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Negative Feedback Regulation of Aurora-A via Phosphorylation of Fas-associated Factor-1

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Authors
Jang, Moon-Sun; Sul, Jee-Won; Choi, Byung-Jung; Lee, Su-Jin; Suh, Jee-Hee; Kim, Nam-Soon; Kim, Woo Ho; Lim, Dae-Sik; Lee, Chang-Woo; Kim, Eunhee
Issue Date
2008-09-12
Publisher
American Society for Biochemistry and Molecular Biology
Citation
J Biol Chem 283, 32344-32351
Abstract
This study reports that Aurora-A (Aur-A) phosphorylates Fas-associated factor-1 (FAF1) at Ser-289 and Ser-291. Forced expression of a FAF1 mutant mimicking phosphorylation at Ser-289 and Ser-291 (FAF1 DD), but not phosphorylation-deficient FAF1 (FAF1 AA), reduced Aur-A expression. However, transfection of FAF1 DD failed to reduce Aur-A expression in the presence of MG132 and MG115, indicating that this decrease is proteasome-mediated. Additionally, transfection of FAF1 DD suppressed the expression of Aur-A in ts20-BALB cells lacking E1 ubiquitin (Ub) activating enzyme activity at restrictive temperatures and also reduced the expression of Aur-A S51D, a mutant resistant to Ub-dependent degradation. Our data indicate that phosphorylated FAF1 mediates the ubiquitin-independent, proteasome-dependent degradation of Aur-A. Overexpression of FAF1 DD blocked Aur-A-induced centrosome amplification and accumulated cells in G(2)/M phase, representing cellular phenotypes consistent with the anticipated loss of Aur-A. Collectively, our findings support the negative feedback regulation of Aur-A via phosphorylation of the death-promoting protein, FAF1, and disclose the presence of molecular cross-talk between constituents of the cell cycle and cell death machinery.
ISSN
0021-9258 (print)1083-351X (online)
Language
English
URI
http://hdl.handle.net/10371/4536
DOI
https://doi.org/10.1074/jbc.M804199200
https://doi.org/10.1074/jbc.M804199200
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College of Medicine/School of Medicine (의과대학/대학원)Pathology (병리학전공)Journal Papers (저널논문_병리학전공)
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