Journal
CELL REPORTS
Volume 18, Issue 11, Pages 2635-2650Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2017.02.046
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Funding
- European Research Council (ERC) [339953]
- Danish National Research Council
- Danish National Research Foundation [DNRF58]
- Lundbeck Foundation
- Novo Nordisk Foundation
- Eiffel PhD fellowship from the Eiffel Excellence Scholarship Programme
- Ligue Nationale Contre le Cancer
- Wellcome Trust [097383]
- UK Medical Research Council
- Algerian Ministry of Higher Education
- Ligue Nationale Contre le Cancer [GB/MA/VSP-11059]
- Medical Research Council [MC_UU_12018/23] Funding Source: researchfish
- Villum Fonden [00007292] Funding Source: researchfish
- MRC [MC_UU_12018/23] Funding Source: UKRI
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The nuclear cap-binding complex (CBC) stimulates processing reactions of capped RNAs, including their splicing, 30-end formation, degradation, and transport. CBC effects are particular for individual RNA families, but how such selectivity is achieved remains elusive. Here, we analyze three mainCBC partners known to impact different RNA species. ARS2 stimulates 3'-end formation/transcription termination of several transcript types, ZC3H18 stimulates degradation of a diverse set of RNAs, and PHAX functions in pre-small nuclear RNA/small nucleolar RNA (pre-snRNA/snoRNA) transport. Surprisingly, these proteins all bind capped RNAs without strong preferences for given transcripts, and their steadystate binding correlates poorly with their function. Despite this, PHAX and ZC3H18 compete for CBC binding and we demonstrate that this competitive binding is functionally relevant. We further show that CBC-containing complexes are short lived in vivo, and we therefore suggest that RNA fate involves the transient formation of mutually exclusive CBC complexes, which may only be consequential at particular checkpoints during RNA biogenesis.
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