CARD9 protein SUMOylation regulates HOXB5 nuclear translocation and Parkin-mediated mitophagy in myocardial I/R injury

被引:0
|
作者
Li, Yuanbin [1 ]
Tang, Yuting [2 ]
Yan, Xu [3 ]
Lin, Hui [1 ]
Jiang, Wanjin [1 ]
Zhang, Luwei [1 ]
Zhao, Hu [3 ]
Chen, Zhuang [1 ]
机构
[1] Hunan Tradit Chinese Med Coll, Dept Med, Zhuzhou 412012, Hunan, Peoples R China
[2] Cent South Univ, Affiliated Canc Hosp, Hunan Canc Hosp, Xiangya Sch Med,Dept Pathol, Changsha, Hunan, Peoples R China
[3] Hunan Acad Tradit Chinese Med, Affiliated Hosp, Dept Cardiovasc, Changsha, Hunan, Peoples R China
基金
中国国家自然科学基金;
关键词
CARD9; HOXB5; nuclear; Mitophagy; O-GlcNAc glycosylation; SUMOylation; translocation; ACTIVATION; APOPTOSIS; PROLIFERATION; CELL;
D O I
10.1111/jcmm.70195
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Myocardial injury induced by ischemia-reperfusion (I/R) remains a difficult clinical problem. However, the exact mechanisms underlying I/R-induced have yet to be clarified. CARD9 is an important cytoplasmic-binding protein. In this study, an immunocoprecipitation assay showed that SUMOylation of the CARD9 protein promoted the binding of CARD9 to HOXB5, but hindered the O-GlcNAc glycosylation of HOXB5, a predicted transcription factor of Parkin and a key factor in mitophagy. O-GlcNAc glycosylation is an important signal for translocation of proteins from the cytoplasm to the nucleus. CARD9 protein SUMOylation is regulated by PIAS3, which is related to I/R-induced myocardial injury. Therefore, we propose that knockdown of PIAS3 inhibits SUMOylation of the CARD9 protein, facilitates the dissociation of CARD9 and HOXB5, which increases the O-GlcNAc-mediated glycosylation of HOXB5, while the resulting HOXB5 nuclear translocation promotes Parkin-induced mitophagy and alleviates myocardial I/R injury.
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页数:15
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