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Functional Interaction between BubR1 and Securin in an Anaphase-Promoting Complex/Cyclosome(Cdc20)-Independent Manner

Cited 10 time in Web of Science Cited 11 time in Scopus
Authors
Kim, Hyun-Soo; Jeon, Yoon-Kyung; Ha, Geun-Hyoung; Park, Hye-Young; Shin, Hyun-Jin; Chung, Doo-Hyun; Lee, Chang-Woo; Lee, Chang Geun; Kim, Yu-Jin
Issue Date
2009-01-01
Publisher
AMER ASSOC CANCER RESEARCH
Citation
CANCER RESEARCH; Vol.69 1; 27-36
Abstract
Activation of the mitotic checkpoint requires the precise timing and spatial organization of mitotic regulatory events, and ensures accurate chromosome segregation. Mitotic checkpoint proteins such its BubR1 and Mad2 bind to Cdc20, and inhibit anaphase-promoting complex/cyclosome(Cdc20)-mediated securin degradation and the onset of anaphase. BubR1 mediates the proper attachment of micro-tubules to kinetochores, and links the regulation of chromosome-spindle attachment to mitotic checkpoint signaling. Therefore, disruption of BubR1 activity results in a loss of the checkpoint control, chromosome instability, and/or early onset of malignancy. In this study, we show that BubR1 directly interacts with securin in vitro and in vivo. In addition, the BubR1 interaction contributes to the stability of securin, and there is a significant positive correlation between BubR1 and securin expressions in human cancer. Importantly, BubR1 competes with Cdc20 for binding to securin, and thereby the interaction between BubR1 and securin is greatly increased by the depletion of Cdc20. Our findings may identify a novel regulation of BubR1 that can generate an additional anaphase-inhibitory signal through the Cdc20-independent interaction of BubR1 with securin. [Cancer Res 2009;69(1):27-36]
ISSN
0008-5472
Language
English
URI
http://hdl.handle.net/10371/76738
DOI
https://doi.org/10.1158/0008-5472.CAN-08-0820
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College of Medicine/School of Medicine (의과대학/대학원)Pathology (병리학전공)Journal Papers (저널논문_병리학전공)
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