ArticlePloS one2011
Phosphorylation of AIB1 at mitosis is regulated by CDK1/CYCLIN B.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 26 citations in OpenAlex.
- Kinesin family member 4A: a potential predictor for progression of human oral cancer.PloS one · 2013Trial
- Targeting CDK1 in cancer: mechanisms and implications.NPJ precision oncology · 2023Review
- AIB1/SRC-3/NCOA3 function in estrogen receptor alpha positive breast cancer.Frontiers in endocrinology · 2023Review
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- Ubiquitin signaling in cell cycle control and tumorigenesis.Cell death and differentiation · 2021Review
- Centromere Protein N Participates in Cellular Proliferation of Human Oral Cancer by Cell-Cycle Enhancement.Journal of Cancer · 2019Article
- Nucleolar and Spindle Associated Protein 1 (NUSAP1) Inhibits Cell Proliferation and Enhances Susceptibility to Epirubicin In Invasive Breast Cancer Cells by Regulating Cyclin D Kinase (CDK1) and DLGAP5 Expression.Medical science monitor : international medical journal of experimental and clinical research · 2018Article
- Critical role of deoxynucleotidyl transferase terminal interacting protein 1 in oral cancer.Laboratory investigation; a journal of technical methods and pathology · 2018Article
- Regulation of steroid hormone receptors and coregulators during the cell cycle highlights potential novel function in addition to roles as transcription factors.Nuclear receptor signaling · 2016Review
- Kinesin family member 14 in human oral cancer: A potential biomarker for tumoral growth.Biochemistry and biophysics reports · 2015Article
- ANGPTL3 is a novel biomarker as it activates ERK/MAPK pathway in oral cancer.Cancer medicine · 2015Article
- ATF7 is stabilized during mitosis in a CDK1-dependent manner and contributes to cyclin D1 expression.Cell cycle (Georgetown, Tex.) · 2015Article
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- The fine-tuning of TRAF2-GSTP1-1 interaction: effect of ligand binding and in situ detection of the complex.Cell death & disease · 2014Article
- Article
- Cyclin-dependent kinase 1-dependent phosphorylation of cAMP response element-binding protein decreases chromatin occupancy.The Journal of biological chemistry · 2013Article
- Annexin A10 in human oral cancer: biomarker for tumoral growth via G1/S transition by targeting MAPK signaling pathways.PloS one · 2012Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundAlthough the AIB1 oncogene has an important role during the early phase of the cell cycle as a coactivator of E2F1, little is known about its function during mitosis. METHODOLOGY/PRINCIPAL
findingsMitotic cells isolated by nocodazole treatment as well as by shake-off revealed a post-translational modification occurring in AIB1 specifically during mitosis. This modification was sensitive to the treatment with phosphatase, suggesting its modification by phosphorylation. Using specific inhibitors and in vitro kinase assays we demonstrate that AIB1 is phosphorylated on Ser728 and Ser867 by Cdk1/cyclin B at the onset of mitosis and remains phosphorylated until exit from M phase. Differences in the sensitivity to phosphatase inhibitors suggest that PP1 mediates dephosphorylation of AIB1 at the end of mitosis. The phosphorylation of AIB1 during mitosis was not associated with ubiquitylation or degradation, as confirmed by western blotting and flow cytometry analysis. In addition, luciferase reporter assays showed that this phosphorylation did not alter the transcriptional properties of AIB1. Importantly, fluorescence microscopy and sub-cellular fractionation showed that AIB1 phosphorylation correlated with the exclusion from the condensed chromatin, thus preventing access to the promoters of AIB1-dependent genes. Phospho-specific antibodies developed against Ser728 further demonstrated the presence of phosphorylated AIB1 only in mitotic cells where it was localized preferentially in the periphery of the cell.
conclusionsCollectively, our results describe a new mechanism for the regulation of AIB1 during mitosis, whereby phosphorylation of AIB1 by Cdk1 correlates with the subcellular redistribution of AIB1 from a chromatin-associated state in interphase to a more peripheral localization during mitosis. At the exit of mitosis, AIB1 is dephosphorylated, presumably by PP1. This exclusion from chromatin during mitosis may represent a mechanism for governing the transcriptional activity of AIB1.
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