%0 Journal Article
%A Vindry, Caroline
%A Marnef, Aline
%A Broomhead, Helen
%A Twyffels, Laure
%A Ozgur, Sevim
%A Stoecklin, Georg
%A Llorian, Miriam
%A Smith, Christopher W
%A Mata, Juan
%A Weil, Dominique
%A Standart, Nancy
%T Dual RNA Processing Roles of Pat1b via Cytoplasmic Lsm1-7 and Nuclear Lsm2-8 Complexes.
%J Cell reports
%V 20
%N 5
%@ 2211-1247
%C Maryland Heights, MO
%I Cell Press
%M DKFZ-2017-04242
%P 1187 - 1200
%D 2017
%X Pat1 RNA-binding proteins, enriched in processing bodies (P bodies), are key players in cytoplasmic 5' to 3' mRNA decay, activating decapping of mRNA in complex with the Lsm1-7 heptamer. Using co-immunoprecipitation and immunofluorescence approaches coupled with RNAi, we provide evidence for a nuclear complex of Pat1b with the Lsm2-8 heptamer, which binds to the spliceosomal U6 small nuclear RNA (snRNA). Furthermore, we establish the set of interactions connecting Pat1b/Lsm2-8/U6 snRNA/SART3 and additional U4/U6.U5 tri-small nuclear ribonucleoprotein particle (tri-snRNP) components in Cajal bodies, the site of snRNP biogenesis. RNA sequencing following Pat1b depletion revealed the preferential upregulation of mRNAs normally found in P bodies and enriched in 3' UTR AU-rich elements. Changes in >180 alternative splicing events were also observed, characterized by skipping of regulated exons with weak donor sites. Our data demonstrate the dual role of a decapping enhancer in pre-mRNA processing as well as in mRNA decay via distinct nuclear and cytoplasmic Lsm complexes.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:28768202
%2 pmc:PMC5554784
%R 10.1016/j.celrep.2017.06.091
%U https://inrepo02.dkfz.de/record/128225