Journal
JOURNAL OF CELL BIOLOGY
Volume 219, Issue 8, Pages -Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.202004062
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Funding
- Beijing Municipal Science and Technology Commission [Z181100001318003]
- National Natural Science Foundation of China [31871426, 31421002, 31561143001, 31630048, 31790403]
- Chinese Ministry of Science and Technology [2017YFA0503401]
- Strategic Priority Research Programof the Chinese Academy of Sciences [XDB19000000]
- Key Research Program of Frontier Sciences of the Chinese Academy of Sciences [QYZDY-SSW-SMC006]
- Japan Society for the Promotion of Science KAKENHI [18H03989, 18H02099, 19H05707]
- Japan Science and Technology Agency CREST [JPMJCR13M7]
- Grants-in-Aid for Scientific Research [18H02099] Funding Source: KAKEN
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Liquid-liquid phase separation (LLPS) compartmentalizes and concentrates biomacromolecules into distinct condensates. Liquid-like condensates can transition into gel and solid states, which are essential for fulfilling their different functions. LLPS plays important roles in multiple steps of autophagy, mediating the assembly of autophagosome formation sites, acting as an unconventional modulator of TORC1-mediated autophagy regulation, and triaging protein cargos for degradation. Gel-like, but not solid, protein condensates can trigger formation of surrounding autophagosomal membranes. Stress and pathological conditions cause aberrant phase separation and transition of condensates, which can evade surveillance by the autophagy machinery. Understanding the mechanisms underlying phase separation and transition will provide potential therapeutic targets for protein aggregation diseases.
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