메뉴 건너뛰기




Volumn 52, Issue 45, 2013, Pages 7999-8011

Differential binding of RhoA, RhoB, and RhoC to protein kinase C-related kinase (PRK) isoforms PRK1, PRK2, and PRK3: PRKs have the highest affinity for RhoB

Author keywords

[No Author keywords available]

Indexed keywords

C-TERMINUS; DIFFERENTIAL BINDING; ISOFORMS; N TERMINUS; PROTEIN KINASE; PROTEIN KINASE C; RHO FAMILY; THERMALLY STABLE;

EID: 84887572710     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi401216w     Document Type: Article
Times cited : (29)

References (54)
  • 2
    • 11844304062 scopus 로고    scopus 로고
    • The role of the Rho GTPases in neuronal development
    • Govek, E. E., Newey, S. E., and Van Aelst, L. (2005) The role of the Rho GTPases in neuronal development Genes Dev. 19, 1-49
    • (2005) Genes Dev. , vol.19 , pp. 1-49
    • Govek, E.E.1    Newey, S.E.2    Van Aelst, L.3
  • 4
    • 18944372230 scopus 로고    scopus 로고
    • Rho kinase, a promising drug target for neurological disorders
    • Mueller, B. K., Mack, H., and Teusch, N. (2005) Rho kinase, a promising drug target for neurological disorders Nat. Rev. Drug Discovery 4, 387-398
    • (2005) Nat. Rev. Drug Discovery , vol.4 , pp. 387-398
    • Mueller, B.K.1    MacK, H.2    Teusch, N.3
  • 5
    • 31844450444 scopus 로고    scopus 로고
    • Targeting Rho and Rho-kinase in the treatment of cardiovascular disease
    • Budzyn, K., Marley, P. D., and Sobey, C. G. (2006) Targeting Rho and Rho-kinase in the treatment of cardiovascular disease Trends Pharmacol. Sci. 27, 97-104
    • (2006) Trends Pharmacol. Sci. , vol.27 , pp. 97-104
    • Budzyn, K.1    Marley, P.D.2    Sobey, C.G.3
  • 6
    • 44449178868 scopus 로고    scopus 로고
    • Rho GTPases in cancer cell biology
    • Vega, F. M. and Ridley, A. J. (2008) Rho GTPases in cancer cell biology FEBS Lett. 582, 2093-2101
    • (2008) FEBS Lett. , vol.582 , pp. 2093-2101
    • Vega, F.M.1    Ridley, A.J.2
  • 10
    • 0032530750 scopus 로고    scopus 로고
    • A protein kinase, PKN, accumulates in Alzheimer neurofibrillary tangles and associated endoplasmic reticulum-derived vesicles and phosphorylates tau protein
    • Kawamata, T., Taniguchi, T., Mukai, H., Kitagawa, M., Hashimoto, T., Maeda, K., Ono, Y., and Tanaka, C. (1998) A protein kinase, PKN, accumulates in Alzheimer neurofibrillary tangles and associated endoplasmic reticulum-derived vesicles and phosphorylates tau protein J. Neurosci. 18, 7402-7410
    • (1998) J. Neurosci. , vol.18 , pp. 7402-7410
    • Kawamata, T.1    Taniguchi, T.2    Mukai, H.3    Kitagawa, M.4    Hashimoto, T.5    Maeda, K.6    Ono, Y.7    Tanaka, C.8
  • 11
    • 0037439106 scopus 로고    scopus 로고
    • A novel inducible transactivation domain in the androgen receptor: Implications for PRK in prostate cancer
    • Metzger, E., Muller, J. M., Ferrari, S., Buettner, R., and Schule, R. (2003) A novel inducible transactivation domain in the androgen receptor: Implications for PRK in prostate cancer EMBO J. 22, 270-280
    • (2003) EMBO J. , vol.22 , pp. 270-280
    • Metzger, E.1    Muller, J.M.2    Ferrari, S.3    Buettner, R.4    Schule, R.5
  • 14
    • 34247631217 scopus 로고    scopus 로고
    • Hyaluronan-CD44 interaction stimulates Rac1 signaling and PKNγ kinase activation leading to cytoskeleton function and cell migration in astrocytes
    • Bourguignon, L. Y. W., Gilad, E., Peyrollier, K., Brightman, A., and Swanson, R. A. (2007) Hyaluronan-CD44 interaction stimulates Rac1 signaling and PKNγ kinase activation leading to cytoskeleton function and cell migration in astrocytes J. Neurochem. 101, 1002-1017
    • (2007) J. Neurochem. , vol.101 , pp. 1002-1017
    • Bourguignon, L.Y.W.1    Gilad, E.2    Peyrollier, K.3    Brightman, A.4    Swanson, R.A.5
  • 16
    • 33947591759 scopus 로고    scopus 로고
    • Rho GTPases regulate PRK2/PKN2 to control entry into mitosis and exit from cytokinesis
    • 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
    • (2007) EMBO J. , vol.26 , pp. 1624-1636
    • Schmidt, A.1    Durgan, J.2    Magalhaes, A.3    Hall, A.4
  • 17
    • 0037033804 scopus 로고    scopus 로고
    • Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in keratinocyte cell-cell adhesion
    • 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
    • (2002) J. Cell Biol. , vol.156 , 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
  • 18
    • 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
  • 19
    • 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
  • 21
    • 0028815490 scopus 로고
    • Cloning and Expression Patterns of 2 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 2 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
  • 22
    • 0033546497 scopus 로고    scopus 로고
    • Identification and characterization of PKNβ, a novel isoform of protein kinase PKN: Expression and arachidonic acid dependency are different from those of PKNα
    • Oishi, K., Mukai, H., Shibata, H., Takahashi, M., and Ona, Y. (1999) Identification and characterization of PKNβ, a novel isoform of protein kinase PKN: Expression and arachidonic acid dependency are different from those of PKNα Biochem. Biophys. Res. Commun. 261, 808-814
    • (1999) Biochem. Biophys. Res. Commun. , vol.261 , pp. 808-814
    • Oishi, K.1    Mukai, H.2    Shibata, H.3    Takahashi, M.4    Ona, Y.5
  • 25
    • 84861938889 scopus 로고    scopus 로고
    • Depletion of protein kinase N3 (PKN3) impairs actin and adherens junctions dynamics and attenuates endothelial cell activation
    • Mopert, K., Loffler, K., Roder, N., Kaufmann, J., and Santel, A. (2012) Depletion of protein kinase N3 (PKN3) impairs actin and adherens junctions dynamics and attenuates endothelial cell activation Eur. J. Cell Biol. 91, 694-705
    • (2012) Eur. J. Cell Biol. , vol.91 , pp. 694-705
    • Mopert, K.1    Loffler, K.2    Roder, N.3    Kaufmann, J.4    Santel, A.5
  • 28
    • 57649210155 scopus 로고    scopus 로고
    • Protein Kinase C-related Kinase and ROCK Are Required for Thrombin-induced Endothelial Cell Permeability Downstream from Gα(12/13) and Gα(11/q)
    • Gavard, J. and Gutkind, J. S. (2008) Protein Kinase C-related Kinase and ROCK Are Required for Thrombin-induced Endothelial Cell Permeability Downstream from Gα(12/13) and Gα(11/q) J. Biol. Chem. 283, 29888-29896
    • (2008) J. Biol. Chem. , vol.283 , pp. 29888-29896
    • Gavard, J.1    Gutkind, J.S.2
  • 29
    • 0032563208 scopus 로고    scopus 로고
    • Different regions of Rho determine Rho-selective binding of different classes of Rho target molecules
    • Fujisawa, K., Madaule, P., Ishizaki, T., Watanabe, G., Bito, H., Saito, Y., Hall, A., and Narumiya, S. (1998) Different regions of Rho determine Rho-selective binding of different classes of Rho target molecules J. Biol. Chem. 273, 18943-18949
    • (1998) J. Biol. Chem. , vol.273 , pp. 18943-18949
    • Fujisawa, K.1    Madaule, P.2    Ishizaki, T.3    Watanabe, G.4    Bito, H.5    Saito, Y.6    Hall, A.7    Narumiya, S.8
  • 31
    • 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
  • 32
    • 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
  • 33
    • 0348010318 scopus 로고    scopus 로고
    • Molecular dissection of the interaction between the small G proteins Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1)
    • Owen, D., Lowe, P. N., Nietlispach, D., Brosnan, C. E., Chirgadze, D. Y., Parker, P. J., Blundell, T. L., and Mott, H. R. (2003) Molecular dissection of the interaction between the small G proteins Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1) J. Biol. Chem. 278, 50578-50587
    • (2003) J. Biol. Chem. , vol.278 , pp. 50578-50587
    • Owen, D.1    Lowe, P.N.2    Nietlispach, D.3    Brosnan, C.E.4    Chirgadze, D.Y.5    Parker, P.J.6    Blundell, T.L.7    Mott, H.R.8
  • 34
    • 0032579489 scopus 로고    scopus 로고
    • Multiple interactions of PRK1 with RhoA: Functional assignment of the HR1 repeat motif
    • Flynn, P., Mellor, H., Palmer, R., Panayotou, G., and Parker, P. J. (1998) Multiple interactions of PRK1 with RhoA: Functional assignment of the HR1 repeat motif J. Biol. Chem. 273, 2698-2705
    • (1998) J. Biol. Chem. , vol.273 , pp. 2698-2705
    • Flynn, P.1    Mellor, H.2    Palmer, R.3    Panayotou, G.4    Parker, P.J.5
  • 35
    • 11144226356 scopus 로고    scopus 로고
    • Models of the cooperative mechanism for Rho effector recognition: Implications for RhoA-mediated effector activation
    • Blumenstein, L. and Ahmadian, M. R. (2004) Models of the cooperative mechanism for Rho effector recognition: Implications for RhoA-mediated effector activation J. Biol. Chem. 279, 53419-53426
    • (2004) J. Biol. Chem. , vol.279 , pp. 53419-53426
    • Blumenstein, L.1    Ahmadian, M.R.2
  • 36
    • 79953683448 scopus 로고    scopus 로고
    • Mutational Analysis Reveals a Single Binding Interface between RhoA and Its Effector, PRK1
    • Hutchinson, C. L., Lowe, P. N., McLaughlin, S. H., Mott, H. R., and Owen, D. (2011) Mutational Analysis Reveals a Single Binding Interface between RhoA and Its Effector, PRK1 Biochemistry 50, 2860-2869
    • (2011) Biochemistry , vol.50 , pp. 2860-2869
    • Hutchinson, C.L.1    Lowe, P.N.2    McLaughlin, S.H.3    Mott, H.R.4    Owen, D.5
  • 38
    • 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
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2247-2256
    • Vincent, S.1    Settleman, J.2
  • 39
    • 0033135283 scopus 로고    scopus 로고
    • The Drosophila Pkn protein kinase is a Rho Rac effector target required for dorsal closure during embryogenesis
    • Lu, Y. and Settleman, J. (1999) The Drosophila Pkn protein kinase is a Rho Rac effector target required for dorsal closure during embryogenesis Genes Dev. 13, 1168-1180
    • (1999) Genes Dev. , vol.13 , pp. 1168-1180
    • Lu, Y.1    Settleman, J.2
  • 40
    • 0034911721 scopus 로고    scopus 로고
    • PKNβ interacts with the SH3 domains of Graf and a novel Graf related protein, Graf2, which are GTPase activating proteins for Rho family
    • Shibata, H., Oishi, K., Yamagiwa, A., Matsumoto, M., Mukai, H., and Ono, Y. (2001) PKNβ interacts with the SH3 domains of Graf and a novel Graf related protein, Graf2, which are GTPase activating proteins for Rho family J. Biochem. 130, 23-31
    • (2001) J. Biochem. , vol.130 , pp. 23-31
    • Shibata, H.1    Oishi, K.2    Yamagiwa, A.3    Matsumoto, M.4    Mukai, H.5    Ono, Y.6
  • 41
    • 0026585599 scopus 로고
    • Statistical Determination of the Average Values of the Extinction Coefficients of Tryptophan and Tyrosine in Native Proteins
    • Mach, H., Middaugh, C. R., and Lewis, R. V. (1992) Statistical Determination of the Average Values of the Extinction Coefficients of Tryptophan and Tyrosine in Native Proteins Anal. Biochem. 200, 74-80
    • (1992) Anal. Biochem. , vol.200 , pp. 74-80
    • MacH, H.1    Middaugh, C.R.2    Lewis, R.V.3
  • 42
    • 64349107039 scopus 로고    scopus 로고
    • Solution Structure and Dynamics of the Small GTPase RalB in Its Active Conformation: Significance for Effector Protein Binding
    • Fenwick, R. B., Prasannan, S., Campbell, L. J., Nietlispach, D., Evetts, K. A., Camonis, J., Mott, H. R., and Owen, D. (2009) Solution Structure and Dynamics of the Small GTPase RalB in Its Active Conformation: Significance for Effector Protein Binding Biochemistry 48, 2192-2206
    • (2009) Biochemistry , vol.48 , pp. 2192-2206
    • Fenwick, R.B.1    Prasannan, S.2    Campbell, L.J.3    Nietlispach, D.4    Evetts, K.A.5    Camonis, J.6    Mott, H.R.7    Owen, D.8
  • 43
    • 0033579936 scopus 로고    scopus 로고
    • The conserved arginine in Rho-GTPase-activating protein is essential for efficient catalysis but not for complex formation with rho CDP and aluminum fluoride
    • Graham, D. L., Eccleston, J. F., and Lowe, P. N. (1999) The conserved arginine in Rho-GTPase-activating protein is essential for efficient catalysis but not for complex formation with rho CDP and aluminum fluoride Biochemistry 38, 985-991
    • (1999) Biochemistry , vol.38 , pp. 985-991
    • Graham, D.L.1    Eccleston, J.F.2    Lowe, P.N.3
  • 44
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore, L. and Wallace, B. A. (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data Nucleic Acids Res. 32, W668-W673
    • (2004) Nucleic Acids Res. , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 45
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • Whitmore, L. and Wallace, B. A. (2008) Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases Biopolymers 89, 392-400
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 46
    • 84887591957 scopus 로고
    • Analysis of Protein-CD Spectra for Secondary Structure Using a Simple Matrix Multiplication
    • Compton, L. A. and Johnson, W. C. (1986) Analysis of Protein-CD Spectra for Secondary Structure Using a Simple Matrix Multiplication Biophys. J. 49, A494
    • (1986) Biophys. J. , vol.49 , pp. 494
    • Compton, L.A.1    Johnson, W.C.2
  • 47
    • 4244085403 scopus 로고    scopus 로고
    • Analysis of protein CD spectra: Comparison of CONTIN, SELCON3, and CDSSTR methods in CDPro software
    • Sreerama, N. and Woody, R. W. (2000) Analysis of protein CD spectra: Comparison of CONTIN, SELCON3, and CDSSTR methods in CDPro software Biophys. J. 78, 334A
    • (2000) Biophys. J. , vol.78
    • Sreerama, N.1    Woody, R.W.2
  • 48
    • 6344231714 scopus 로고    scopus 로고
    • Why three Rho proteins? RhoA, RhoB, RhoC, and cell motility
    • Wheeler, A. P. and Ridley, A. J. (2004) Why three Rho proteins? RhoA, RhoB, RhoC, and cell motility Exp. Cell Res. 301, 43-49
    • (2004) Exp. Cell Res. , vol.301 , pp. 43-49
    • Wheeler, A.P.1    Ridley, A.J.2
  • 49
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi, J. Y., Blundell, T. L., and Mizuguchi, K. (2001) FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties J. Mol. Biol. 310, 243
    • (2001) J. Mol. Biol. , vol.310 , pp. 243
    • Shi, J.Y.1    Blundell, T.L.2    Mizuguchi, K.3
  • 52
    • 24944591007 scopus 로고    scopus 로고
    • Specificity Determinants on Cdc42 for Binding Its Effector Protein ACK
    • Elliot-Smith, A. E., Mott, H. R., Lowe, P. N., Laue, E. D., and Owen, D. (2005) Specificity Determinants on Cdc42 for Binding Its Effector Protein ACK Biochemistry 44, 12373-12383
    • (2005) Biochemistry , vol.44 , pp. 12373-12383
    • Elliot-Smith, A.E.1    Mott, H.R.2    Lowe, P.N.3    Laue, E.D.4    Owen, D.5
  • 54
    • 0027412196 scopus 로고
    • Alscript: A Tool to Format Multiple Sequence Alignments
    • Barton, G. J. (1993) Alscript: A Tool to Format Multiple Sequence Alignments Protein Eng. 6, 37-40
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.