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SEPA-1 Mediates the Specific Recognition and Degradation of P Granule Components by Autophagy in C. elegans
Yuxia Zhang1,4,Libo Yan1,2,4,Zhi Zhou1,4,Peiguo Yang1,4,E. Tian1,Kai Zhang3,Yu Zhao1,Zhipeng Li1,Bing Song1,Jinghua Han1,Long Miao3andHong Zhang1,,
1 National Institute of Biological Sciences, Beijing 102206, P.R. China
2 Graduate Program in Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100730, P.R. China
3 National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China
4 These authors contributed equally to this work
Summary
How autophagy, an evolutionarily conserved intracellular catabolic system for bulk degradation, selectively degrades protein aggregates is poorly understood. Here, we show that several maternally derived germ P granule components are selectively eliminated by autophagy in somatic cells during C. elegans embryogenesis. The activity of sepa-1 is required for the degradation of these P granule components and for their accumulation into aggregates, termed PGL granules, in autophagy mutants. SEPA-1 forms protein aggregates and is also a preferential target of autophagy. SEPA-1 directly binds to the P granule component PGL-3 and also to the autophagy protein LGG-1/Atg8. SEPA-1 aggregates consistently colocalize with PGL granules and with LGG-1 puncta. Thus, SEPA-1 functions as a bridging molecule in mediating the specific recognition and degradation of P granule components by autophagy. Our study reveals a mechanism for preferential degradation of protein aggregates by autophagy and emphasizes the physiological significance of selective autophagy during animal development.
