title: A large ribonucleoprotein particle induced by cytoplasmic PrP shares striking similarities with the chromatoid body, an RNA granule predicted to function in posttranscriptional gene regulation.
abstract: The observation that PrP is present in the cytosol of some neurons and non-neuronal cells and that the N-terminal signal peptide is slightly inefficient has brought speculations concerning a possible function of the protein in the cytosol. Here, we show that cells expressing a cytosolic form of PrP termed cyPrP display a large juxtanuclear cytoplasmic RNA organelle. Although cyPrP spontaneously forms aggresomes, we used several mutants to demonstrate that the assembly of this RNA organelle is independent from cyPrP aggregation. Components of the organelle fall into three classes: mRNAs; proteins, including the RNAseIII family polymerase Dicer, the decapping enzyme Dcp1a, the DEAD-box RNA helicase DDX6, and the small nuclear ribonucleoprotein-associated proteins SmB/B'/N; and non-coding RNAs, including rRNA 5S, tRNAs, U1 small nuclear RNA, and microRNAs. This composition is similar to RNA granules or chromatoid bodies from germ cells, or planarian stem cells and neurons, which are large ribonucleoprotein complexes predicted to function in RNA processing and posttranscriptional gene regulation. The domain of PrP encompassing residues 30 to 49 is essential for the formation of the RNA particle. Our findings confirm the intriguing relation between PrP and RNA in cells, and underscore an unexpected function for cytosolic PrP: assembling a large RNA processing center which we have termed PrP-RNP for PrP-induced ribonucleoprotein particle.
authors.affiliation: Department of Biochemistry, Faculty of Medicine, University of Sherbrooke, 3001 12(ème) avenue nord, Sherbrooke, Québec, Canada J1H 5N4.
authors.forename: Simon
authors.initials: S
authors.lastname: Beaudoin
authors.forename: Benoît
authors.initials: B
authors.lastname: Vanderperre
authors.forename: Catherine
authors.initials: C
authors.lastname: Grenier
authors.forename: Isabelle
authors.initials: I
authors.lastname: Tremblay
authors.forename: Frederic
authors.initials: F
authors.lastname: Leduc
authors.forename: Xavier
authors.initials: X
authors.lastname: Roucou
mesh_terms: D000818:Animals; D045744:Cell Line, Tumor; D003594:Cytoplasmic Granules / Q000378:metabolism*; D005786:Gene Expression Regulation; D005854:Germ Cells / Q000378:metabolism; D051379:Mice; D009474:Neurons / Q000378:metabolism; D022022:Nuclear Pore / Q000378:metabolism; D010932:Planarians / Q000166:cytology / Q000378:metabolism; D011328:Prions / Q000378:metabolism*; D011485:Protein Binding; D012313:RNA / Q000378:metabolism*; D012337:RNA, Ribosomal, 18S / Q000378:metabolism; D012339:RNA, Ribosomal, 28S / Q000378:metabolism; D012342:RNA, Small Nuclear / Q000378:metabolism; D012343:RNA, Transfer / Q000378:metabolism; D012261:Ribonucleoproteins / Q000737:chemistry / Q000378:metabolism*; D013234:Stem Cells / Q000378:metabolism; D014158:Transcription, Genetic; D014746:Vimentin / Q000378:metabolism
chemical_list: D011328:Prions; D012337:RNA, Ribosomal, 18S; D012339:RNA, Ribosomal, 28S; D012342:RNA, Small Nuclear; D012261:Ribonucleoproteins; C405483:U1 small nuclear RNA; D014746:Vimentin; D012313:RNA; D012343:RNA, Transfer