Basic information
| PhaSepDB ID | psself49 | Reference | 26727894,24268778 | Uniprot Entry | P35637 | Gene names | FUS |
|---|---|---|---|---|---|---|---|
| Class | PS-self | Location | Cytoplasm | MLO | Stress granule | ||
LLPS related evidences
| Publication note | Here, we examine the mechanism of this process and find that RNA binding nucleates the formation of higher-order FUS ribonucleoprotein assemblies that bind the CTD. Both the low-complexity domain and the arginine-glycine rich domain of FUS contribute to assembly. The assemblies appear fibrous by electron microscopy and have characteristics of β zipper structures. (Organism: Homo sapiens; Cell line: _) |
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|---|---|---|---|
| Material state | hydrogel : Protein constructs containing the assembly domains of FUS also readily formed microscopic hydrogels. | ||
| LLPS region | 1-526,RGG domain,LC domain | Key domains | _ : _ |
LLPS partner
| Protein partner | _ ( _ ) |
_ |
|---|---|---|
| RNA partner | 48 nt RNA from the promoter of DNMT3b |
FUS in the absence of RNA had some ability to spontaneously form ropey assemblies but mostly was found in round disk-shaped assemblies ranging from 30 to 50 nm in diameter. Upon addition of RNA, large branched assemblies were formed and sub-architecture could be observed that appeared as bundles of fibers forming the branches of these ropey structures. |
| Others | _ |
_ |
LLPS regulation
| PTM | _ |
_ |
|---|---|---|
| Mutation | _ |
_ |
| Alternative splicing | _ | |
| Repeat | _ | |
| Oligomerization | _ | |