ArticleMolecular biology of the cell1998
Human and yeast cdk-activating kinases (CAKs) display distinct substrate specificities.
Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed.
- The non-canonical CDK2 activator SPY1 uses separable mechanisms to activate phosphorylated and unphosphorylated CDK2.The Biochemical journal · 2026Article
- uORF-mediated translational control of CAK and Cdk activation in response to low nutrients in yeast.EMBO reports · 2026Article
- Cdk activation by phosphorylation: linking growth signals to cell cycle control.Biochemical Society transactions · 2025Review
- Non-canonical CDK6 activity promotes cilia disassembly by suppressing axoneme polyglutamylation.The Journal of cell biology · 2025Article
- Meiotic Cell Cycle Progression in Mouse Oocytes: Role of Cyclins.International journal of molecular sciences · 2023Review
- Immortalization of primary cells derived from the endangered Ryukyu long-furred rat.In vitro cellular & developmental biology. Animal · 2023Article
- CDKs in Sarcoma: Mediators of Disease and Emerging Therapeutic Targets.International journal of molecular sciences · 2020Review
- The G2-to-M transition from a phosphatase perspective: a new vision of the meiotic division.Cell division · 2020Review
- Strategies to generate functionally normal neutrophils to reduce infection and infection-related mortality in cancer chemotherapy.Pharmacology & therapeutics · 2019Review
- Breaking Bad: How Viruses Subvert the Cell Cycle.Frontiers in cellular and infection microbiology · 2018Review
- Cyclin-Dependent Kinase-Dependent Phosphorylation of Sox2 at Serine 39 Regulates Neurogenesis.Molecular and cellular biology · 2017Article
- Article
- Cdk2 catalytic activity is essential for meiotic cell division in vivo.The Biochemical journal · 2016Article
- Different types of cell cycle- and apoptosis-related gene expressions alter in corticosteroid-, vincristine-, and melphalan-resistant u-266 multiple myeloma cell lines.Turkish journal of haematology : official journal of Turkish Society of Haematology · 2014Article
- Cdc37 engages in stable, S14A mutation-reinforced association with the most atypical member of the yeast kinome, Cdk-activating kinase (Cak1).Cell stress & chaperones · 2014Article
- Article
- CDK4 T172 phosphorylation is central in a CDK7-dependent bidirectional CDK4/CDK2 interplay mediated by p21 phosphorylation at the restriction point.PLoS genetics · 2013Article
- Slowly progressing nucleotide excision repair in trichothiodystrophy group A patient fibroblasts.Molecular and cellular biology · 2011Article
- Zinc requirement during meiosis I-meiosis II transition in mouse oocytes is independent of the MOS-MAPK pathway.Biology of reproduction · 2011Article
- Recombinant Leishmania mexicana CRK3:CYCA has protein kinase activity in the absence of phosphorylation on the T-loop residue Thr178.Molecular and biochemical parasitology · 2010Article
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5 authors.
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Abstract
Cell cycle progression is controlled by the sequential functions of cyclin-dependent kinases (cdks). Cdk activation requires phosphorylation of a key residue (on sites equivalent to Thr-160 in human cdk2) carried out by the cdk-activating kinase (CAK). Human CAK has been identified as a p40(MO15)/cyclin H/MAT1 complex that also functions as part of transcription factor IIH (TFIIH) where it phosphorylates multiple transcriptional components including the C-terminal domain (CTD) of the large subunit of RNA polymerase II. In contrast, CAK from budding yeast consists of a single polypeptide (Cak1p), is not a component of TFIIH, and lacks CTD kinase activity. Here we report that Cak1p and p40(MO15) have strikingly different substrate specificities. Cak1p preferentially phosphorylated monomeric cdks, whereas p40(MO15) preferentially phosphorylated cdk/cyclin complexes. Furthermore, p40(MO15) only phosphorylated cdk6 bound to cyclin D3, whereas Cak1p recognized monomeric cdk6 and cdk6 bound to cyclin D1, D2, or D3. We also found that cdk inhibitors, including p21(CIP1), p27(KIP1), p57(KIP2), p16(INK4a), and p18(INK4c), could block phosphorylation by p40(MO15) but not phosphorylation by Cak1p. Our results demonstrate that although both Cak1p and p40(MO15) activate cdks by phosphorylating the same residue, the structural mechanisms underlying the enzyme-substrate recognition differ greatly. Structural and physiological implications of these findings will be discussed.
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