Table 4.
Proteins form LLPS in cancer
| Name | Disease | Mechanism | Reference |
|---|---|---|---|
| AHNAK | Cancer cell survival | AHNAK is a G1-enriched interactor of 53BP1 that ensures optimal partitioning of 53BP1 into phase-separated condensates and limits excessive interaction with p53, which leads to apoptosis in cancer cells | 260 |
| AKAP95 | Cancer | AKAP95 is a nuclear protein that regulates transcription and RNA splicing by forming liquid-like condensates in nucleus. | 261 |
| HP1γ | Myeloma | The deacetylation of HP1γ promotes nuclear condensation, and this condensed form of HP1γ plays a crucial role in drug resistance by facilitating DNA repair in multiple myeloma cell. | 286 |
| NONO | Tumor radioresistance | LLPS of NONO recruits nuclear EGFR and DNA-PK and promotes DNA repair, leading to radioresistance. | 262 |
| NPM1 (Nucleophosmin) | Triple-negative breast cancer (TNBC) | NPM1 undergoes LLPS through interactions with nucleolar components, including rRNA and proteins featuring multivalent arginine-rich linear motifs (R-motifs). NPM1 binds to the PD-L1 promoter in TNBC cells, activating PD-L1 transcription. | 263,264 |
|
NUP98 (Nucleoporin 98) |
Leukemia | The biomolecular condensation is embedded within the N-terminus of NUP98 and possesses the ability to induce leukemia-specific gene expression. | 290 |
|
RIα (Type I regulatory subunit of PKA) |
Cell transformation | Loss of RIα LLPS in normal cells induces cell transformation. | 44 |
| SPOP | Prostate, breast cancer | Cancer-associated mutations in tumor suppressor SPOP disrupt LLPS and correlate with a loss of function. | 275 |
| U2AF1 | Myeloid malignancies | U2AF1 splicing factor mutations, lead to an increased SG response, indicating a new function for biomolecular condensates in adaptive oncogenic mechanisms. | 292 |