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Hdm2 disrupts HdmX-mediated nuclear export of p53 by sequestering it in nucleus.
Ni, Yue; Chen, Hongce; Cheng, Xuecheng; Sun, Beini; Wu, Zhirui; Zhan, Qiuqiang; Zhuang, Zhengfei.
Afiliación
  • Ni Y; MOE Key Laboratory of Laser Life Science & Guangdong Provincial Key Laboratory of Laser Life Science, College of Biophotonics, School of Optoelectronic Science and Engineering, South China Normal University, Guangzhou, 510631, China; Centre for Optical and Electromagnetic Research, South China A
  • Chen H; MOE Key Laboratory of Laser Life Science & Guangdong Provincial Key Laboratory of Laser Life Science, College of Biophotonics, School of Optoelectronic Science and Engineering, South China Normal University, Guangzhou, 510631, China. Electronic address: hcchen2009@126.com.
  • Cheng X; MOE Key Laboratory of Laser Life Science & Guangdong Provincial Key Laboratory of Laser Life Science, College of Biophotonics, School of Optoelectronic Science and Engineering, South China Normal University, Guangzhou, 510631, China.
  • Sun B; MOE Key Laboratory of Laser Life Science & Guangdong Provincial Key Laboratory of Laser Life Science, College of Biophotonics, School of Optoelectronic Science and Engineering, South China Normal University, Guangzhou, 510631, China.
  • Wu Z; MOE Key Laboratory of Laser Life Science & Guangdong Provincial Key Laboratory of Laser Life Science, College of Biophotonics, School of Optoelectronic Science and Engineering, South China Normal University, Guangzhou, 510631, China.
  • Zhan Q; Centre for Optical and Electromagnetic Research, South China Academy of Advanced Optoelectronics, South China Normal University, Guangzhou, 510631, China.
  • Zhuang Z; MOE Key Laboratory of Laser Life Science & Guangdong Provincial Key Laboratory of Laser Life Science, College of Biophotonics, School of Optoelectronic Science and Engineering, South China Normal University, Guangzhou, 510631, China. Electronic address: zhuangzf@scnu.edu.cn.
Exp Cell Res ; 441(2): 114185, 2024 Aug 15.
Article en En | MEDLINE | ID: mdl-39069150
ABSTRACT
Dysfunction of the tumor suppressor p53 occurs in most human cancers, Hdm2 and HdmX play critical roles in p53 inactivation and degradation. Under unstressed conditions, HdmX binds to p53 like Hdm2, but HdmX cannot directly induce p53 degradation. Moreover, HdmX has been reported to stimulate Hdm2-mediated ubiquitination and degradation of p53. Here we reported that HdmX promoted the nuclear export of p53 independent of Hdm2 in living cells using FRET technology. Whereas, Hdm2 impeded HdmX-mediated nuclear export of p53 by sequestering it in nucleus. Interestingly, the C-terminal RING domain mutant Hdm2C464A formed heterooligomers with p53 in nucleus, which was inhibited by HdmX. The heterooligomers were located near PML-NBs. This study indicate that the nuclear Hdm2-HdmX interaction aborts the HdmX-mediated nuclear export of p53.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Núcleo Celular / Proteína p53 Supresora de Tumor / Proteínas Proto-Oncogénicas / Proteínas de Ciclo Celular / Transporte Activo de Núcleo Celular / Proteínas Proto-Oncogénicas c-mdm2 Límite: Humans Idioma: En Revista: Exp Cell Res Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Núcleo Celular / Proteína p53 Supresora de Tumor / Proteínas Proto-Oncogénicas / Proteínas de Ciclo Celular / Transporte Activo de Núcleo Celular / Proteínas Proto-Oncogénicas c-mdm2 Límite: Humans Idioma: En Revista: Exp Cell Res Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos