukai, H., and Ono, Y. (1994) A novel protein kinase with leucine zipper-like sequences. Its catalytic domain is highly homologous to that of protein kinase C. Biochem. Biophys. Res. Commun. 199, 897-904 (Pubitemid 24181746)
    • (1994) Biochemical and Biophysical Research Communications , vol.199 , Issue.2 , pp. 897-904
    • Mukai, H.1    Ono, Y.2
  • 4
    • 0030894714 scopus 로고    scopus 로고
    • The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization
    • Vincent, S., and Settleman, J. (1997) The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization. Mol. Cell Biol. 17, 2247-2256 (Pubitemid 27133312)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.4 , pp. 2247-2256
    • Vincent, S.1    Settleman, J.2
  • 7
    • 0037033804 scopus 로고    scopus 로고
    • Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in keratinocyte cell-cell adhesion
    • DOI 10.1083/jcb.200105140
    • Calautti, E., Grossi, M., Mammucari, C., Aoyama, Y., Pirro, M., Ono, Y., Li, J., and Dotto, G. P. (2002) Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in keratinocyte cell-cell adhesion. J. Cell Biol. 156, 137-148 (Pubitemid 34846942)
    • (2002) Journal of Cell Biology , vol.156 , Issue.1 , pp. 137-148
    • Calautti, E.1    Grossi, M.2    Mammucari, C.3    Aoyama, Y.4    Pirro, M.5    Ono, Y.6    Li, J.7    Dotto, G.P.8
  • 8
    • 3142773619 scopus 로고    scopus 로고
    • 2+ signaling, and cortactin-cytoskeleton function leading to keratinocyte adhesion and differentiation
    • 2+ signaling, and cortactin-cytoskeleton function leading to keratinocyte adhesion and differentiation. J. Biol. Chem. 279, 29654-29669
    • (2004) J. Biol. Chem. , vol.279 , pp. 29654-29669
    • Bourguignon, L.Y.1    Singleton, P.A.2    Diedrich, F.3
  • 9
    • 0037283966 scopus 로고    scopus 로고
    • The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC
    • Mukai, H. (2003) The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC. J. Biochem. 133, 17-27
    • (2003) J. Biochem. , vol.133 , pp. 17-27
    • Mukai, H.1
  • 10
    • 33947591759 scopus 로고    scopus 로고
    • Rho GTPases regulate PRK2/PKN2 to control entry into mitosis and exit from cytokinesis
    • DOI 10.1038/sj.emboj.7601637, PII 7601637
    • Schmidt, A., Durgan, J., Magalhaes, A., and Hall, A. (2007) Rho GTPases regulate PRK2/PKN2 to control entry into mitosis and exit from cytokinesis. EMBO J. 26, 1624-1636 (Pubitemid 46480950)
    • (2007) EMBO Journal , vol.26 , Issue.6 , pp. 1624-1636
    • Schmidt, A.1    Durgan, J.2    Magalhaes, A.3    Hall, A.4
  • 11
    • 78751692389 scopus 로고    scopus 로고
    • The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells
    • Wallace, S. W., Magalhaes, A., and Hall, A. (2011) The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells. Mol. Cell. Biol. 31, 81-91
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 81-91
    • Wallace, S.W.1    Magalhaes, A.2    Hall, A.3
  • 12
    • 0037439106 scopus 로고    scopus 로고
    • A novel inducible transactivation domain in the androgen receptor: Implications for PRK in prostate cancer
    • DOI 10.1093/emboj/cdg023
    • Metzger, E., Müller, J. M., Ferrari, S., Buettner, R., and Schüle, R. (2003) A novel inducible transactivation domain in the androgen receptor. Implications for PRK in prostate cancer. EMBO J. 22, 270-280 (Pubitemid 36119433)
    • (2003) EMBO Journal , vol.22 , Issue.2 , pp. 270-280
    • Metzger, E.1    Muller, J.M.2    Ferrari, S.3    Buettner, R.4    Schule, R.5
  • 14
    • 9644252822 scopus 로고    scopus 로고
    • Protein kinase C-related kinase 2 regulates hepatitis C virus RNA polymerase function by phosphorylation
    • Kim, S. J., Kim, J. H., Kim, Y. G., Lim, H. S., and Oh, J. W. (2004) Protein kinase C-related kinase 2 regulates hepatitis C virus RNA polymerase function by phosphorylation. J. Biol. Chem. 279, 50031-50041
    • (2004) J. Biol. Chem. , vol.279 , pp. 50031-50041
    • Kim, S.J.1    Kim, J.H.2    Kim, Y.G.3    Lim, H.S.4    Oh, J.W.5
  • 15
    • 70349245233 scopus 로고    scopus 로고
    • Suppression of hepatitis C virus replication by protein kinase C-related kinase 2 inhibitors that block phosphorylation of viral RNA polymerase
    • Kim, S. J., Kim, J. H., Sun, J. M., Kim, M. G., and Oh, J. W. (2009) Suppression of hepatitis C virus replication by protein kinase C-related kinase 2 inhibitors that block phosphorylation of viral RNA polymerase. J. Viral Hepat. 16, 697-704
    • (2009) J. Viral Hepat. , vol.16 , pp. 697-704
    • Kim, S.J.1    Kim, J.H.2    Sun, J.M.3    Kim, M.G.4    Oh, J.W.5
  • 16
    • 0034653608 scopus 로고    scopus 로고
    • The PI3K-PBK1 connection: More than just a road to PKB
    • DOI 10.1042/0264-6021:3460561
    • Vanhaesebroeck, B., and Alessi, D. R. (2000) The PI3K-PDK1 connection. More than just a road to PKB. Biochem. J. 346, 561-576 (Pubitemid 30171014)
    • (2000) Biochemical Journal , vol.346 , Issue.3 , pp. 561-576
    • Vanhaesebroeck, B.1    Alessi, D.R.2
  • 17
    • 0035413599 scopus 로고    scopus 로고
    • Phosphoinositide-regulated kinases and phosphoinositide phosphatases
    • DOI 10.1021/cr000091i
    • Leslie, N. R., Biondi, R. M., and Alessi, D. R. (2001) Phosphoinositide-regulated kinases and phosphoinositide phosphatases. Chem. Rev. 101, 2365-2380 (Pubitemid 35373024)
    • (2001) Chemical Reviews , vol.101 , Issue.8 , pp. 2365-2380
    • Leslie, N.R.1    Biondi, R.M.2    Alessi, D.R.3
  • 18
    • 0033545393 scopus 로고    scopus 로고
    • Intracellular signalling: PDK1 - A kinase at the hub of things
    • DOI 10.1016/S0960-9822(99)80058-X
    • Belham, C., Wu, S., and Avruch, J. (1999) Intracellular signalling. PDK1, a kinase at the hub of things. Curr. Biol. 9, R93-96 (Pubitemid 29087534)
    • (1999) Current Biology , vol.9 , Issue.3
    • Belham, C.1    Shilan, W.2    Avruch, J.3
  • 19
    • 0034161251 scopus 로고    scopus 로고
    • Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA
    • Biondi, R. M., Cheung, P. C., Casamayor, A., Deak, M., Currie, R. A., and Alessi, D. R. (2000) Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA. EMBO J. 19, 979-988 (Pubitemid 30119823)
    • (2000) EMBO Journal , vol.19 , Issue.5 , pp. 979-988
    • Biondi, R.M.1    Cheung, P.C.F.2    Casamayor, A.3    Deak, M.4    Currie, R.A.5    Alessi, D.R.6
  • 20
    • 79959568260 scopus 로고    scopus 로고
    • Hydrophobic motif phosphorylation is not required for activation loop phosphorylation of p70 ribosomal protein S6 kinase 1 (S6K1)
    • Keshwani, M. M., von Daake, S., Newton, A. C., Harris, T. K., and Taylor, S. S. (2011) Hydrophobic motif phosphorylation is not required for activation loop phosphorylation of p70 ribosomal protein S6 kinase 1 (S6K1). J. Biol. Chem. 286, 23552-23558
    • (2011) J. Biol. Chem. , vol.286 , pp. 23552-23558
    • Keshwani, M.M.1    Von Daake, S.2    Newton, A.C.3    Harris, T.K.4    Taylor, S.S.5
  • 21
    • 0037102153 scopus 로고    scopus 로고
    • High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site
    • Biondi, R. M., Komander, D., Thomas, C. C., Lizcano, J. M., Deak, M., Alessi, D. R., and van Aalten, D. M. (2002) High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site. EMBO J. 21, 4219-4228
    • (2002) EMBO J. , vol.21 , pp. 4219-4228
    • Biondi, R.M.1    Komander, D.2    Thomas, C.C.3    Lizcano, J.M.4    Deak, M.5    Alessi, D.R.6    Van Aalten, D.M.7
  • 22
    • 0242612949 scopus 로고    scopus 로고
    • A phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1
    • Frödin, M., Jensen, C. J., Merienne, K., and Gammeltoft, S. (2000) A phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1. EMBO J. 19, 2924-2934 (Pubitemid 30386764)
    • (2000) EMBO Journal , vol.19 , Issue.12 , pp. 2924-2934
    • Frodin, M.1    Jensen, C.J.2    Merienne, K.3    Gammeltoft, S.4
  • 23
    • 0035882103 scopus 로고    scopus 로고
    • The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB
    • DOI 10.1093/emboj/20.16.4380
    • Biondi, R. M., Kieloch, A., Currie, R. A., Deak, M., and Alessi, D. R. (2001) The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB. EMBO J. 20, 4380-4390 (Pubitemid 32772032)
    • (2001) EMBO Journal , vol.20 , Issue.16 , pp. 4380-4390
    • Biondi, R.M.1    Kieloch, A.2    Currie, R.A.3    Deak, M.4    Alessi, D.R.5
  • 24
    • 0034617281 scopus 로고    scopus 로고
    • A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Cζ (PKCζ) and PKC- related kinase 2 by PDK1
    • DOI 10.1074/jbc.M000421200
    • Balendran, A., Biondi, R. M., Cheung, P. C., Casamayor, A., Deak, M., and Alessi, D. R. (2000) A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Cζ (PKCζ) and PKC-related kinase 2 by PDK1. J. Biol. Chem. 275, 20806-20813 (Pubitemid 30457673)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.27 , pp. 20806-20813
    • Balendran, A.1    Biondi, R.M.2    Cheung, P.C.F.3    Casamayor, A.4    Deak, M.5    Alessi, D.R.6
  • 25
    • 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., and Newton, A. C. (2001) 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) J. Biol. Chem. , vol.276 , pp. 19588-19596
    • Gao, T.1    Toker, A.2    Newton, A.C.3
  • 26
    • 0037107414 scopus 로고    scopus 로고
    • A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation
    • DOI 10.1093/emboj/cdf551
    • Frödin, M., Antal, T. L., Dümmler, B. A., Jensen, C. J., Deak, M., Gammeltoft, S., and Biondi, R. M. (2002) A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation. EMBO J. 21, 5396-5407 (Pubitemid 35231019)
    • (2002) EMBO Journal , vol.21 , Issue.20 , pp. 5396-5407
    • Frodin, M.1    Antal, T.L.2    Dummler, B.A.3    Jensen, C.J.4    Deak, M.5    Gammeltoft, S.6    Biondi, R.M.7
  • 27
    • 0036295728 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation
    • DOI 10.1016/S1097-2765(02)00550-6
    • Yang, J., Cron, P., Thompson, V., Good, V. M., Hess, D., Hemmings, B. A., and Barford, D. (2002) Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation. Mol. Cell 9, 1227-1240 (Pubitemid 34722302)
    • (2002) Molecular Cell , vol.9 , Issue.6 , 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
  • 28
    • 71049176927 scopus 로고    scopus 로고
    • Regulation of the interaction between protein kinase C-related protein kinase 2 (PRK2) and its upstream kinase, 3-phosphoinositide-dependent protein kinase 1 (PDK1)
    • Dettori, R., Sonzogni, S., Meyer, L., Lopez-Garcia, L. A., Morrice, N. A., Zeuzem, S., Engel, M., Piiper, A., Neimanis, S., Frödin, M., and Biondi, R. M. (2009) Regulation of the interaction between protein kinase C-related protein kinase 2 (PRK2) and its upstream kinase, 3-phosphoinositide- dependent protein kinase 1 (PDK1). J. Biol. Chem. 284, 30318-30327
    • (2009) J. Biol. Chem. , vol.284 , pp. 30318-30327
    • Dettori, R.1    Sonzogni, S.2    Meyer, L.3    Lopez-Garcia, L.A.4    Morrice, N.A.5    Zeuzem, S.6    Engel, M.7    Piiper, A.8    Neimanis, S.9    Frödin, M.10    Biondi, R.M.11
  • 30
    • 0027944808 scopus 로고
    • Activation of PKN, a novel 120-kDa protein kinase with leucine zipper-like sequences, by unsaturated fatty acids and by limited proteolysis
    • Mukai, H., Kitagawa, M., Shibata, H., Takanaga, H., Mori, K., Shimakawa, M., Miyahara, M., Hirao, K., and Ono, Y. (1994) Activation of PKN, a novel 120-kDa protein kinase with leucine zipper-like sequences, by unsaturated fatty acids and by limited proteolysis. Biochem. Biophys. Res. Commun. 204, 348-356
    • (1994) Biochem. Biophys. Res. Commun. , vol.204 , pp. 348-356
    • Mukai, H.1    Kitagawa, M.2    Shibata, H.3    Takanaga, H.4    Mori, K.5    Shimakawa, M.6    Miyahara, M.7    Hirao, K.8    Ono, Y.9
  • 32
    • 0034602393 scopus 로고    scopus 로고
    • Inhibition of Akt and its anti-apoptotic activities by tumor necrosis factor-induced protein kinase C-related kinase 2 (PRK2) cleavage
    • Koh, H., Lee, K. H., Kim, D., Kim, S., Kim, J. W., and Chung, J. (2000) Inhibition of Akt and its anti-apoptotic activities by tumor necrosis factor-induced protein kinase C-related kinase 2 (PRK2) cleavage. J. Biol. Chem. 275, 34451-34458
    • (2000) J. Biol. Chem. , vol.275 , pp. 34451-34458
    • Koh, H.1    Lee, K.H.2    Kim, D.3    Kim, S.4    Kim, J.W.5    Chung, J.6
  • 34
    • 0032826336 scopus 로고    scopus 로고
    • Mutational analysis of the regulatory mechanism of PKN: The regulatory region of PKN contains an arachidonic acid-sensitive autoinhibitory domain
    • Yoshinaga, C., Mukai, H., Toshimori, M., Miyamoto, M., and Ono, Y. (1999) Mutational analysis of the regulatory mechanism of PKN. The regulatory region of PKN contains an arachidonic acid-sensitive autoinhibitory domain. J. Biochem. 126, 475-484 (Pubitemid 29452611)
    • (1999) Journal of Biochemistry , vol.126 , Issue.3 , pp. 475-484
    • Yoshinaga, C.1    Mukai, H.2    Toshimori, M.3    Miyamoto, M.4    Ono, Y.5
  • 36
    • 0028815490 scopus 로고
    • Cloning and expression patterns of two members of a novel protein kinase-C-related kinase family
    • Palmer, R. H., Ridden, J., and Parker, P. J. (1995) Cloning and expression patterns of two members of a novel protein kinase-C-related kinase family. Eur. J. Biochem. 227, 344-351
    • (1995) Eur. J. Biochem. , vol.227 , pp. 344-351
    • Palmer, R.H.1    Ridden, J.2    Parker, P.J.3
  • 37
    • 0033231561 scopus 로고    scopus 로고
    • The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1
    • Maesaki, R., Ihara, K., Shimizu, T., Kuroda, S., Kaibuchi, K., and Hakoshima, T. (1999) The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1. Mol. Cell 4, 793-803
    • (1999) Mol. Cell , vol.4 , pp. 793-803
    • Maesaki, R.1    Ihara, K.2    Shimizu, T.3    Kuroda, S.4    Kaibuchi, K.5    Hakoshima, T.6
  • 38
    • 0030035043 scopus 로고    scopus 로고
    • Identification of a putative target for Rho as the serine-threonine kinase protein kinase N
    • Amano, M., Mukai, H., Ono, Y., Chihara, K., Matsui, T., Hamajima, Y., Okawa, K., Iwamatsu, A., and Kaibuchi, K. (1996) Identification of a putative target for Rho as the serine-threonine kinase protein kinase N. Science 271, 648-650 (Pubitemid 26052909)
    • (1996) Science , vol.271 , Issue.5249 , pp. 648-650
    • Amano, M.1    Mukai, H.2    Ono, Y.3    Chihara, K.4    Matsui, T.5    Hamajima, Y.6    Okawa, K.7    Iwamatsu, A.8    Kaibuchi, K.9
  • 40
    • 0029078831 scopus 로고
    • Expression, purification, and characterization of the ubiquitous protein kinase C-related kinase 1
    • Palmer, R. H., and Parker, P. J. (1995) Expression, purification, and characterization of the ubiquitous protein kinase C-related kinase 1. Biochem. J. 309, 315-320
    • (1995) Biochem. J. , vol.309 , pp. 315-320
    • Palmer, R.H.1    Parker, P.J.2
  • 42
    • 0037082158 scopus 로고    scopus 로고
    • High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells
    • Durocher, Y., Perret, S., and Kamen, A. (2002) High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells. Nucleic Acids Res. 30, E9
    • (2002) Nucleic Acids Res. , vol.30
    • Durocher, Y.1    Perret, S.2    Kamen, A.3
  • 44
    • 0030980027 scopus 로고    scopus 로고
    • Isolation and characterization of a structural homologue of human PRK2 from rat liver: Distinguishing substrate and lipid activator specificities
    • DOI 10.1074/jbc.272.15.10030
    • Yu, W., Liu, J., Morrice, N. A., and Wettenhall, R. E. (1997) Isolation and characterization of a structural homologue of human PRK2 from rat liver. Distinguishing substrate and lipid activator specificities. J. Biol. Chem. 272, 10030-10034 (Pubitemid 27171676)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.15 , pp. 10030-10034
    • Yu, W.1    Liu, J.2    Morrice, N.A.3    Wettenhall, R.E.H.4
  • 45
    • 0023283609 scopus 로고
    • The hormone response element of the mouse mammary tumor virusDNAmediates the progestin and androgen induction of transcription in the proviral long terminal repeat region
    • Cato, A. C., Henderson, D., and Ponta, H. (1987) The hormone response element of the mouse mammary tumor virusDNAmediates the progestin and androgen induction of transcription in the proviral long terminal repeat region. EMBO J. 6, 363-368
    • (1987) EMBO J. , vol.6 , pp. 363-368
    • Cato, A.C.1    Henderson, D.2    Ponta, H.3
  • 46
    • 33745002702 scopus 로고    scopus 로고
    • An Allosteric Mechanism for Activation of the Kinase Domain of Epidermal Growth Factor Receptor
    • DOI 10.1016/j.cell.2006.05.013, PII S0092867406005848
    • Zhang, X., Gureasko, J., Shen, K., Cole, P. A., and Kuriyan, J. (2006) An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 125, 1137-1149 (Pubitemid 43866200)
    • (2006) Cell , vol.125 , Issue.6 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 47
    • 79953308071 scopus 로고    scopus 로고
    • Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms
    • Jura, N., Zhang, X., Endres, N. F., Seeliger, M. A., Schindler, T., and Kuriyan, J. (2011) Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms. Mol. Cell 42, 9-22
    • (2011) Mol. Cell , vol.42 , pp. 9-22
    • Jura, N.1    Zhang, X.2    Endres, N.F.3    Seeliger, M.A.4    Schindler, T.5    Kuriyan, J.6
  • 49
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate
    • DOI 10.1126/science.275.5300.665
    • Franke, T. F., Kaplan, D. R., Cantley, L. C., and Toker, A. (1997) Direct regulation of the Akt proto-oncogene product by phosphatidylinositol 3,4-bisphosphate. Science 275, 665-668 (Pubitemid 27061333)
    • (1997) Science , vol.275 , Issue.5300 , pp. 665-668
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 52
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D. R., Zheng, J. H., Ten Eyck, L. F., Xuong, N. H., Taylor, S. S., and Sowadski, J. M. (1991) Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 414-420 (Pubitemid 21917166)
    • (1991) Science , vol.253 , Issue.5018 , pp. 414-420
    • Knighton, D.R.1    Zheng, J.2    Ten, E.L.F.3    Xuong, N.-H.4    Taylor, S.S.5    Sowadski, J.M.6
  • 53
    • 0034646677 scopus 로고    scopus 로고
    • Rho GTPase control of protein kinase C-related protein kinase activation by 3-phosphoinositide-dependent protein kinase
    • DOI 10.1074/jbc.275.15.11064
    • Flynn, P., Mellor, H., Casamassima, A., and Parker, P. J. (2000) Rho GT-Pase control of protein kinase C-related protein kinase activation by 3-phosphoinositide-dependent protein kinase. J. Biol. Chem. 275, 11064-11070 (Pubitemid 30212747)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.15 , pp. 11064-11070
    • Flynn, P.1    Mellor, H.2    Casamassima, A.3    Parker, P.J.4
  • 55
    • 68549123439 scopus 로고    scopus 로고
    • 3,5-Diphenylpent-2-enoic acids as allosteric activators of the protein kinase PDK1. Structure-activity relationships and thermodynamic characterization of0 binding as paradigms for PIF-binding pocket-targeting compounds
    • Stroba, A., Schaeffer, F., Hindie, V., Lopez-Garcia, L., Adrian, I., Fröhner, W., Hartmann, R. W., Biondi, R. M., and Engel, M. (2009) 3,5-Diphenylpent-2-enoic acids as allosteric activators of the protein kinase PDK1. Structure-activity relationships and thermodynamic characterization of0 binding as paradigms for PIF-binding pocket-targeting compounds. J. Med. Chem. 52, 4683-4693
    • (2009) J. Med. Chem. , vol.52 , pp. 4683-4693
    • Stroba, A.1    Schaeffer, F.2    Hindie, V.3    Lopez-Garcia, L.4    Adrian, I.5    Fröhner, W.6    Hartmann, R.W.7    Biondi, R.M.8    Engel, M.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.