ArticleViruses2013
The cyclin-dependent kinase ortholog pUL97 of human cytomegalovirus interacts with cyclins.
Article in Viruses, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Baculoviruses exploit the mitotic kinase CDK1 to disrupt the nuclear lamina.PLoS pathogens · 2026Article
- Article
- Review
- Review
- Highly Conserved Interaction Profiles between Clinically Relevant Mutants of the Cytomegalovirus CDK-like Kinase pUL97 and Human Cyclins: Functional Significance of Cyclin H.International journal of molecular sciences · 2022Article
- Functional Relevance of the Interaction between Human Cyclins and the Cytomegalovirus-Encoded CDK-Like Protein Kinase pUL97.Viruses · 2021Article
- The Cytomegalovirus Protein Kinase pUL97:Host Interactions, Regulatory Mechanisms and Antiviral Drug Targeting.Microorganisms · 2020Review
- Human cytomegaloviral multifunctional protein kinase pUL97 impairs zebrafish embryonic development and increases mortality.Scientific reports · 2019Article
- Cyclins B1, T1, and H differ in their molecular mode of interaction with cytomegalovirus protein kinase pUL97.The Journal of biological chemistry · 2019Article
- Article
- P-TEFb goes viral.Inside the cell · 2016Review
- Enhanced neutrophil activity is associated with shorter time to tumor progression in glioblastoma patients.Oncoimmunology · 2016Article
- ELM 2016--data update and new functionality of the eukaryotic linear motif resource.Nucleic acids research · 2016Article
- The Interaction between Cyclin B1 and Cytomegalovirus Protein Kinase pUL97 is Determined by an Active Kinase Domain.Viruses · 2015Article
- Differential properties of cytomegalovirus pUL97 kinase isoforms affect viral replication and maribavir susceptibility.Journal of virology · 2014Article
- Human cytomegalovirus replication is strictly inhibited by siRNAs targeting UL54, UL97 or UL122/123 gene transcripts.PloS one · 2014Article
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Authors and funding
7 authors.
Funding
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Abstract
The human cytomegalovirus (HCMV)-encoded protein kinase, pUL97, is considered a cyclin-dependent kinase (CDK) ortholog, due to shared structural and functional characteristics. The primary mechanism of CDK activation is binding to corresponding cyclins, including cyclin T1, which is the usual regulatory cofactor of CDK9. This study provides evidence of direct interaction between pUL97 and cyclin T1 using yeast two-hybrid and co-immunoprecipitation analyses. Confocal immunofluorescence revealed partial colocalization of pUL97 with cyclin T1 in subnuclear compartments, most pronounced in viral replication centres. The distribution patterns of pUL97 and cyclin T1 were independent of HCMV strain and host cell type. The sequence domain of pUL97 responsible for the interaction with cyclin T1 was between amino acids 231-280. Additional co-immunoprecipitation analyses showed cyclin B1 and cyclin A as further pUL97 interaction partners. Investigation of the pUL97-cyclin T1 interaction in an ATP consumption assay strongly suggested phosphorylation of pUL97 by the CDK9/cyclin T1 complex in a substrate concentration-dependent manner. This is the first demonstration of interaction between a herpesviral CDK ortholog and cellular cyclins.
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