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@ARTICLE{Vindry:128225,
      author       = {C. Vindry and A. Marnef and H. Broomhead and L. Twyffels
                      and S. Ozgur and G. Stoecklin$^*$ and M. Llorian and C. W.
                      Smith and J. Mata and D. Weil and N. Standart},
      title        = {{D}ual {RNA} {P}rocessing {R}oles of {P}at1b via
                      {C}ytoplasmic {L}sm1-7 and {N}uclear {L}sm2-8 {C}omplexes.},
      journal      = {Cell reports},
      volume       = {20},
      number       = {5},
      issn         = {2211-1247},
      address      = {Maryland Heights, MO},
      publisher    = {Cell Press},
      reportid     = {DKFZ-2017-04242},
      pages        = {1187 - 1200},
      year         = {2017},
      abstract     = {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.},
      cin          = {A200},
      ddc          = {570},
      cid          = {I:(DE-He78)A200-20160331},
      pnm          = {311 - Signalling pathways, cell and tumor biology
                      (POF3-311)},
      pid          = {G:(DE-HGF)POF3-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28768202},
      pmc          = {pmc:PMC5554784},
      doi          = {10.1016/j.celrep.2017.06.091},
      url          = {https://inrepo02.dkfz.de/record/128225},
}