Cyclin dependent kinase activating kinases

Current Opinion in Cell Biology

Volumn 8, Issue 6, 1996, Pages 788-794

  Sclafani, Robert A ^a  

^a UNIVERSITY OF COLORADO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE;

CELL CYCLE; ENZYME PHOSPHORYLATION; GENETIC TRANSCRIPTION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; REGULATORY MECHANISM; REVIEW;

EID: 0030561404     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(96)80079-2     Document Type: Article

References (35)

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3. Fesquet D, Labbé J-C, Derancourt J, Capony J-P, Galas S, Girard F, Lorca T, Shuttleworth J, Dorée M, Cavadore J-C. The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr161 and its homologues. EMBO J. 12:1993;3111-3121.
4. cdc2. EMBO J. 12:1993;3123-3132.
5. Morgan DO. Principles of CDK regulation. Nature. 374:1995;131-134.
6. Lees E. Cyclin dependent kinase regulation. Curr Opin Cell Biol. 7:1995;773-780.
7. Devault A, Martinez AM, Fesquet D, Labbe JC, Morin N, Tassan JP, Nigg EA, Cavadore JC, Doree M. MAT1 ('menage à trois') a new RING finger protein subunit stabilizing cyclin-H - cdk7 complexes in starfish and Xenopus CAK. of special interest EMBO J. 14:1995;5027-5036 The study isolates and characterizes the MAT1 protein as a RING-finger protein that acts in the assembly of CDK7 - cyclin H complexes from starfish and frogs in an in vitro reticulocyte lysate system. As starfish MAT1 is not able to substitute for frog MAT1 in assembly of these complexes, the RING finger may not be the site of interaction.
8. Tassan JP, Jaquenoud M, Fry AM, Frutiger S, Hughes GJ, Nigg EA. In vitro assembly of a functional human CDK7 - cyclin H complex requires MAT1, a novel 36 kDa RING finger protein. of special interest EMBO J. 14:1995;5608-5617 Similar to the studies discussed in [7]. Human MAT1 protein is shown to be an assembly factor for CDK7 - cyclin H complexes. In addition, the RING-finger domain is shown to be dispensable for MAT1 function.
9. Fischer RP, Jin P, Chamberlin HM, Morgan DO. Alternative mechanisms of CAK assembly require an assembly factor or an activating kinase. of outstanding interest Cell. 83:1995;47-57 Two pathways are shown to exist for regulating the assembly of CDK7 - cyclin H complexes, namely phosphorylation on Thr170 by another kinase, or binding of MAT1 protein. Evidence is also presented for a positive feedback loop in that CDK2 - cyclin A can act as this other kinase in vitro.
10. Gerber MR, Farrell A, Deshaies RJ, Herskowitz I, Morgan DO. Cdc37 is required for association of the protein kinase Cdc28 with G1 and mitotic cyclins. Proc Natl Acad Sci USA. 92:1995;4651-4655.
11. Feaver WJ, Gileadi O, Li Y, Kornberg RD. Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK. Cell. 79:1994;1103-1109.
12. Serizawa H, Makela TP, Conaway JW, Conaway RC, Weinberg RA, Young RA. Association of Cdk-activating kinase subunits with transcription factor TFIIH. Nature. 374:1995;280-282.
13. Guzder SN, Habraken Y, Sung P, Prakash L, Prakash S. Reconstitution of yeast nucleotide excision repair with purified rad proteins, replication protein A, and transcription factor TFIIH. J Biol Chem. 270:1995;12973-12976.
14. Makela TP, Parvin JD, Kim J, Huber LJ, Sharp PA, Weinberg RA. A kinase-deficient transcription factor TFIIH is functional in basal and activated transcription. of special interest Proc Natl Acad Sci USA. 92:1995;5174-5178 CAK and CTD-kinase may be different because biochemical CDK - cyclin H heterogeneity exists. Different pools of kinases with different substrate specificities are demonstrated.
15. Shlekhattar I, Mermelstein F, Fisher RP, Drapkin R, Dynlacht B, Wessling HC, Morgan DO, Reinberg D. Cdk-activating kinase complex is a component of human transcription factor TFIIH. of special interest Nature. 374:1995;283-287 As in [14], biochemical evidence is presented that CAK and CTD-kinase may be different, in this case because lower molecular weight CDK7 - cyclin H complexes are shown to have CAK but not CTD-kinase activity.
16. Sterner DE, Lee JM, Hardin SE, Greenleaf AL. The yeast carboxyl-terminal domain kinase CTDK-I is a divergent cyclin - cyclin-dependent kinase complex. Mol Cell Biol. 15:1995;5716-5724.
17. Buck V, Russell P, Millar JBA. Identification of a cdk-activating kinase in fission yeast. of outstanding interest EMBO J. 14:1995;6173-6183 Describes a genetic, biochemical and physiological analysis of the role of the fission yeast CDK7 homolog, Mop1 or Crk1. Despite its elegant genetic analysis, however, the study cannot conclude that CDK7 acts as CAK in vivo because a transcriptional defect would mask a cell cycle defect. See also [18].
18. Damagnez V, Makela TP, Cattarel G. Schizosaccharomyces pombe Mop1 - Mcs2 is related to mammalian CAK. of outstanding interest EMBO J. 14:1995;6164-6172 Similar to the studies described in [17], but also shows that human and yeast CDK7 and cyclin H homologs can bind each other in the two-hybrid system, and that human CDK7 can complement a deletion of mop1.
19. Molz L, Beach D. Characterisation of the fission yeast mcs2 cyclin and its associated protein kinase activity. EMBO J. 12:1993;1723-1732.
20. of special interest Cismowski MJ, Laff GM, Solomon MJ, Reed SI. KIN28 encodes a C-terminal domain kinase that controls mRNA transcription in Saccharomyces cerevisiae but lacks cyclin-dependent kinase-activating kinase (CAK) activity. of outstanding interest Mol Cell Biol. 15:1995;2983-2992 This very important study provides the first clue that CDK7 may not act as CAK in vivo. Kin28, which is the budding yeast CDK7 homolog, does not act as CAK in the cell and only acts as the CTD-kinase (see also [21]). The fission yeast studies [17,18] were unable to separate these two roles.
21. Valay JG, Simon M, Dubois MF, Bensaude O, Facca C, Faye G. The KIN28 Gene is required both RNA polymerase II mediated transcription and phosphorylation of the Rpb2p CTD. of special interest J Mol Biol. 249:1995;535-544 The theory that Kin28, which is the budding yeast CDK7 homolog, has a role mainly as a transcriptional regulator in vivo is supported by this elegant molecular genetic analysis.
22. cdc2 kinase at the G1/S and G2/M transitions of the cell cycle: identification of major phosphorylation sites. EMBO J. 10:1991;305-316.
23. Gu Y, Rosenblatt J, Morgan DO. Cell regulation of CDK2 activity by phosphorylation of T160 and Tyr15. EMBO J. 11:1992;3995-4005.
24. Tassan J-P, Schultz SJ, Bartek J, Nigg EA. Cell cycle analysis of the activity, subcellular localization, and subunit composition of human CAK (CDK-activating kinase). J Cell Biol. 127:1994;467-478.
25. MO15. J Cell Sci. 107:1994;2789-2799.
26. Aprelikova O, Xiong Y, Liu ET. Both p16 and p21 families of cyclin-dependent kinase (CDK) inhibitors block the phosphorylation of cyclin-dependent kinases by the CDK-activating kinase. of special interest J Biol Chem. 270:1995;18195-18197 Provides an explanation for how the apparent lack of cell cycle regulation of CAK might still lead to cell cycle regulation of CDKs. In this model, CAK is active throughout the cell cycle, but is prevented from activating CDKs by the CDIs.
27. Fisher RP, Morgan DO. A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase. Cell. 78:1994;713-724.
28. Makela TP, Tassan JP, Nigg EA, Frutiger S, Hughes GJ, Weinberg RA. A cyclin associated with the CDK-activating kinase MO15. Nature. 371:1994;254-257.
29. Desai D, Wessling HC, Fischer RP, Morgan DO. The effect of phosphorylation by CAK on cyclin binding by CDC2 and CDK2. of special interest Mol Cell Biol. 15:1995;345-350 A thorough biochemical study that shows that most CDK - cyclin complexes, except for CDC2 - cyclin A, can form without phosphorylation by CAK.
30. Connell-Crowley L, Solomon MJ, Wei N, Harper JW. Phosphorylation independent activation of human cyclin-dependent kinase 2 by cyclin A in vitro. Mol Biol Cell. 4:1993;79-92.
31. 1 cyclin-dependent kinases. Genes Dev. 9:1995;1149-1163.
32. 160 by the cyclin-dependent kinase-interacting phosphatase KAP in the absence of cyclin. of special interest Science. 270:1995;90-93 In addition to [26], this study also provides a possible mechanism for Thr160-dependent CDK regulation by demonstrating Thr160 dephosphorylation by the phosphatase KAP.
33. Kaldis P, Sutton A, Solomon MJ. The Cdk-activating kinase (CAK) from budding yeast. Cell. 86:1996;553-564 This paper, together with [34,35], shows that Cak1/Civ1 is the physiological CAK of budding yeast. Cak1/Civ1 is shown to be neither a CDK7 homolog nor even a CDK homolog. Cak1/Civ1 is the product of an essential gene. Unlike CDKs, Cak1/Civ1 is active as a monomer when expressed in bacteria. These results raise the intriguing possibility that CDK7 - cyclin H in other organisms is not the physiological CAK, and may only be important for transcriptional regulation. However, it is still possible that budding yeast represents the exception and not the rule. Only time (and more experiments) will tell.
34. Thuret J-Y, Valay J-G, Faye G, Mann C. Civ1 (CAK in vivo), a novel Cdk-activating kinase. of outstanding interest Cell. 86:1996;565-576 See annotation [33].
35. Espinoza FH, Farrell A, Bromage-Erdjument H, Tempst P, Morgan DO. A cyclin-dependent kinase-activating kinase (CAK) in budding yeast unrelated to vertebrate CAK. of outstanding interest Science. 273:1996;1714-1717 See annotation [33].