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泛素依赖性蛋白质降解对c-Jun和JunD的差异调节

Differential regulation of c-Jun and JunD by ubiquitin-dependent protein degradation.

作者信息

Musti A M, Treier M, Peverali F A, Bohmann D

机构信息

EMBL, Heidelberg, Germany.

出版信息

Biol Chem. 1996 Oct;377(10):619-24. doi: 10.1515/bchm3.1996.377.10.619.

DOI:10.1515/bchm3.1996.377.10.619
PMID:8922589
Abstract

c-Jun and JunD are two closely related members of the Jun family of transcription factors which markedly differ in their biological functions. Whereas c-Jun behaves as a positive regulator of cell growth and may cause cell transformation when overexpressed, JunD antagonizes both of these effects. To better understand how the activities of c-Jun and JunD are controlled, we investigated how their stabilities within the cell are determined. We show that, in contrast to c-Jun which is degraded following multi ubiquitination, JunD is not efficiently ubiquitinated and exhibits a correspondingly longer half-life. Mutational analysis reveals that the determinant for the difference in ubiquitination resides in the NH2-terminal regions of the proteins which in c-Jun contains the delta-domain.

摘要

c-Jun和JunD是转录因子Jun家族中两个密切相关的成员,它们的生物学功能明显不同。c-Jun作为细胞生长的正调节因子,过度表达时可能导致细胞转化,而JunD则拮抗这两种作用。为了更好地理解c-Jun和JunD的活性是如何被调控的,我们研究了它们在细胞内的稳定性是如何决定的。我们发现,与多聚泛素化后被降解的c-Jun不同,JunD不能有效地被泛素化,因此具有相应更长的半衰期。突变分析表明,泛素化差异的决定因素位于蛋白质的NH2末端区域,在c-Jun中该区域包含δ结构域。

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1
Differential regulation of c-Jun and JunD by ubiquitin-dependent protein degradation.泛素依赖性蛋白质降解对c-Jun和JunD的差异调节
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