In:
RNA, Cold Spring Harbor Laboratory, Vol. 21, No. 2 ( 2015-02), p. 262-278
Abstract:
The nuclear exosome targeting complex (NEXT) directs a major 3′–5′ exonuclease, the RNA exosome, for degradation of nuclear noncoding (nc) RNAs. We identified the RNA-binding component of the NEXT complex, RBM7, as a substrate of p38 MAPK /MK2-mediated phosphorylation at residue S136. As a result of this phosphorylation, RBM7 displays a strongly decreased RNA-binding capacity, while inhibition of p38 MAPK or mutation of S136A in RBM7 increases its RNA association. Interestingly, promoter-upstream transcripts (PROMPTs), such as proRBM39, proEXT1, proDNAJB4, accumulated upon stress stimulation in a p38 MAPK /MK2-dependent manner, a process inhibited by overexpression of RBM7 S136A . While there are no stress-dependent changes in RNA-polymerase II (RNAPII) occupation of PROMPT regions representing unchanged transcription, stability of PROMPTs is increased. Hence, we propose that phosphorylation of RBM7 by the p38 MAPK /MK2 axis increases nuclear ncRNA stability by blocking their RBM7-binding and subsequent RNA exosome targeting to allow stress-dependent modulations of the noncoding transcriptome.
Type of Medium:
Online Resource
ISSN:
1355-8382
,
1469-9001
DOI:
10.1261/rna.048090.114
Language:
English
Publisher:
Cold Spring Harbor Laboratory
Publication Date:
2015
detail.hit.zdb_id:
1475737-0
SSG:
12
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