CG&D
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Li, W.
Right arrow Articles by Dai, W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Li, W.
Right arrow Articles by Dai, W.
Cell Growth & Differentiation Vol. 10, 769-775, November 1999
© 1999 American Association for Cancer Research


Articles

BUBR1 Phosphorylation Is Regulated during Mitotic Checkpoint Activation1

Wenqing Li, Zhengdao Lan, Huiyun Wu, Shechao Wu, Juliana Meadows, Jie Chen, Veronica Zhu and Wei Dai2

Division of Hematology and Oncology, Department of Internal Medicine, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267

Abstract

Eukaryotic cells have evolved a mechanism that delays the progression of mitosis until condensed chromosomes are properly positioned on the mitotic spindle. To understand the molecular basis of such monitoring mechanism in human cells, we have been studying genes that regulate the mitotic checkpoint. Our early studies have led to the cloning of a full-length cDNA encoding MAD3-like protein (also termed BUBR1/MAD3/SSK1). Dot blot analyses show that BUBR1 mRNA is expressed in tissues with a high mitotic index but not in differentiated tissues. Western blot analyses show that in asynchronous cells, BUBR1 protein primarily exhibits a molecular mass of 120 kDa, and its expression is detected in most cell lines examined. In addition, BUBR1 is present during various stages of the cell cycle. As cells enter later S and G2, BUBR1 levels are increased significantly. Nocodazole-arrested mitotic cells obtained by mechanical shake-off contain BUBR1 antigen with a slower mobility on denaturing SDS gels. Phosphatase treatment restores the slowly migrating band to the interphase state, indicating that the slow mobility of the BUBR1 antigen is attributable to phosphorylation. Furthermore, purified recombinant His6-BUBR1 is capable of autophosphorylation. Our studies indicate that BUBR1 phosphorylation status is regulated during spindle disruption. Considering its strong homology to BUB1 protein kinase, BUBR1 may also play an important role in mitotic checkpoint control by phosphorylation of a critical cellular component(s) of the mitotic checkpoint pathway.




This article has been cited by other articles:


Home page
J Biol ChemHome page
F. Yang, L. Hu, C. Chen, J. Yu, C. B. O'Connell, A. Khodjakov, M. Pagano, and W. Dai
BubR1 Is Modified by Sumoylation during Mitotic Progression
J. Biol. Chem., February 10, 2012; 287(7): 4875 - 4882.
[Abstract] [Full Text] [PDF]


Home page
J. Pharmacol. Exp. Ther.Home page
L. M. Greene, S. M. Nathwani, S. A. Bright, D. Fayne, A. Croke, M. Gagliardi, A. M. McElligott, L. O'Connor, M. Carr, N. O. Keely, et al.
The Vascular Targeting Agent Combretastatin-A4 and a Novel cis-Restricted {beta}-Lactam Analogue, CA-432, Induce Apoptosis in Human Chronic Myeloid Leukemia Cells and Ex Vivo Patient Samples Including Those Displaying Multidrug Resistance
J. Pharmacol. Exp. Ther., November 1, 2010; 335(2): 302 - 313.
[Abstract] [Full Text] [PDF]


Home page
Molecular Cancer TherapeuticsHome page
V. Appierto, P. Tiberio, E. Cavadini, P. Casalini, G. Cappelletti, and F. Formelli
Antimitotic effect of the retinoid 4-oxo-fenretinide through inhibition of tubulin polymerization: a novel mechanism of retinoid growth-inhibitory activity
Mol. Cancer Ther., December 1, 2009; 8(12): 3360 - 3368.
[Abstract] [Full Text] [PDF]


Home page
J Biol ChemHome page
Y. W. Chan, K. F. On, W. M. Chan, W. Wong, H. O. Siu, P. M. Hau, and R. Y. C. Poon
The Kinetics of p53 Activation Versus Cyclin E Accumulation Underlies the Relationship between the Spindle-assembly Checkpoint and the Postmitotic Checkpoint
J. Biol. Chem., June 6, 2008; 283(23): 15716 - 15723.
[Abstract] [Full Text] [PDF]


Home page
Cancer Res.Home page
R. Aneja, M. Liu, C. Yates, J. Gao, X. Dong, B. Zhou, S. N. Vangapandu, J. Zhou, and H. C. Joshi
Multidrug Resistance-Associated Protein-Overexpressing Teniposide-Resistant Human Lymphomas Undergo Apoptosis by a Tubulin-Binding Agent
Cancer Res., March 1, 2008; 68(5): 1495 - 1503.
[Abstract] [Full Text] [PDF]


Home page
Mol. Pharmacol.Home page
L. M. Greene, G. Campiani, M. Lawler, D. C. Williams, and D. M. Zisterer
BubR1 Is Required for a Sustained Mitotic Spindle Checkpoint Arrest in Human Cancer Cells Treated with Tubulin-Targeting Pyrrolo-1,5-Benzoxazepines
Mol. Pharmacol., February 1, 2008; 73(2): 419 - 430.
[Abstract] [Full Text] [PDF]


Home page
J Biol ChemHome page
S. Matsumura, F. Toyoshima, and E. Nishida
Polo-like Kinase 1 Facilitates Chromosome Alignment during Prometaphase through BubR1
J. Biol. Chem., May 18, 2007; 282(20): 15217 - 15227.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
W. Tao, V. J. South, R. E. Diehl, J. P. Davide, L. Sepp-Lorenzino, M. E. Fraley, K. L. Arrington, and R. B. Lobell
An Inhibitor of the Kinesin Spindle Protein Activates the Intrinsic Apoptotic Pathway Independently of p53 and De Novo Protein Synthesis
Mol. Cell. Biol., January 15, 2007; 27(2): 689 - 698.
[Abstract] [Full Text] [PDF]


Home page
Mol Cancer ResHome page
C. Guo, G. Wu, J. L. Chin, G. Bauman, M. Moussa, F. Wang, N. M. Greenberg, S. S. Taylor, and J. W. Xuan
Bub1 Up-Regulation and Hyperphosphorylation Promote Malignant Transformation in SV40 Tag-Induced Transgenic Mouse Models
Mol. Cancer Res., December 1, 2006; 4(12): 957 - 969.
[Abstract] [Full Text] [PDF]


Home page
EMBO J.Home page
A. Hanisch, H. H. Sillje, and E. A. Nigg
Timely anaphase onset requires a novel spindle and kinetochore complex comprising Ska1 and Ska2
EMBO J., November 29, 2006; 25(23): 5504 - 5515.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
M. Kim, K. Murphy, F. Liu, S. E. Parker, M. L. Dowling, W. Baff, and G. D. Kao
Caspase-Mediated Specific Cleavage of BubR1 Is a Determinant of Mitotic Progression
Mol. Cell. Biol., November 1, 2005; 25(21): 9232 - 9248.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
T. Oikawa, M. Okuda, Z. Ma, R. Goorha, H. Tsujimoto, H. Inokuma, and K. Fukasawa
Transcriptional Control of BubR1 by p53 and Suppression of Centrosome Amplification by BubR1
Mol. Cell. Biol., May 15, 2005; 25(10): 4046 - 4061.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
Q. Wang, T. Liu, Y. Fang, S. Xie, X. Huang, R. Mahmood, G. Ramaswamy, K. M. Sakamoto, Z. Darzynkiewicz, M. Xu, et al.
BUBR1 deficiency results in abnormal megakaryopoiesis
Blood, February 15, 2004; 103(4): 1278 - 1285.
[Abstract] [Full Text] [PDF]


Home page
Cancer Res.Home page
W. Dai, Q. Wang, T. Liu, M. Swamy, Y. Fang, S. Xie, R. Mahmood, Y.-M. Yang, M. Xu, and C. V. Rao
Slippage of Mitotic Arrest and Enhanced Tumor Development in Mice with BubR1 Haploinsufficiency
Cancer Res., January 15, 2004; 64(2): 440 - 445.
[Abstract] [Full Text] [PDF]


Home page
J. Leukoc. Biol.Home page
K.-H. Baek, H.-J. Shin, J.-K. Yoo, J.-H. Cho, Y.-H. Choi, Y.-C. Sung, F. McKeon, and C.-W. Lee
p53 deficiency and defective mitotic checkpoint in proliferating T lymphocytes increase chromosomal instability through aberrant exit from mitotic arrest
J. Leukoc. Biol., June 1, 2003; 73(6): 850 - 861.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation
Copyright © 1999 by the American Association of Cancer Research.