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| Cyclin B1 | |
|---|---|
| Name | Cyclin B1 |
| Uniprot | P14635 |
| Omim | 118372 |
| Gene | CCNB1 |
| Organism | Homo sapiens |
Cyclin B1 is a regulatory protein that controls progression through the eukaryotic cell cycle, particularly the transition from G2 phase to mitosis. It forms a complex with cyclin-dependent kinase 1 to trigger mitotic events in organisms ranging from yeast to mammals. Cyclin B1 is studied across multiple fields including cell biology, oncology, and developmental biology.
Cyclin B1 is a member of the cyclin family with a conserved cyclin box that mediates interactions with kinases and substrates; structural analyses reference paradigms from X-ray crystallography, NMR spectroscopy, and models used by groups at institutions like European Molecular Biology Laboratory, Max Planck Society, and Cold Spring Harbor Laboratory. The protein contains a destruction box (D-box) motif recognized by the anaphase-promoting complex co-activator interactions characterized by laboratories including Francis Crick Institute and Johns Hopkins University. Biochemical studies often cite methods from Harvard University, Massachusetts Institute of Technology, Stanford University, and University of California, San Francisco to analyze post-translational modifications such as phosphorylation by Aurora kinase A, Polo-like kinase 1, and dephosphorylation by protein phosphatase 2A. Structural motifs first compared in model organisms such as Saccharomyces cerevisiae, Schizosaccharomyces pombe, Xenopus laevis, and Drosophila melanogaster inform conservation across evolution cited alongside findings from National Institutes of Health funded consortia. Cyclin B1 is subject to ubiquitination by UBE2C and recognition by CDC20 and CDH1 in APC/C-mediated proteolysis, with mechanistic parallels discussed in literature from Institut Pasteur and Weizmann Institute of Science.
Cyclin B1 expression is cell-cycle regulated, rising during S and G2 phases under control of transcription factors documented by researchers at European Research Council-funded groups and institutions such as University of Cambridge, Yale University, and University of Oxford. Promoter analyses reference regulatory inputs from factors studied at Howard Hughes Medical Institute, Cold Spring Harbor Laboratory, and Karolinska Institutet. Post-transcriptional regulation involves microRNAs characterized in studies at Salk Institute, Broad Institute, and University of Toronto; examples of regulatory networks were mapped in collaborations involving Wellcome Trust and Medical Research Council. Cyclin B1 localization shifts from cytoplasm to nucleus via a nuclear export signal and nuclear localization sequence influenced by kinases documented at Imperial College London and University of Chicago. Cell-cycle checkpoints integrating signals from Ataxia telangiectasia mutated, CHK1, and p53 pathways modulate Cyclin B1 levels, with checkpoint studies appearing in work from Dana-Farber Cancer Institute, Memorial Sloan Kettering Cancer Center, and Fred Hutchinson Cancer Center.
Cyclin B1 forms the maturation-promoting factor with CDK1, initiating mitotic processes such as nuclear envelope breakdown, spindle assembly, and chromosome condensation; foundational discoveries are associated with laboratories at Columbia University, University of California, Berkeley, and Princeton University. Its activation triggers phosphorylation cascades involving substrates studied at European Molecular Biology Laboratory, National Cancer Institute, and Johns Hopkins University School of Medicine. Mitotic exit requires Cyclin B1 degradation through APC/C activity; mechanistic insights have been produced by groups at Rockefeller University, University of Pennsylvania, and ETH Zurich. Roles in spindle assembly checkpoint signaling intersect with research from Cold Spring Harbor Laboratory, EMBL-EBI, and Max Delbrück Center for Molecular Medicine. Comparative functional studies in Xenopus egg extracts and yeast cell cycles were pioneered by teams at University of Geneva and University of Cologne.
Cyclin B1 interacts directly with CDK1 and with regulators including Wee1, Myt1, CDC25C, and members of the APC/C complex; interaction mapping has been advanced by proteomics centers at European Bioinformatics Institute, ProteomeXchange, and Massachusetts General Hospital. It participates in pathways that intersect with MAPK signaling studied at Cold Spring Harbor Laboratory and Institute of Cancer Research, and with DNA damage response pathways involving BRCA1, BRCA2, and RAD51 as characterized by researchers at Cold Spring Harbor, Memorial Sloan Kettering, and Royal Marsden Hospital. Cross-talk with apoptosis regulators such as BCL2 family members and mitotic kinases like Aurora B has been reported from studies at Yale Cancer Center, MD Anderson Cancer Center, and Vanderbilt University Medical Center. Large-scale interaction screens including yeast two-hybrid and mass spectrometry approaches were contributed by European Proteomics Association collaborators and consortia including Human Protein Atlas teams.
Aberrant Cyclin B1 expression is associated with multiple cancers studied at National Cancer Institute, Memorial Sloan Kettering Cancer Center, MD Anderson Cancer Center, and Royal Marsden Hospital; tumor types include breast, lung, colorectal, ovarian, and prostate cancers reported in clinical series from Mayo Clinic, Cleveland Clinic, and Johns Hopkins Hospital. Overexpression correlates with prognosis metrics used in trials overseen by European Society for Medical Oncology and American Society of Clinical Oncology. Autoantibodies to Cyclin B1 have been described in paraneoplastic syndromes studied at Stanford Hospital and UCSF Medical Center. Cyclin B1 dysregulation contributes to genomic instability linked to defects in BRCA1-mediated repair and chromosomal segregation errors reported by groups at Cold Spring Harbor Laboratory and Sanger Institute. Therapeutic strategies targeting CDK1/Cyclin B1 axis are explored in preclinical studies at GlaxoSmithKline, Novartis, Pfizer, and academic centers such as Dana-Farber.
Tools for Cyclin B1 research include antibodies developed by vendors collaborating with European Molecular Biology Laboratory, fluorescent fusion constructs used in live-cell imaging at Max Planck Institute for Biochemistry and Karolinska Institutet, and CRISPR/Cas9-mediated gene editing employed in labs at Broad Institute and Wellcome Sanger Institute. Model systems range from yeast models developed at University of Edinburgh to vertebrate models in labs at University of Tokyo and University of Sydney. High-content screens, kinase assays, and cell-cycle reporters are standard in facilities such as Friedrich Miescher Institute and RIKEN, with data integration by groups at EMBL-EBI and European Bioinformatics Institute. Clinical translational studies linking Cyclin B1 to patient outcomes have been conducted at Karolinska University Hospital, Royal Free Hospital, and Mount Sinai Health System.
Category:Cell cycle proteins