Dataset Information

Immunoprecipitation-Mass Spectrometry (IP-MS) of SRPK1 in endothelial cells

ABSTRACT: To identify the E3 ubiquitin ligase responsible for the polyubiquitination of SRPK1, we performed immunoprecipitation (IP) using an anti-SRPK1 antibody or IgG control as well as endothelial lysates treated with PA and MG-132, followed by mass spectrometry analysis

INSTRUMENT(S):

ORGANISM(S): Rattus Norvegicus (rat)

TISSUE(S): Primary Cell, Endothelial Cell

SUBMITTER: Xiao-Hui Tan

LAB HEAD: Rui-Li GUAN

PROVIDER: PXD062417 | Pride | 2026-05-30

REPOSITORIES: Pride

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Publications

Palmitoylation-Mediated Ubiquitination of SRPK1 Regulates Ferroptosis in High-Fat-Induced Erectile Dysfunction.

Tan Xiao-Hui XH Li Ke-Fan KF Yuan Yi-Ming YM Xia Man-Cheng MC Zhao Fang-Zhou FZ Ying Hong-Gang HG Zhou Zhuo Z Gao Peng-Chao PC Xie Guo-Qing GQ Li Xue-Song XS Jiang Hui H Guan Rui-Li RL

Advanced science (Weinheim, Baden-Wurttemberg, Germany) 20260129 19

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) ...[more]

PMID: 41610308

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			Action	DRS
	IgGrep6.msf	Msf
	IgGrep6.msfView	Msf
	IgGrep6.pdResult	Other
	IgGrep6.pdResultView	Other
	IgGrep6.raw	Raw