BRF1 Complex recruits RNA degradation activities

Stable Identifier
R-HSA-450488
Type
Reaction [binding]
Species
Homo sapiens
Compartment
cytosol
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BRF1 Complex recruits RNA degradation activities
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BRF1 recruits RNA degradation activities to hydrolyze the RNA bound to BRF1. Coimmunoprecipitation has shown BRF1 interacts with the exosome (3' to 5' nuclease), XRN1 (5' to 3' nuclease), and DCP1a and DCP2 (decapping). BRF1 localizes RNAs to processing bodies, sites of translation repression and possible sites of RNA degradation.

Literature References
PubMed ID Title Journal Year
15687258 Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1

Lykke-Andersen, J, Wagner, E

Genes Dev 2005
11719186 AU binding proteins recruit the exosome to degrade ARE-containing mRNAs

Chen, CY, Gherzi, R, Ong, SE, Chan, EL, Raijmakers, R, Pruijn, GJ, Stoecklin, G, Moroni, C, Mann, M, Karin, M

Cell 2001
14976220 Roles of AUF1 isoforms, HuR and BRF1 in ARE-dependent mRNA turnover studied by RNA interference

Raineri, I, Wegmueller, D, Gross, B, Certa, U, Moroni, C

Nucleic Acids Res 2004
17369404 TTP and BRF proteins nucleate processing body formation to silence mRNAs with AU-rich elements

Franks, TM, Lykke-Andersen, J

Genes Dev 2007
Participants
Input
Output
Participant Of
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Orthologous Events
BRF1 Complex recruits RNA degradation activities (Caenorhabditis elegans)
BRF1 Complex recruits RNA degradation activities (Canis familiaris)
BRF1 Complex recruits RNA degradation activities (Danio rerio)
BRF1 Complex recruits RNA degradation activities (Dictyostelium discoideum)
BRF1 Complex recruits RNA degradation activities (Drosophila melanogaster)
BRF1 Complex recruits RNA degradation activities (Gallus gallus)
BRF1 Complex recruits RNA degradation activities (Mus musculus)
BRF1 Complex recruits RNA degradation activities (Rattus norvegicus)
BRF1 Complex recruits RNA degradation activities (Xenopus tropicalis)
Authored
May, B  (2009-12-29)
Reviewed
Wilusz, J  (2010-06-29)
Created
May, B  (2009-12-17)
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