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Title 

Negative feedback regulation of Aurora-a via phosphorylation of Fas-associated factor-1

Authors 

M S JangJ W SulB J ChoiS J LeeJ H SuhNam-Soon KimW H KimD S LimC W LeeE Kim

Publisher 

American Society for Biochemistry and Molecular Biology

Issue Date 

2008

Citation 

Journal of Biological Chemistry, vol. 283, no. 47, pp. 32344-32351

Keywords 

amplificationbiological organscell deathchemical reactionsdegradationenzyme activityfeedbackgas emissionsmachinerynucleic acids

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 G2/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

Link 

http://dx.doi.org/10.1074/jbc.M804199200

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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