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SPATA33 is an autophagy mediator for cargo selectivity in germline mitophagy.

ABSTRACT: 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.

SUBMITTER: Zhang Y

PROVIDER: S-EPMC7937689 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature

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SPATA33 is an autophagy mediator for cargo selectivity in germline mitophagy.

Zhang Ying Y Xu Xu X Hu Mengxin M Wang Xin X Cheng Hanhua H Zhou Rongjia R

Cell death and differentiation 20201021 3

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 ...[more]

PMID: 33087875

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