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SIRT2 regulates high mobility group protein B1 nucleoplasmic shuttle and degradation via deacetylation in microglia.
Xing, Wan-Qun; Piao, Xian-Ji; Han, Qi; Shi, Hui-Ying; Wu, Wen-Cong; Si, Fan; Lu, Jing-Jing; Zhou, Tie-Zhong; Guo, Jing-Ru; Li, Shi-Ze; Xu, Bin.
Afiliación
  • Xing WQ; College of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, China.
  • Piao XJ; The Fifth Affiliated Hospital of Harbin Medical University, Daqing, China.
  • Han Q; College of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, China.
  • Shi HY; College of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, China.
  • Wu WC; College of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, China.
  • Si F; College of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, China.
  • Lu JJ; College of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, China.
  • Zhou TZ; College of Animal Husbandry and Veterinary Medicine, Jinzhou Medical University, Jinzhou, China.
  • Guo JR; College of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, China.
  • Li SZ; College of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, China.
  • Xu B; College of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, China.
J Cell Physiol ; : e31364, 2024 Aug 11.
Article en En | MEDLINE | ID: mdl-39129208
ABSTRACT
High mobility group protein B1 (HMGB1) acts as a pathogenic inflammatory response to mediate ranges of conditions such as epilepsy, septic shock, ischemia, traumatic brain injury, Parkinson's disease, Alzheimer's disease and mass spectrometry. HMGB1 promotes inflammation during sterile and infectious damage and plays a crucial role in disease development. Mobilization from the nucleus to the cytoplasm is the first important step in the release of HMGB1 from activated immune cells. Here, we demonstrated that Sirtuin 2 (SIRT2) physically interacts with and deacetylates HMGB1 at 43 lysine residue at nuclear localization signal locations, strengthening its interaction with HMGB1 and causing HMGB1 to be localized in the cytoplasm. These discoveries are the first to shed light on the SIRT2 nucleoplasmic shuttle, which influences HMGB1 and its degradation, hence revealing novel therapeutic targets and avenues for neuroinflammation treatment.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: J Cell Physiol Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: J Cell Physiol Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Estados Unidos