Basic information
LLPS related evidences
| Publication note | Here, we establish, based on live cell microscopy and CRISPR/Cas9-mediated endogenous protein tagging, that 53BP1-marked repair compartments are dynamic, show droplet-like behavior, and undergo frequent fusion and fission events. 53BP1 assembly, but not the upstream accumulation of γH2AX and MDC1, is highly sensitive to changes in osmotic pressure, temperature, salt concentration and to disruption of hydrophobic interactions. Phase separation of 53BP1 is substantiated by optoDroplet experiments, which further allowed dissection of the 53BP1 sequence elements that cooperate for light-induced clustering. (Organism: Homo sapiens; Cell line: U2OS cells) |
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| Material state | liquid : Similar to 53BP1 assembly around DNA lesions, 53BP1 optoDroplet fusions could be readily observed, demonstrating their liquid‐like behavior | ||
| LLPS region | 1140-1972,1203-1972 | Key domains | C‐terminus,largely unstructured N‐terminus : the C‐terminus, comprising amino acids 1140–1972, was sufficient for optoDroplet formation and that the oligomerization domain (OD) was critically involved. The largely unstructured N‐terminus of 53BP1 was dispensable for optoDroplet formation. |
LLPS partner
| Protein partner | _ ( _ ) |
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|---|---|---|
| RNA partner | _ |
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| Others | _ |
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LLPS regulation
| PTM | _ |
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|---|---|---|
| Mutation | p.W1495A |
The W1495A TTD mutation abolished foci formation when multiple DNA lesions were induced, but allowed for damage recruitment when a strong singular nucleation event was provided by FokI induction. |
| Alternative splicing | _ | |
| Repeat | _ | |
| Oligomerization | _ | |