The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.
Forkhead Box M1B Transcriptional Activity Requires Binding of Cdk-Cyclin Complexes for Phosphorylation-Dependent Recruitment of p300/CBP Coactivators
Open accessAbstract
Previous liver regeneration studies demonstrated that the mouse forkhead box M1B (FoxM1B) transcription factor regulates hepatocyte proliferation through expression of cell cycle genes that stimulate cyclin-dependent kinase 2 (Cdk2) and Cdk1 activity. In this study, we demonstrated that disruption of the FoxM1B Cdk1/2 phosphorylation site at Thr residue 596 significantly reduced both FoxM1B transcriptional activity and Cdk phosphorylation of the FoxM1B T596A mutant protein in vivo. Retention of this FoxM1B 596 Cdk phosphorylation site was found to be essential for recruiting the histone acetyltransferase CREB binding protein (CBP) to the FoxM1B transcriptional activation domain. Consistent with these findings, dominant negative Cdk1 protein significantly reduced FoxM1B transcriptional activity and inhibited FoxM1B recruitment of the CBP coactivator protein. Likewise, Cdc25B-mediated stimulation of Cdk activity together with elevated levels of the CBP coactivator protein provided a 6.2-fold synergistic increase in FoxM1B transcriptional activity. Furthermore, mutation of the FoxM1B Leu 641 residue within an LXL motif (residues 639 to 641) inhibited recruitment of Cdk-cyclin complexes and caused significant reduction in both FoxM1B transcriptional activity and in vivo Cdk phosphorylation of the FoxM1B Thr 596 residue. We demonstrated that FoxM1B transcriptional activity requires binding of either S-phase or M-phase Cdk-cyclin complexes to mediate efficient Cdk phosphorylation of the FoxM1B Thr 596 residue, which is essential for recruitment of p300/CBP coactivator proteins.
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Cites
Akt Promotes Cell Survival by Phosphorylating and Inhibiting a Forkhead Transcription Factor
Brunet, A., Bonni, A., Zigmond, M. J., Lin, M. Z., Juo, P., Hu, L. S., Anderson, M. J., Arden, K. C., Blenis, J., & Greenberg, M. E. (1999) · Cell · doi:10.1016/s0092-8674(00)80595-4 · Cited by 5,594
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Phosphorylated CREB binds specifically to the nuclear protein CBP
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Mitotic kinases as regulators of cell division and its checkpoints
Nigg, E. A. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35048096 · Cited by 1,547
Cooperation between Complexes that Regulate Chromatin Structure and Transcription
Narlikar, G. J., Fan, H.-Y., & Kingston, R. E. (2002) · Cell · doi:10.1016/s0092-8674(02)00654-2 · Cited by 1,484
AFX-like Forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1
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Cited by
Forkhead box proteins: tuning forks for transcriptional harmony.
Lam, E. W.-F., Brosens, J. J., Gomes, A. R., & Koo, C.-Y. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3539 · Cited by 684
Wang, I.-C., Chen, Y.-J., Hughes, D., Petrovic, V., Major, M. L., Park, H. J., Tan, Y., Ackerson, T., & Costa, R. H. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.24.10875-10894.2005 · Cited by 627
Self-citationAnders, L., Ke, N., Hydbring, P., Choi, Y. J., Widlund, H. R., Chick, J. M., Zhai, H., Vidal, M., Gygi, S. P., Braun, P., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.10.001 · Cited by 543
FoxM1: At the crossroads of ageing and cancer
Laoukili, J., Stahl, M., & Medema, R. H. (2007) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2006.08.006 · Cited by 377
Cell cycle transcription control: DREAM/MuvB and RB-E2F complexes.
Fischer, M., & Müller, G. A. (2017) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2017.1360836 · Cited by 255
Metadata
- Authors
- Major, M. L., Lepe, R., & Costa, R. H.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2004-04
- Volume
- 24
- Issue
- 7
- Pages
- 2649-2661
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2161425163
- Cited by
- 266
- References
- 68
- FWCI
- 4.37
- Type
- journal article
- Language
- en
- Open access
- green
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