粒体自噬
自噬
细胞生物学
线粒体
自噬体
调解人
ATG16L1
帕金
品脱1
生物
化学
生物化学
细胞凋亡
疾病
病理
帕金森病
医学
作者
Ying Zhang,Xu Xu,Mengxin Hu,Xin Wang,Hanhua Cheng,Rongjia Zhou
标识
DOI:10.1038/s41418-020-00638-2
摘要
Selective autophagic degradation of mitochondria (mitophagy) is important in maintaining proper cellular homeostasis. Here, we found that SPATA33 is a novel autophagy mediator for mitophagy in testis. The SPATA33 protein localizes on mitochondria via its binding of the carboxyl terminal with the outer mitochondrial membrane protein VDAC2. Upon starvation induction, SPATA33 is recruited to autophagosome by binding the autophagy machinery ATG16L1 via its N-terminal along with mitochondria. Notably, Spata33 knockout inhibited autophagy and overexpression can promote autophagosome formation for mitochondrial sequestration. Therefore, SPATA33 confers selectivity for mitochondrial degradation and promotes mitophagy in male germline cells.
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