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Deacylases-structure, function, and relationship to diseases.
Wang, Shuxian; Xing, Xiaoke; Ma, Jialin; Zheng, Sihao; Song, Qibin; Zhang, Pingfeng.
Affiliation
  • Wang S; Cancer Center, Renmin Hospital of Wuhan University, China.
  • Xing X; Cancer Center, Renmin Hospital of Wuhan University, China.
  • Ma J; Cancer Center, Renmin Hospital of Wuhan University, China.
  • Zheng S; Cancer Center, Renmin Hospital of Wuhan University, China.
  • Song Q; Cancer Center, Renmin Hospital of Wuhan University, China.
  • Zhang P; Cancer Center, Renmin Hospital of Wuhan University, China.
FEBS Lett ; 598(9): 959-977, 2024 May.
Article in En | MEDLINE | ID: mdl-38644468
ABSTRACT
Reversible S-acylation plays a pivotal role in various biological processes, modulating protein functions such as subcellular localization, protein stability/activity, and protein-protein interactions. These modifications are mediated by acyltransferases and deacylases, among which the most abundant modification is S-palmitoylation. Growing evidence has shown that this rivalrous pair of modifications, occurring in a reversible cycle, is essential for various biological functions. Aberrations in this process have been associated with various diseases, including cancer, neurological disorders, and immune diseases. This underscores the importance of studying enzymes involved in acylation and deacylation to gain further insights into disease pathogenesis and provide novel strategies for disease treatment. In this Review, we summarize our current understanding of the structure and physiological function of deacylases, highlighting their pivotal roles in pathology. Our aim is to provide insights for further clinical applications.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Neoplasms Limits: Animals / Humans Language: En Journal: FEBS Lett Year: 2024 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Neoplasms Limits: Animals / Humans Language: En Journal: FEBS Lett Year: 2024 Document type: Article