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Palmitoylation-Mediated Ubiquitination of SRPK1 Regulates Ferroptosis in High-Fat-Induced Erectile Dysfunction.
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ID: paper-41610308
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Palmitoylation-Mediated Ubiquitination of SRPK1 Regulates Ferroptosis in High-Fat-Induced Erectile Dysfunction.
Tan XH, Li KF, Yuan YM, Xia MC, Zhao FZ et al.
Abstract
Serine-arginine protein kinase 1 (SRPK1) is a major protein kinase involved in mRNA splicing, cell cycle, and endothelial function. Recent studies have highlighted a close relationship between palmitic acid (PA) and endothelial cell ferroptosis. Here, we demonstrate that PA promotes the ubiquitination-dependent degradation of SRPK1 mediated by the E3 ubiquitin ligase mindbomb 1 (MIB1) at lysine 494. Moreover, SRPK1 S-palmitoylation is catalyzed by zinc-finger DHHC S-acyltransferase 24 (ZDHHC24) ...
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