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000128225 0247_ $$2doi$$a10.1016/j.celrep.2017.06.091
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000128225 041__ $$aeng
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000128225 1001_ $$aVindry, Caroline$$b0
000128225 245__ $$aDual RNA Processing Roles of Pat1b via Cytoplasmic Lsm1-7 and Nuclear Lsm2-8 Complexes.
000128225 260__ $$aMaryland Heights, MO$$bCell Press$$c2017
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000128225 520__ $$aPat1 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.
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000128225 7001_ $$aMarnef, Aline$$b1
000128225 7001_ $$aBroomhead, Helen$$b2
000128225 7001_ $$aTwyffels, Laure$$b3
000128225 7001_ $$aOzgur, Sevim$$b4
000128225 7001_ $$0P:(DE-HGF)0$$aStoecklin, Georg$$b5
000128225 7001_ $$aLlorian, Miriam$$b6
000128225 7001_ $$aSmith, Christopher W$$b7
000128225 7001_ $$aMata, Juan$$b8
000128225 7001_ $$aWeil, Dominique$$b9
000128225 7001_ $$aStandart, Nancy$$b10
000128225 773__ $$0PERI:(DE-600)2649101-1$$a10.1016/j.celrep.2017.06.091$$gVol. 20, no. 5, p. 1187 - 1200$$n5$$p1187 - 1200$$tCell reports$$v20$$x2211-1247$$y2017
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000128225 9141_ $$y2017
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