Journal
SCIENTIFIC REPORTS
Volume 2, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/srep00603
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Funding
- European Research Council [206726-CLIP]
- Medical Research Council [U105185858]
- Slovenian Research Agency [P2-0209, J2-2197, L2-1112, Z7-3665, J3-4026]
- Wellcome Trust
- MRC Strategic Grant Award [089701/Z/09/Z]
- Motor Neuron Disease Association
- Heaton-Ellis Trust
- Psychiatry Research Trust
- MEXT
- CREST, JST
- Nakajima Foundation
- Wellcome Trust [089701/Z/09/Z] Funding Source: Wellcome Trust
- Grants-in-Aid for Scientific Research [22500335] Funding Source: KAKEN
- Medical Research Council [MC_U105185858, G0900688, MC_G1000733, G0500289B, G0500289] Funding Source: researchfish
- MRC [G0900688, MC_U105185858, G0500289, MC_G1000733] Funding Source: UKRI
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Fused in sarcoma (FUS) and TAR DNA-binding protein 43 (TDP-43) are RNA-binding proteins pathogenetically linked to amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD), but it is not known if they regulate the same transcripts. We addressed this question using crosslinking and immunoprecipitation (iCLIP) in mouse brain, which showed that FUS binds along the whole length of the nascent RNA with limited sequence specificity to GGU and related motifs. A saw-tooth binding pattern in long genes demonstrated that FUS remains bound to pre-mRNAs until splicing is completed. Analysis of FUS-/- brain demonstrated a role for FUS in alternative splicing, with increased crosslinking of FUS in introns around the repressed exons. We did not observe a significant overlap in the RNA binding sites or the exons regulated by FUS and TDP-43. Nevertheless, we found that both proteins regulate genes that function in neuronal development.
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