| Primary Identifier | IPR034459 | Type | Family |
| Short Name | FUS |
| description | FUS (FUsed in Sarcoma, also known as TLS, Translocated in LipoSarcoma) is a RNA binding protein participating in nucleo-cytoplasmic RNA shuttling. It has functions in multiple cellular pathways. Mutations in the FUS gene cause amyotrophic lateral sclerosis (ALS), a progressive and ultimately fatal neurodegenerative disease of the upper and lower motor neurons of the brain and spinal cord []. TLS contains the unstructured N-terminal half followed by the RRM and zinc finger-like domains, which are connected to each other by a flexible linker. Interestingly, whether its RRM domain functions in the binding with RNAs is controversial. Moreover, its C-terminal RGG2-zinc finger-RGG3 domains have been found to function in the interaction with RNA [].TAF15/EWS/TLS family members include human FUS (Fused in liposarcoma), EWS (Ewing Sarcoma) and TAF15 (TATA binding associated factor 15), and the Drosophila orthologue Cabeza. They are RNA binding proteins that contain a transcriptional-activation domain (EAD), 3 glycine-arginine(RGG) rich regions, an RNA-binding domain (RBD), and a zinc finger domain [, ]. They are involved in transcription and alternative splicing. They are subjected to different environmental signals that induce post-translational modifications in their RBD and in the RGG domains, thus modulating their activity []. TAF15/EWS/TLS play important roles in oncogenesis and neuronal disease []. |
