ArticleThe Biochemical journal2017
Structure and inhibitor specificity of the PCTAIRE-family kinase CDK16.
Article in The Biochemical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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Who cites it
27 citing papers in PubMed, 58 citations in OpenAlex.
- PP2A and CDK16 antagonistically regulate WIPI2B phosphorylation and neuronal autophagosome biogenesis.iScience · 2026Article
- Cyclins and Cyclin-Dependent Kinases: Structure, Biological Functions, and Innovative Targeting Strategies in Cancer.MedComm · 2026Review
- Long-term enoxaparin use and osteoporosis risk: a real-world cohort study with integrative computational and network toxicology approaches.Journal of translational medicine · 2026Article
- Computer-aided discovery of CDK16 inhibitors: a docking-augmented machine learning regression modelling approach.Journal of computer-aided molecular design · 2026Article
- Structural basis of the cyclin Y/14-3-3 protein-mediated activation of CDK16.Nature communications · 2026Article
- CCNY-mediated phosphorylation and TET2-BACH1-driven DNA demethylation activate PRC1 to augment NSCLC progression.Journal of experimental & clinical cancer research : CR · 2025Article
- MicroRNA 320a-3p up-regulation reduces PD-L1 expression in gastric cancer cells: an experimental and bioinformatic study.Scientific reports · 2025Article
- Cyclin-dependent protein kinases and cell cycle regulation in biology and disease.Signal transduction and targeted therapy · 2025Review
- A Huluwa phosphorylation switch regulates embryonic axis induction.Nature communications · 2024Article
- Insights into the structural and functional activities of forgotten Kinases: PCTAIREs CDKs.Molecular cancer · 2024Review
- Discovery of 3-Amino-1International journal of molecular sciences · 2022Article
- CDK16 promotes the progression and metastasis of triple-negative breast cancer by phosphorylating PRC1.Journal of experimental & clinical cancer research : CR · 2022Article
- PCTAIRE1 promotes mitotic progression and resistance against antimitotic and apoptotic signals.Journal of cell science · 2022Article
- LncRNA HCG18 facilitates melanoma progression by modulating miR-324-5p/CDK16 axis.American journal of translational research · 2022Article
- Serine/Threonine Protein Phosphatase 2A Regulates the Transport of Axonal Mitochondria.Frontiers in cellular neuroscience · 2022Article
- CDK15 promotes colorectal cancer progression via phosphorylating PAK4 and regulating β-catenin/ MEK-ERK signaling pathway.Cell death and differentiation · 2022Article
- Targeting CDK9 for Anti-Cancer Therapeutics.Cancers · 2021Review
- Proteomic investigation of Cbl and Cbl-b in neuroblastoma cell differentiation highlights roles for SHP-2 and CDK16.iScience · 2021Article
- AMPK-dependent activation of the Cyclin Y/CDK16 complex controls autophagy.Nature communications · 2020Article
- Trafficking of Stretch-Regulated TRPV2 and TRPV4 Channels Inferred Through Interactomics.Biomolecules · 2019Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
CDK16 (also known as PCTAIRE1 or PCTK1) is an atypical member of the cyclin-dependent kinase (CDK) family that has emerged as a key regulator of neurite outgrowth, vesicle trafficking and cancer cell proliferation. CDK16 is activated through binding to cyclin Y via a phosphorylation-dependent 14-3-3 interaction and has a unique consensus substrate phosphorylation motif compared with conventional CDKs. To elucidate the structure and inhibitor-binding properties of this atypical CDK, we screened the CDK16 kinase domain against different inhibitor libraries and determined the co-structures of identified hits. We discovered that the ATP-binding pocket of CDK16 can accommodate both type I and type II kinase inhibitors. The most potent CDK16 inhibitors revealed by cell-free and cell-based assays were the multitargeted cancer drugs dabrafenib and rebastinib. An inactive DFG-out binding conformation was confirmed by the first crystal structures of CDK16 in separate complexes with the inhibitors indirubin E804 and rebastinib, respectively. The structures revealed considerable conformational plasticity, suggesting that the isolated CDK16 kinase domain was relatively unstable in the absence of a cyclin partner. The unusual structural features and chemical scaffolds identified here hold promise for the development of more selective CDK16 inhibitors and provide opportunity to better characterise the role of CDK16 and its related CDK family members in various physiological and pathological contexts.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.