메뉴 건너뛰기




Volumn 41, Issue 4, 2013, Pages 1008-1016

Structural characterization of the cyclin-dependent protein kinase family

Author keywords

Cell cycle; Cyclin; Cyclin dependent kinase (CDK); Phosphorylation; Transcription; X ray crystallography

Indexed keywords

CYCLIN DEPENDENT KINASE; CYCLINE;

EID: 84880564100     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20130097     Document Type: Article
Times cited : (35)

References (60)
  • 1
    • 1642323740 scopus 로고    scopus 로고
    • Protein kinase inhibitors: Insights into drug design from structure
    • Noble, M.E., Endicott, J.A. and Johnson, L.N. (2004) Protein kinase inhibitors: insights into drug design from structure. Science 303, 1800-1805
    • (2004) Science , vol.303 , pp. 1800-1805
    • Noble, M.E.1    Endicott, J.A.2    Johnson, L.N.3
  • 2
    • 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
  • 3
    • 84866729606 scopus 로고    scopus 로고
    • Assembly of allosteric macromolecular switches: Lessons from PKA
    • Taylor, S.S., Ilouz, R., Zhang, P. and Kornev, A.P. (2012) Assembly of allosteric macromolecular switches: lessons from PKA. Nat. Rev. Mol. Cell Biol. 13, 646-658
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 646-658
    • Taylor, S.S.1    Ilouz, R.2    Zhang, P.3    Kornev, A.P.4
  • 4
    • 75349112388 scopus 로고    scopus 로고
    • Recent developments in cyclin-dependent kinase biochemical and structural studies
    • Echalier, A., Endicott, J.A. and Noble, M.E. (2010) Recent developments in cyclin-dependent kinase biochemical and structural studies. Biochim. Biophys. Acta 1804, 511-519
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 511-519
    • Echalier, A.1    Endicott, J.A.2    Noble, M.E.3
  • 5
    • 0031466305 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: Engines, clocks, and microprocessors
    • Morgan, D.O. (1997) Cyclin-dependent kinases: engines, clocks, and microprocessors. Annu. Rev. Cell Dev. Biol. 13, 261-291
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 261-291
    • Morgan, D.O.1
  • 7
    • 8644219655 scopus 로고    scopus 로고
    • Living with or without cyclins and cyclin-dependent kinases
    • Sherr, C.J. and Roberts, J.M. (2004) Living with or without cyclins and cyclin-dependent kinases. Genes Dev. 18, 2699-2711
    • (2004) Genes Dev. , vol.18 , pp. 2699-2711
    • Sherr, C.J.1    Roberts, J.M.2
  • 8
    • 84871963013 scopus 로고    scopus 로고
    • P21WAF1 and tumourigenesis: 20 years after
    • Warfel, N.A. and El-Deiry, W.S. (2013) p21WAF1 and tumourigenesis: 20 years after. Curr. Opin. Oncol. 25, 52-58
    • (2013) Curr. Opin. Oncol. , vol.25 , pp. 52-58
    • Warfel, N.A.1    El-Deiry, W.S.2
  • 9
    • 81055138204 scopus 로고    scopus 로고
    • Quality control in the initiation of eukaryotic DNA replication
    • Diffley, J.F. (2011) Quality control in the initiation of eukaryotic DNA replication. Philos. Trans. R. Soc. London Ser. B 366, 3545-3553
    • (2011) Philos. Trans. R. Soc. London Ser. B , vol.366 , pp. 3545-3553
    • Diffley, J.F.1
  • 10
    • 29244468847 scopus 로고    scopus 로고
    • Secrets of a double agent: CDK7 in cell-cycle control and transcription
    • Fisher, R.P. (2005) Secrets of a double agent: CDK7 in cell-cycle control and transcription. J. Cell Sci. 118, 5171-5180
    • (2005) J. Cell Sci. , vol.118 , pp. 5171-5180
    • Fisher, R.P.1
  • 11
    • 79953162883 scopus 로고    scopus 로고
    • Function and regulation of the Mediator complex
    • Conaway, R.C. and Conaway, J.W. (2011) Function and regulation of the Mediator complex. Curr. Opin. Genet. Dev. 21, 225-230
    • (2011) Curr. Opin. Genet. Dev. , vol.21 , pp. 225-230
    • Conaway, R.C.1    Conaway, J.W.2
  • 12
    • 79960377780 scopus 로고    scopus 로고
    • A history of TFIIH: Two decades of molecular biology on a pivotal transcription/repair factor
    • Egly, J.M. and Coin, F. (2011) A history of TFIIH: two decades of molecular biology on a pivotal transcription/repair factor. DNA Repair 10, 714-721
    • (2011) DNA Repair , vol.10 , pp. 714-721
    • Egly, J.M.1    Coin, F.2
  • 15
    • 84859791205 scopus 로고    scopus 로고
    • Cyclin K goes with Cdk12 and Cdk13
    • Kohoutek, J. and Blazek, D. (2012) Cyclin K goes with Cdk12 and Cdk13. Cell Div. 7, 12
    • (2012) Cell Div. , vol.7 , pp. 12
    • Kohoutek, J.1    Blazek, D.2
  • 19
    • 70350782350 scopus 로고    scopus 로고
    • PCTK proteins: The forgotten brain kinases?
    • Cole, A.R. (2009) PCTK proteins: the forgotten brain kinases? Neurosignals 17, 288-297
    • (2009) Neurosignals , vol.17 , pp. 288-297
    • Cole, A.R.1
  • 20
    • 0036711806 scopus 로고    scopus 로고
    • Regulation of the CDK-related protein kinase PCTAIRE-1 and its possible role in neurite outgrowth in Neuro-2A cells
    • Graeser, R., Gannon, J., Poon, R.Y., Dubois, T., Aitken, A. and Hunt, T. (2002) Regulation of the CDK-related protein kinase PCTAIRE-1 and its possible role in neurite outgrowth in Neuro-2A cells. J. Cell Sci. 115, 3479-3490
    • (2002) J. Cell Sci. , vol.115 , pp. 3479-3490
    • Graeser, R.1    Gannon, J.2    Poon, R.Y.3    Dubois, T.4    Aitken, A.5    Hunt, T.6
  • 22
    • 26244442308 scopus 로고    scopus 로고
    • PCTAIRE protein kinases interact directly with the COPII complex and modulate secretory cargo transport
    • Palmer, K.J., Konkel, J.E. and Stephens, D.J. (2005) PCTAIRE protein kinases interact directly with the COPII complex and modulate secretory cargo transport. J. Cell Sci. 118, 3839-3847
    • (2005) J. Cell Sci. , vol.118 , pp. 3839-3847
    • Palmer, K.J.1    Konkel, J.E.2    Stephens, D.J.3
  • 23
    • 33744545575 scopus 로고    scopus 로고
    • Pctaire1 phosphorylates N-ethylmaleimide-sensitive fusion protein: Implications in the regulation of its hexamerization and exocytosis
    • Liu, Y., Cheng, K., Gong, K., Fu, A.K. and Ip, N.Y. (2006) Pctaire1 phosphorylates N-ethylmaleimide-sensitive fusion protein: implications in the regulation of its hexamerization and exocytosis. J. Biol. Chem. 281, 9852-9858
    • (2006) J. Biol. Chem. , vol.281 , pp. 9852-9858
    • Liu, Y.1    Cheng, K.2    Gong, K.3    Fu, A.K.4    Ip, N.Y.5
  • 25
    • 0032190168 scopus 로고    scopus 로고
    • Characterization of brain PCTAIRE-1 kinase immunoreactivity and its interactions with p11 and 14-3-3 proteins
    • Le Bouffant, F., Capdevielle, J., Guillemot, J.C. and Sladeczek, F. (1998) Characterization of brain PCTAIRE-1 kinase immunoreactivity and its interactions with p11 and 14-3-3 proteins. Eur. J. Biochem. 257, 112-120
    • (1998) Eur. J. Biochem. , vol.257 , pp. 112-120
    • Le Bouffant, F.1    Capdevielle, J.2    Guillemot, J.C.3    Sladeczek, F.4
  • 27
    • 80053070661 scopus 로고    scopus 로고
    • Involvement of cyclin-dependent kinase-like 2 in cognitive function required for contextual and spatial learning in mice
    • Gomi, H., Sassa, T., Thompson, R.F. and Itohara, S. (2010) Involvement of cyclin-dependent kinase-like 2 in cognitive function required for contextual and spatial learning in mice. Front. Behav. Neurosci. 4, 17
    • (2010) Front. Behav. Neurosci. , vol.4 , pp. 17
    • Gomi, H.1    Sassa, T.2    Thompson, R.F.3    Itohara, S.4
  • 28
    • 43049089394 scopus 로고    scopus 로고
    • Inactivation of the CDKL3 gene at 5q31. 1 by a balanced t(X;5) translocation associated with nonspecific mild mental retardation
    • Dubos, A., Pannetier, S. and Hanauer, A. (2008) Inactivation of the CDKL3 gene at 5q31.1 by a balanced t(X;5) translocation associated with nonspecific mild mental retardation. Am. J. Med. Genet., Part A 146, 1267-1279
    • (2008) Am. J. Med. Genet., Part A , vol.146 , pp. 1267-1279
    • Dubos, A.1    Pannetier, S.2    Hanauer, A.3
  • 32
  • 33
    • 75349091799 scopus 로고    scopus 로고
    • Defining the conserved internal architecture of a protein kinase
    • Kornev, A.P. and Taylor, S.S. (2010) Defining the conserved internal architecture of a protein kinase. Biochim. Biophys. Acta 1804, 440-444
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 440-444
    • Kornev, A.P.1    Taylor, S.S.2
  • 34
    • 84861859600 scopus 로고    scopus 로고
    • The structural basis for control of eukaryotic protein kinases
    • Endicott, J.A., Noble, M.E. and Johnson, L.N. (2012) The structural basis for control of eukaryotic protein kinases. Annu. Rev. Biochem. 81, 587-613
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 587-613
    • Endicott, J.A.1    Noble, M.E.2    Johnson, L.N.3
  • 35
    • 0030962139 scopus 로고    scopus 로고
    • The Cdk-like protein PCTAIRE-1 from mouse brain associates with p11 and 14-3-3 proteins
    • Sladeczek, F., Camonis, J.H., Burnol, A.F. and Le Bouffant, F. (1997) The Cdk-like protein PCTAIRE-1 from mouse brain associates with p11 and 14-3-3 proteins. Mol. Gen. Genet. 254, 571-577
    • (1997) Mol. Gen. Genet. , vol.254 , pp. 571-577
    • Sladeczek, F.1    Camonis, J.H.2    Burnol, A.F.3    Le Bouffant, F.4
  • 36
    • 0037199958 scopus 로고    scopus 로고
    • Pctaire1 interacts with p35 and is a novel substrate for Cdk5/p35
    • Cheng, K., Li, Z., Fu, W.Y., Wang, J.H., Fu, A.K. and Ip, N.Y. (2002) Pctaire1 interacts with p35 and is a novel substrate for Cdk5/p35. J. Biol. Chem. 277, 31988-31993
    • (2002) J. Biol. Chem. , vol.277 , pp. 31988-31993
    • Cheng, K.1    Li, Z.2    Fu, W.Y.3    Wang, J.H.4    Fu, A.K.5    Ip, N.Y.6
  • 38
    • 34248597065 scopus 로고    scopus 로고
    • Differential regulation and properties of MAPKs
    • Raman, M., Chen, W. and Cobb, M.H. (2007) Differential regulation and properties of MAPKs. Oncogene 26, 3100-3112
    • (2007) Oncogene , vol.26 , pp. 3100-3112
    • Raman, M.1    Chen, W.2    Cobb, M.H.3
  • 39
    • 0029767016 scopus 로고    scopus 로고
    • Structural basis of cyclin-dependent kinase activation by phosphorylation
    • Russo, A.A., Jeffrey, P.D. and Pavletich, N.P. (1996) Structural basis of cyclin-dependent kinase activation by phosphorylation. Nat. Struct. Biol. 3, 696-700
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 696-700
    • Russo, A.A.1    Jeffrey, P.D.2    Pavletich, N.P.3
  • 40
    • 0030866897 scopus 로고    scopus 로고
    • Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
    • Canagarajah, B.J., Khokhlatchev, A., Cobb, M.H. and Goldsmith, E.J. (1997) Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Cell 90, 859-869
    • (1997) Cell , vol.90 , pp. 859-869
    • Canagarajah, B.J.1    Khokhlatchev, A.2    Cobb, M.H.3    Goldsmith, E.J.4
  • 41
    • 33947256308 scopus 로고    scopus 로고
    • Docking interactions in protein kinase and phosphatase networks
    • Remenyi, A., Good, M.C. and Lim, W.A. (2006) Docking interactions in protein kinase and phosphatase networks. Curr. Opin. Struct. Biol. 16, 676-685
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 676-685
    • Remenyi, A.1    Good, M.C.2    Lim, W.A.3
  • 42
    • 33751261134 scopus 로고    scopus 로고
    • Mechanisms of MAPK signalling specificity
    • Bardwell, L. (2006) Mechanisms of MAPK signalling specificity. Biochem. Soc. Trans. 34, 837-841
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 837-841
    • Bardwell, L.1
  • 43
    • 84875465105 scopus 로고    scopus 로고
    • Protein-peptide complex crystallization: A case study on the ERK2 mitogen-activated protein kinase
    • Gogl, G., Toro, I. and Remenyi, A. (2013) Protein-peptide complex crystallization: a case study on the ERK2 mitogen-activated protein kinase. Acta Crystallogr., Sect. D: Biol. Crystallogr. 69, 486-489
    • (2013) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.69 , pp. 486-489
    • Gogl, G.1    Toro, I.2    Remenyi, A.3
  • 45
    • 0033224309 scopus 로고    scopus 로고
    • The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases
    • Brown, N.R., Noble, M.E., Endicott, J.A. and Johnson, L.N. (1999) The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases. Nat. Cell Biol. 1, 438-443
    • (1999) Nat. Cell Biol. , vol.1 , pp. 438-443
    • Brown, N.R.1    Noble, M.E.2    Endicott, J.A.3    Johnson, L.N.4
  • 50
    • 84867395695 scopus 로고    scopus 로고
    • The CDK9 tail determines the reaction pathway of positive transcription elongation factor b
    • Baumli, S., Hole, A.J., Wang, L.Z., Noble, M.E. and Endicott, J.A. (2012) The CDK9 tail determines the reaction pathway of positive transcription elongation factor b. Structure 20, 1788-1795
    • (2012) Structure , vol.20 , pp. 1788-1795
    • Baumli, S.1    Hole, A.J.2    Wang, L.Z.3    Noble, M.E.4    Endicott, J.A.5
  • 51
    • 0033817555 scopus 로고    scopus 로고
    • CDK9 autophosphorylation regulates high-affinity binding of the human immunodeficiency virus type 1 Tat-P-TEFb complex to TAR RNA
    • Garber, M.E., Mayall, T.P., Suess, E.M., Meisenhelder, J., Thompson, N.E. and Jones, K.A. (2000) CDK9 autophosphorylation regulates high-affinity binding of the human immunodeficiency virus type 1 Tat-P-TEFb complex to TAR RNA. Mol. Cell. Biol. 20, 6958-6969
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6958-6969
    • Garber, M.E.1    Mayall, T.P.2    Suess, E.M.3    Meisenhelder, J.4    Thompson, N.E.5    Jones, K.A.6
  • 52
    • 80052034056 scopus 로고    scopus 로고
    • The structure of CDK8/CycC implicates specificity in the CDK/cyclin family and reveals interaction with a deep pocket binder
    • Schneider, E.V., Bottcher, J., Blaesse, M., Neumann, L., Huber, R. and Maskos, K. (2011) The structure of CDK8/CycC implicates specificity in the CDK/cyclin family and reveals interaction with a deep pocket binder. J. Mol. Biol. 412, 251-266
    • (2011) J. Mol. Biol. , vol.412 , pp. 251-266
    • Schneider, E.V.1    Bottcher, J.2    Blaesse, M.3    Neumann, L.4    Huber, R.5    Maskos, K.6
  • 53
    • 0029665852 scopus 로고    scopus 로고
    • Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex
    • Russo, A.A., Jeffrey, P.D., Patten, A.K., Massague, J. and Pavletich, N.P. (1996) Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex. Nature 382, 325-331
    • (1996) Nature , vol.382 , pp. 325-331
    • Russo, A.A.1    Jeffrey, P.D.2    Patten, A.K.3    Massague, J.4    Pavletich, N.P.5
  • 56
    • 0001212842 scopus 로고    scopus 로고
    • Three-dimensional structure of human cyclin H, a positive regulator of the CDK-activating kinase
    • Kim, K.K., Chamberlin, H.M., Morgan, D.O. and Kim, S.H. (1996) Three-dimensional structure of human cyclin H, a positive regulator of the CDK-activating kinase. Nat. Struct. Biol. 3, 849-855
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 849-855
    • Kim, K.K.1    Chamberlin, H.M.2    Morgan, D.O.3    Kim, S.H.4
  • 60
    • 21944438071 scopus 로고    scopus 로고
    • Structure of the Mediator subunit cyclin C and its implications for CDK8 function
    • Hoeppner, S., Baumli, S. and Cramer, P. (2005) Structure of the Mediator subunit cyclin C and its implications for CDK8 function. J. Mol. Biol. 350, 833-842
    • (2005) J. Mol. Biol. , vol.350 , pp. 833-842
    • Hoeppner, S.1    Baumli, S.2    Cramer, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.