泛素连接酶
生物
泛素
转录因子
ATF4
磷酸化
ATF3
蛋白酶体
F盒蛋白
蛋白质降解
分子生物学
DNA连接酶
抄写(语言学)
细胞生物学
生物化学
发起人
基因表达
基因
语言学
哲学
作者
Irina Lassot,Emmanuel Ségéral,Clarisse Berlioz‐Torrent,H Durand,Lionel Groussin,Tsonwin Hai,Richard Bénarous,Florence Margottin-Goguet
标识
DOI:10.1128/mcb.21.6.2192-2202.2001
摘要
The ubiquitin-proteasome pathway regulates gene expression through protein degradation. Here we show that the F-box protein betaTrCP, the receptor component of the SCF E3 ubiquitin ligase responsible for IkappaBalpha and beta-catenin degradation, is colocalized in the nucleus with ATF4, a member of the ATF-CREB bZIP family of transcription factors, and controls its stability. Association between the two proteins depends on ATF4 phosphorylation and on ATF4 serine residue 219 present in the context of DSGXXXS, which is similar but not identical to the motif found in other substrates of betaTrCP. ATF4 ubiquitination in HeLa cells is enhanced in the presence of betaTrCP. The F-box-deleted betaTrCP protein behaves as a negative transdominant mutant that inhibits ATF4 ubiquitination and degradation and, subsequently, enhances its activity in cyclic AMP-mediated transcription. ATF4 represents a novel substrate for the SCF(betaTrCP) complex, which is the first mammalian E3 ubiquitin ligase identified so far for the control of the degradation of a bZIP transcription factor.
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