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| Effect of Phosphorylation by Akt on Miz1's Ubiquitination |
| TIAN Xue-jun1,2, YANG Yi1,2, LIU Jing2, CHEN Kan1 |
1. School of Life Sciences,Zhejiang Sci-Tech University,Hangzhou 310018,China;
2. Feinberg School of Medicine,Northwestern University,Chicago 60611,USA |
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Abstract Miz1 is an important transcription factor,and also a signal-and pathway-specific modulator or regulator. Upon TNFα stimulation,Miz1 undergoes ubiquitination and degradation,releasing its inhibition on JNK signaling pathway,which leads to the activation of JNK. Phosphorylation and ubiquitination have multiple connections. Recent study showes that protein kinase Akt can specifically phosphorylate Miz1 to regulate cell-cycle arrest after DNA damage. Through the site-directed mutagenesis of Mus wild-type Miz1 at specifically phosphorylation site to get S419A Miz1,and then immunoblotting and in vivo ubiquitination assay,the results show that phosphorylation of Miz1 by Akt is not requied for its ubiquitination,and even suppresses it
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Received: 24 January 2011
Published: 25 August 2011
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