氧化还原敏感的TP53INP1类泛素化修饰作为一种氧化应激传感器来激活TP53。
Redox-sensitive TP53INP1 SUMOylation as an oxidative stress sensor to activate TP53.
作者信息
Bonacci Thomas, Peuget Sylvain, Soubeyran Philippe, Iovanna Juan, Dusetti Nelson J
机构信息
CRCM; Cancer Research Center of Marseille; INSERM U1068; Institut Paoli-Calmettes; Aix-Marseille University ; CNRS, UMR7258 ; Marseille, France.
出版信息
Mol Cell Oncol. 2014 Dec 23;1(3):e964044. doi: 10.4161/23723548.2014.964044. eCollection 2014 Jul-Sep.
Abstract
Oxidative stress-induced sumoylation of TP53INP1 (tumor protein p53-induced nuclear protein 1) is essential to enhance the TP53 response. Sumoylation of TP53INP1 on the K113 residue, which is mediated by protein inhibitor of activated STAT 3 (PIAS3) and chromobox homolog 4 (CBX4) and removed by SUMO1/sentrin specific peptidase (SENP1, 2 and 6), favors its interaction with TP53 in the nucleus and enhances TP53-induced gene expression.
摘要
氧化应激诱导的TP53INP1（肿瘤蛋白p53诱导的核蛋白1）的SUMO化对于增强TP53反应至关重要。TP53INP1在K113残基上的SUMO化由活化STAT 3的蛋白抑制剂（PIAS3）和染色体盒同源物4（CBX4）介导，并由SUMO1/ sentrin特异性肽酶（SENP1、2和6）去除，这有利于其在细胞核中与TP53相互作用，并增强TP53诱导的基因表达。
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