TY  - JOUR
AU  - Vindry, Caroline
AU  - Marnef, Aline
AU  - Broomhead, Helen
AU  - Twyffels, Laure
AU  - Ozgur, Sevim
AU  - Stoecklin, Georg
AU  - Llorian, Miriam
AU  - Smith, Christopher W
AU  - Mata, Juan
AU  - Weil, Dominique
AU  - Standart, Nancy
TI  - Dual RNA Processing Roles of Pat1b via Cytoplasmic Lsm1-7 and Nuclear Lsm2-8 Complexes.
JO  - Cell reports
VL  - 20
IS  - 5
SN  - 2211-1247
CY  - Maryland Heights, MO
PB  - Cell Press
M1  - DKFZ-2017-04242
SP  - 1187 - 1200
PY  - 2017
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:28768202
C2  - pmc:PMC5554784
DO  - DOI:10.1016/j.celrep.2017.06.091
UR  - https://inrepo02.dkfz.de/record/128225
ER  -