Redox-sensitive TP53INP1 SUMOylation as an oxidative stress sensor to activate TP53.
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.
CRCM; Cancer Research Center of Marseille; INSERM U1068; Institut Paoli-Calmettes; Aix-Marseille University ; CNRS, UMR7258 ; Marseille, France.
Thomas
T
Bonacci
CRCM; Cancer Research Center of Marseille; INSERM U1068; Institut Paoli-Calmettes; Aix-Marseille University ; CNRS, UMR7258 ; Marseille, France.
Sylvain
S
Peuget
CRCM; Cancer Research Center of Marseille; INSERM U1068; Institut Paoli-Calmettes; Aix-Marseille University ; CNRS, UMR7258 ; Marseille, France.
Philippe
P
Soubeyran
CRCM; Cancer Research Center of Marseille; INSERM U1068; Institut Paoli-Calmettes; Aix-Marseille University ; CNRS, UMR7258 ; Marseille, France.
Juan
J
Iovanna
CRCM; Cancer Research Center of Marseille; INSERM U1068; Institut Paoli-Calmettes; Aix-Marseille University ; CNRS, UMR7258 ; Marseille, France.
Nelson J
NJ
Dusetti