Insights into Molecular Diversity within the FUS/EWS/TAF15 Protein Family: Unraveling Phase Separation of the N-Terminal Low-Complexity Domain from RNA-Binding Protein EWS.
Journal
Journal of the American Chemical Society
ISSN: 1520-5126
Titre abrégé: J Am Chem Soc
Pays: United States
ID NLM: 7503056
Informations de publication
Date de publication:
27 Mar 2024
27 Mar 2024
Historique:
medline:
28
3
2024
pubmed:
16
3
2024
entrez:
16
3
2024
Statut:
ppublish
Résumé
The FET protein family, comprising FUS, EWS, and TAF15, plays crucial roles in mRNA maturation, transcriptional regulation, and DNA damage response. Clinically, they are linked to Ewing family tumors and neurodegenerative diseases such as amyotrophic lateral sclerosis. The fusion protein EWS::FLI1, the causative mutation of Ewing sarcoma, arises from a genomic translocation that fuses a portion of the low-complexity domain (LCD) of EWS (EWS
Identifiants
pubmed: 38492239
doi: 10.1021/jacs.3c12034
doi:
Substances chimiques
RNA-Binding Protein EWS
0
RNA-Binding Protein FUS
0
Proteins
0
Tyrosine
42HK56048U
TAF15 protein, human
0
TATA-Binding Protein Associated Factors
0
FUS protein, human
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
8071-8085Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM136917
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM153388
Pays : United States
Commentaires et corrections
Type : UpdateOf