Journal
MOLECULAR CELL
Volume 77, Issue 6, Pages 1163-+Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2019.12.026
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Funding
- JSPS KAKENHI grants [25111004, 18H03989, 19H05707, 17K18339, 19K16344, 17H05894, 17K07319, 16H06375, 16H06280, 18H04853, 18J13429]
- CREST, Japan Science and Technology Agency [JPMJCR13M7]
- Takeda Science Foundation
- Mochida Memorial Foundation for Medical and Pharmaceutical Research
- Tokyo Biochemical Research Foundation
- Naito Foundation
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Clearance of biomolecular condensates by selective autophagy is thought to play a crucial role in cellular homeostasis. However, the mechanism underlying selective autophagy of condensates and whether liquidity determines a condensate's susceptibility to degradation by autophagy remain unknown. Here, we show that the selective autophagic cargo aminopeptidase I (Ape1) undergoes phase separation to form semi-liquid droplets. The Ape1-specific receptor protein Atg19 localizes to the surface of Ape1 droplets both in vitro and in vivo, with the floatability of Atg19 preventing its penetration into droplets. In vitro reconstitution experiments reveal that Atg19 and lipidated Atg8 are necessary and sufficient for selective sequestration of Ape1 droplets by membranes. This sequestration is impaired by mutational solidification of Ape1 droplets or diminished ability of Atg19 to float. Taken together, we propose that cargo liquidity and the presence of sufficient amounts of autophagic receptor on cargo are crucial for selective autophagy of biomolecular condensates.
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