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 (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 Ouyang, B.
Right arrow Articles by Dai, W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ouyang, B.
Right arrow Articles by Dai, W.

Cell Growth & Differentiation, Vol 9, Issue 10 877-885, Copyright © 1998 by American Association of Cancer Research


ARTICLES

Human Bub1: a putative spindle checkpoint kinase closely linked to cell proliferation

B Ouyang, Z Lan, J Meadows, H Pan, K Fukasawa, W Li and W Dai
Department of Medicine, University of Cincinnati College of Medicine, Ohio 45267, USA.

Eukaryotic cells have evolved a mechanism that delays the onset of anaphase until chromosomes are properly positioned on the spindle. To understand the molecular basis of such surveillance mechanism in human cells, we have cloned a full-length cDNA encoding a putative mitotic checkpoint kinase termed hBub1. Sequence comparison reveals that hBub1 is a structurally conserved protein, sharing 23% amino acid residue identity with BUB1 of budding yeast. In addition, the NH2-terminal portion (161 amino acids) of hBub1 shows a significant homology to yeast MAD3, a protein also known to be involved in the mitotic checkpoint response pathway. Northern blot analyses show that the hBub1 mRNA level is abundantly expressed in tissues or cells with a high mitotic index. When Dami cells undergo terminal differentiation after treatment with phorbol ester, hBub1 expression in this cell line is down-regulated rapidly. The hBub1 protein level is low in G1 and remains relatively constant in S, G2, and M phases. Immunofluorescence analysis shows that hBub1 protein colocalizes with a centromere-kinetochore antigen CREST in interphase, mitotic prophase, and nocodazole-treated cells. Antibody electroporation experiments show that hBub1 is an important component of the spindle checkpoint pathway. Furthermore, fluorescence in situ hybridization analysis maps the hBub1 gene to chromosome 2q12-13. Our studies suggest that hBub1 expression is restricted to proliferating cells and appears to be involved in regulating cell cycle progression. The molecular cloning of hBub1 cDNA will facilitate the study of its role in spindle checkpoint control as well as its potential role in certain genetic disorders.


This article has been cited by other articles:


Home page
Proc. Natl. Acad. Sci. USAHome page
M. Leng, D. W. Chan, H. Luo, C. Zhu, J. Qin, and Y. Wang
MPS1-dependent mitotic BLM phosphorylation is important for chromosome stability
PNAS, August 1, 2006; 103(31): 11485 - 11490.
[Abstract] [Full Text] [PDF]


Home page
Molecular Cancer TherapeuticsHome page
T. Kosakowska-Cholody, W. M. Cholody, A. Monks, B. A. Woynarowska, and C. J. Michejda
WMC-79, a potent agent against colon cancers, induces apoptosis through a p53-dependent pathway
Mol. Cancer Ther., October 1, 2005; 4(10): 1617 - 1627.
[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
Mol. Biol. CellHome page
S. Kadura, X. He, V. Vanoosthuyse, K. G. Hardwick, and S. Sazer
The A78V Mutation in the Mad3-like Domain of Schizosaccharomyces pombe Bub1p Perturbs Nuclear Accumulation and Kinetochore Targeting of Bub1p, Bub3p, and Mad3p and Spindle Assembly Checkpoint Function
Mol. Biol. Cell, January 1, 2005; 16(1): 385 - 395.
[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
Mol. Biol. CellHome page
M. L. Whitfield, G. Sherlock, A. J. Saldanha, J. I. Murray, C. A. Ball, K. E. Alexander, J. C. Matese, C. M. Perou, M. M. Hurt, P. O. Brown, et al.
Identification of Genes Periodically Expressed in the Human Cell Cycle and Their Expression in Tumors
Mol. Biol. Cell, June 1, 2002; 13(6): 1977 - 2000.
[Abstract] [Full Text] [PDF]


Home page
Cell Growth Differ.Home page
W. Li, Z. Lan, H. Wu, S. Wu, J. Meadows, J. Chen, V. Zhu, and W. Dai
BUBR1 Phosphorylation Is Regulated during Mitotic Checkpoint Activation
Cell Growth Differ., November 1, 1999; 10(11): 769 - 775.
[Abstract] [Full Text]




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 © 1998 by the American Association of Cancer Research.