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Volumn 5, Issue , 2015, Pages

Structures of the CDK12/CycK complex with AMP-PNP reveal a flexible C-terminal kinase extension important for ATP binding

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLYLIMIDODIPHOSPHATE; CCNK PROTEIN, HUMAN; CDK12 PROTEIN, HUMAN; CYCLIN DEPENDENT KINASE; CYCLINE; PROTEIN BINDING;

EID: 84948164846     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep17122     Document Type: Article
Times cited : (29)

References (48)
  • 1
    • 71049169616 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: A family portrait
    • Malumbres, M. et al. Cyclin-dependent kinases: a family portrait. Nat Cell Biol 11, 1275-6 (2009).
    • (2009) Nat Cell Biol , vol.11 , pp. 1275-1276
    • Malumbres, M.1
  • 2
    • 84880264045 scopus 로고    scopus 로고
    • Cdks, cyclins and CKIs: Roles beyond cell cycle regulation
    • Lim, S. & Kaldis, P. Cdks, cyclins and CKIs: roles beyond cell cycle regulation. Development 140, 3079-93 (2013).
    • (2013) Development , vol.140 , pp. 3079-3093
    • Lim, S.1    Kaldis, P.2
  • 3
    • 84856767106 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 16/PCTAIRE kinase 1 is activated by cyclin Y and is essential for spermatogenesis
    • Mikolcevic, P. et al. Cyclin-dependent kinase 16/PCTAIRE kinase 1 is activated by cyclin Y and is essential for spermatogenesis. Mol Cell Biol 32, 868-79 (2012).
    • (2012) Mol Cell Biol , vol.32 , pp. 868-879
    • Mikolcevic, P.1
  • 4
    • 71649108294 scopus 로고    scopus 로고
    • Cell cycle control of wnt receptor activation
    • Davidson, G. et al. Cell cycle control of wnt receptor activation. Dev Cell 17, 788-99 (2009).
    • (2009) Dev Cell , vol.17 , pp. 788-799
    • Davidson, G.1
  • 5
    • 84868011832 scopus 로고    scopus 로고
    • Orphan kinases turn eccentric: A new class of cyclin Y-activated, membrane-targeted CDKs
    • Mikolcevic, P., Rainer, J. & Geley, S. Orphan kinases turn eccentric: a new class of cyclin Y-activated, membrane-targeted CDKs. Cell Cycle 11, 3758-68 (2012).
    • (2012) Cell Cycle , vol.11 , pp. 3758-3768
    • Mikolcevic, P.1    Rainer, J.2    Geley, S.3
  • 6
    • 0020961333 scopus 로고
    • Cyclin: A protein specified by maternal mRNA in sea urchin eggs that is destroyed at each cleavage division
    • Evans, T., Rosenthal, E. T., Youngblom, J., Distel, D. & Hunt, T. Cyclin: a protein specified by maternal mRNA in sea urchin eggs that is destroyed at each cleavage division. Cell 33, 389-96 (1983).
    • (1983) Cell , vol.33 , pp. 389-396
    • Evans, T.1    Rosenthal, E.T.2    Youngblom, J.3    Distel, D.4    Hunt, T.5
  • 7
    • 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. & Johnson, L. N. The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases. Nat Cell Biol 1, 438-43 (1999).
    • (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
  • 8
    • 34547697834 scopus 로고    scopus 로고
    • Cyclin B and cyclin A confer different substrate recognition properties on CDK2
    • Brown, N. R. et al. Cyclin B and cyclin A confer different substrate recognition properties on CDK2. Cell Cycle 6, 1350-9 (2007).
    • (2007) Cell Cycle , vol.6 , pp. 1350-1359
    • Brown, N.R.1
  • 9
    • 0032167631 scopus 로고    scopus 로고
    • Substrate recruitment to cyclin-dependent kinase 2 by a multipurpose docking site on cyclin A
    • Schulman, B. A., Lindstrom, D. L. & Harlow, E. Substrate recruitment to cyclin-dependent kinase 2 by a multipurpose docking site on cyclin A. Proc Natl Acad Sci USA 95, 10453-8 (1998).
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10453-10458
    • Schulman, B.A.1    Lindstrom, D.L.2    Harlow, E.3
  • 10
    • 0027994603 scopus 로고
    • A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase
    • Fisher, R. P. & Morgan, D. O. A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase. Cell 78, 713-24 (1994).
    • (1994) Cell , vol.78 , pp. 713-724
    • Fisher, R.P.1    Morgan, D.O.2
  • 11
    • 0028070243 scopus 로고
    • A cyclin associated with the CDK-activating kinase MO15
    • Makela, T. P. et al. A cyclin associated with the CDK-activating kinase MO15. Nature 371, 254-7 (1994).
    • (1994) Nature , vol.371 , pp. 254-257
    • Makela, T.P.1
  • 12
    • 0034896206 scopus 로고    scopus 로고
    • CrkRS: A novel conserved Cdc2-related protein kinase that colocalises with SC35 speckles
    • Ko, T. K., Kelly, E. & Pines, J. CrkRS: a novel conserved Cdc2-related protein kinase that colocalises with SC35 speckles. J Cell Sci 114, 2591-603 (2001).
    • (2001) J Cell Sci , vol.114 , pp. 2591-2603
    • Ko, T.K.1    Kelly, E.2    Pines, J.3
  • 13
    • 0034731311 scopus 로고    scopus 로고
    • A new subfamily of high molecular mass CDC2-related kinases with PITAI/VRE motifs
    • Marques, F. et al. A new subfamily of high molecular mass CDC2-related kinases with PITAI/VRE motifs. Biochem Biophys Res Commun 279, 832-7 (2000).
    • (2000) Biochem Biophys Res Commun , vol.279 , pp. 832-837
    • Marques, F.1
  • 14
    • 33749467712 scopus 로고    scopus 로고
    • CDC2L5, a Cdk-like kinase with RS domain, interacts with the ASF/SF2-associated protein p32 and affects splicing in vivo
    • Even, Y. et al. CDC2L5, a Cdk-like kinase with RS domain, interacts with the ASF/SF2-associated protein p32 and affects splicing in vivo. J Cell Biochem 99, 890-904 (2006).
    • (2006) J Cell Biochem , vol.99 , pp. 890-904
    • Even, Y.1
  • 15
    • 84868681176 scopus 로고    scopus 로고
    • Interaction of cyclin-dependent kinase 12/CrkRS with cyclin K1 is required for the phosphorylation of the C-terminal domain of RNA polymerase II
    • Cheng, S. W. et al. Interaction of cyclin-dependent kinase 12/CrkRS with cyclin K1 is required for the phosphorylation of the C-terminal domain of RNA polymerase II. Mol Cell Biol 32, 4691-704 (2012).
    • (2012) Mol Cell Biol , vol.32 , pp. 4691-4704
    • Cheng, S.W.1
  • 16
    • 80054756087 scopus 로고    scopus 로고
    • The Cyclin K/Cdk12 complex maintains genomic stability via regulation of expression of DNA damage response genes
    • Blazek, D. et al. The Cyclin K/Cdk12 complex maintains genomic stability via regulation of expression of DNA damage response genes. Genes Dev 25, 2158-72 (2011).
    • (2011) Genes Dev , vol.25 , pp. 2158-2172
    • Blazek, D.1
  • 17
    • 77958587420 scopus 로고    scopus 로고
    • CDK12 is a transcription elongation-associated CTD kinase, the metazoan ortholog of yeast Ctk1
    • Bartkowiak, B. et al. CDK12 is a transcription elongation-associated CTD kinase, the metazoan ortholog of yeast Ctk1. Genes Dev 24, 2303-16 (2010).
    • (2010) Genes Dev , vol.24 , pp. 2303-2316
    • Bartkowiak, B.1
  • 18
    • 84859791205 scopus 로고    scopus 로고
    • Cyclin K goes with Cdk12 and Cdk13
    • Kohoutek, J. & Blazek, D. Cyclin K goes with Cdk12 and Cdk13. Cell Div 7, 12 (2012).
    • (2012) Cell Div , vol.7 , pp. 12
    • Kohoutek, J.1    Blazek, D.2
  • 19
    • 70449641057 scopus 로고    scopus 로고
    • Progression through the RNA polymerase II CTD cycle
    • Buratowski, S. Progression through the RNA polymerase II CTD cycle. Mol Cell 36, 541-6 (2009).
    • (2009) Mol Cell , vol.36 , pp. 541-546
    • Buratowski, S.1
  • 20
    • 70249104647 scopus 로고    scopus 로고
    • Defining mechanisms that regulate RNA polymerase II transcription in vivo
    • Fuda, N. J., Ardehali, M. B. & Lis, J. T. Defining mechanisms that regulate RNA polymerase II transcription in vivo. Nature 461, 186-92 (2009).
    • (2009) Nature , vol.461 , pp. 186-192
    • Fuda, N.J.1    Ardehali, M.B.2    Lis, J.T.3
  • 21
    • 84902603155 scopus 로고    scopus 로고
    • RNA polymerase II transcription elongation and Pol II CTD Ser2 phosphorylation: A tail of two kinases
    • Bowman, E. A. & Kelly, W. G. RNA polymerase II transcription elongation and Pol II CTD Ser2 phosphorylation: A tail of two kinases. Nucleus 5, 224-36 (2014).
    • (2014) Nucleus , vol.5 , pp. 224-236
    • Bowman, E.A.1    Kelly, W.G.2
  • 22
    • 84904343427 scopus 로고    scopus 로고
    • The structure and substrate specificity of human Cdk12/Cyclin K
    • Bosken, C. A. et al. The structure and substrate specificity of human Cdk12/Cyclin K. Nat Commun 5, 3505 (2014).
    • (2014) Nat Commun , vol.5 , pp. 3505
    • Bosken, C.A.1
  • 23
    • 84923196896 scopus 로고    scopus 로고
    • Characterization of human cyclin-dependent kinase 12 (CDK12) and CDK13 complexes in C-terminal domain phosphorylation, gene transcription, and RNA processing
    • Liang, K. et al. Characterization of human cyclin-dependent kinase 12 (CDK12) and CDK13 complexes in C-terminal domain phosphorylation, gene transcription, and RNA processing. Mol Cell Biol 35, 928-38 (2015).
    • (2015) Mol Cell Biol , vol.35 , pp. 928-938
    • Liang, K.1
  • 24
    • 84922118253 scopus 로고    scopus 로고
    • Expression, purification, and identification of associated proteins of the full-length hCDK12/CyclinK complex
    • Bartkowiak, B. & Greenleaf, A. L. Expression, purification, and identification of associated proteins of the full-length hCDK12/CyclinK complex. J Biol Chem 290, 1786-95 (2015).
    • (2015) J Biol Chem , vol.290 , pp. 1786-1795
    • Bartkowiak, B.1    Greenleaf, A.L.2
  • 25
    • 84893936668 scopus 로고    scopus 로고
    • 3′ end formation of pre-mRNA and phosphorylation of Ser2 on the RNA polymerase II CTD are reciprocally coupled in human cells
    • Davidson, L., Muniz, L. & West, S. 3′ end formation of pre-mRNA and phosphorylation of Ser2 on the RNA polymerase II CTD are reciprocally coupled in human cells. Genes Dev 28, 342-56 (2014).
    • (2014) Genes Dev , vol.28 , pp. 342-356
    • Davidson, L.1    Muniz, L.2    West, S.3
  • 26
    • 84919665147 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 12 increases 3′ end processing of growth factor-induced c-FOS transcripts
    • Eifler, T. T. et al. Cyclin-dependent kinase 12 increases 3′ end processing of growth factor-induced c-FOS transcripts. Mol Cell Biol 35, 468-78 (2015).
    • (2015) Mol Cell Biol , vol.35 , pp. 468-478
    • Eifler, T.T.1
  • 27
    • 33645214031 scopus 로고    scopus 로고
    • Identification and characterization of the CDK12/cyclin L1 complex involved in alternative splicing regulation
    • Chen, H. H., Wang, Y. C. & Fann, M. J. Identification and characterization of the CDK12/cyclin L1 complex involved in alternative splicing regulation. Mol Cell Biol 26, 2736-45 (2006).
    • (2006) Mol Cell Biol , vol.26 , pp. 2736-2745
    • Chen, H.H.1    Wang, Y.C.2    Fann, M.J.3
  • 28
    • 79959838081 scopus 로고    scopus 로고
    • Integrated genomic analyses of ovarian carcinoma
    • Cancer Genome Atlas Research, N. Integrated genomic analyses of ovarian carcinoma. Nature 474, 609-15 (2011).
    • (2011) Nature , vol.474 , pp. 609-615
    • Cancer Genome Atlas Research, N.,1
  • 29
    • 84897457200 scopus 로고    scopus 로고
    • Ovarian cancer-associated mutations disable catalytic activity of CDK12, a kinase that promotes homologous recombination repair and resistance to cisplatin and poly(ADP-ribose) polymerase inhibitors
    • Joshi, P. M., Sutor, S. L., Huntoon, C. J. & Karnitz, L. M. Ovarian cancer-associated mutations disable catalytic activity of CDK12, a kinase that promotes homologous recombination repair and resistance to cisplatin and poly(ADP-ribose) polymerase inhibitors. J Biol Chem 289, 9247-53 (2014).
    • (2014) J Biol Chem , vol.289 , pp. 9247-9253
    • Joshi, P.M.1    Sutor, S.L.2    Huntoon, C.J.3    Karnitz, L.M.4
  • 30
    • 84937622540 scopus 로고    scopus 로고
    • Ovarian carcinoma CDK12 mutations misregulate expression of DNA repair genes via deficient formation and function of the Cdk12/CycK complex
    • Ekumi, K. M. et al. Ovarian carcinoma CDK12 mutations misregulate expression of DNA repair genes via deficient formation and function of the Cdk12/CycK complex. Nucleic Acids Res 43, 2575-89 (2015).
    • (2015) Nucleic Acids Res , vol.43 , pp. 2575-2589
    • Ekumi, K.M.1
  • 31
    • 84892712017 scopus 로고    scopus 로고
    • Genome-wide profiling of genetic synthetic lethality identifies CDK12 as a novel determinant of PARP1/2 inhibitor sensitivity
    • Bajrami, I. et al. Genome-wide profiling of genetic synthetic lethality identifies CDK12 as a novel determinant of PARP1/2 inhibitor sensitivity. Cancer Res 74, 287-97 (2014).
    • (2014) Cancer Res , vol.74 , pp. 287-297
    • Bajrami, I.1
  • 32
    • 84873935155 scopus 로고    scopus 로고
    • Substituted 4-(thiazol-5-yl)-2-(phenylamino)pyrimidines are highly active CDK9 inhibitors: Synthesis, X-ray crystal structures, structure-activity relationship, and anticancer activities
    • Shao, H. et al. Substituted 4-(thiazol-5-yl)-2-(phenylamino)pyrimidines are highly active CDK9 inhibitors: synthesis, X-ray crystal structures, structure-activity relationship, and anticancer activities. J Med Chem 56, 640-59 (2013).
    • (2013) J Med Chem , vol.56 , pp. 640-659
    • Shao, H.1
  • 33
    • 33846483298 scopus 로고    scopus 로고
    • Crystal structure of human cyclin K, a positive regulator of cyclin-dependent kinase 9
    • Baek, K., Brown, R. S., Birrane, G. & Ladias, J. A. Crystal structure of human cyclin K, a positive regulator of cyclin-dependent kinase 9. J Mol Biol 366, 563-73 (2007).
    • (2007) J Mol Biol , vol.366 , pp. 563-573
    • Baek, K.1    Brown, R.S.2    Birrane, G.3    Ladias, J.A.4
  • 34
    • 46949093191 scopus 로고    scopus 로고
    • The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation
    • Baumli, S. et al. The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation. EMBO J 27, 1907-18 (2008).
    • (2008) EMBO J , vol.27 , pp. 1907-1918
    • Baumli, S.1
  • 35
    • 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. & Endicott, J. A. The CDK9 tail determines the reaction pathway of positive transcription elongation factor b. Structure 20, 1788-95 (2012).
    • (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
  • 36
    • 0028157664 scopus 로고
    • Atomic structure of the MAP kinase ERK2 at 2.3 A resolution
    • Zhang, F., Strand, A., Robbins, D., Cobb, M. H. & Goldsmith, E. J. Atomic structure of the MAP kinase ERK2 at 2.3 A resolution. Nature 367, 704-11 (1994).
    • (1994) Nature , vol.367 , pp. 704-711
    • Zhang, F.1    Strand, A.2    Robbins, D.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 37
    • 77953431827 scopus 로고    scopus 로고
    • Crystal structure of HIV-1 Tat complexed with human P-TEFb
    • Tahirov, T. H. et al. Crystal structure of HIV-1 Tat complexed with human P-TEFb. Nature 465, 747-51 (2010).
    • (2010) Nature , vol.465 , pp. 747-751
    • Tahirov, T.H.1
  • 38
    • 16344365524 scopus 로고    scopus 로고
    • A uniform procedure for the purification of CDK7/CycH/MAT1, CDK8/CycC and CDK9/ CycT1
    • Pinhero, R., Liaw, P. & Yankulov, K. A uniform procedure for the purification of CDK7/CycH/MAT1, CDK8/CycC and CDK9/ CycT1. Biol Proced Online 6, 163-172 (2004).
    • (2004) Biol Proced Online , vol.6 , pp. 163-172
    • Pinhero, R.1    Liaw, P.2    Yankulov, K.3
  • 41
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr D Biol Crystallogr 67, 235-42 (2011).
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 42
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J Appl Crystallogr 40, 658-674 (2007).
    • (2007) J Appl Crystallogr , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 43
    • 43749083257 scopus 로고    scopus 로고
    • CHAINSAW: A program for mutating pdb files used as templates in molecular replacement
    • Stein, N. CHAINSAW: a program for mutating pdb files used as templates in molecular replacement. J. Appl. Cryst. 41, 641-643 (2008).
    • (2008) J. Appl. Cryst. , vol.41 , pp. 641-643
    • Stein, N.1
  • 45
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • Murshudov, G. N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr D Biol Crystallogr 67, 355-67 (2011).
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 355-367
    • Murshudov, G.N.1
  • 46
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66, 213-21 (2010).
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 47
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66, 12-21 (2010).
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 12-21
    • Chen, V.B.1


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