The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci - PubMed (original) (raw)
. 2002 Dec;8(12):1489-501.
Affiliations
- PMID: 12515382
- PMCID: PMC1370355
The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci
Dierk Ingelfinger et al. RNA. 2002 Dec.
Abstract
Sm and Sm-like (LSm) proteins form heptameric complexes that are involved in various steps of RNA metabolism. In yeast, the Lsm1-7 complex functions in mRNA degradation and is associated with several enzymes of this pathway, while the complex LSm2-8, the composition of which largely overlaps with that of LSm1-7, has a role in pre-mRNA splicing. A human gene encoding an LSm1 homolog has been identified, but its role in mRNA degradation has yet to be elucidated. We performed subcellular localization studies and found hLSm1 predominantly in the cytoplasm. However, it is not distributed evenly; rather, it is highly enriched in small, discrete foci. The endogenous hLSm4 is similarly localized, as are the overexpressed proteins hLSm1-7, but not hLSm8. The foci also contain two key factors in mRNA degradation, namely the decapping enzyme hDcp1/2 and the exonuclease hXrn1. Moreover, coexpression of wild-type and mutant LSm proteins, as well as fluorescence resonance energy transfer (FRET) studies, indicate that the mammalian proteins hLSm1-7 form a complex similar to the one found in yeast, and that complex formation is required for enrichment of the proteins in the cytoplasmic foci. Therefore, the foci contain a partially or fully assembled machinery for the degradation of mRNA.
Similar articles
- Yeast Sm-like proteins function in mRNA decapping and decay.
Tharun S, He W, Mayes AE, Lennertz P, Beggs JD, Parker R. Tharun S, et al. Nature. 2000 Mar 30;404(6777):515-8. doi: 10.1038/35006676. Nature. 2000. PMID: 10761922 - mRNA decay: x (XRN1) marks the spot.
Long RM, McNally MT. Long RM, et al. Mol Cell. 2003 May;11(5):1126-8. doi: 10.1016/s1097-2765(03)00198-9. Mol Cell. 2003. PMID: 12769838 Review. - Dual RNA Processing Roles of Pat1b via Cytoplasmic Lsm1-7 and Nuclear Lsm2-8 Complexes.
Vindry C, Marnef A, Broomhead H, Twyffels L, Ozgur S, Stoecklin G, Llorian M, Smith CW, Mata J, Weil D, Standart N. Vindry C, et al. Cell Rep. 2017 Aug 1;20(5):1187-1200. doi: 10.1016/j.celrep.2017.06.091. Cell Rep. 2017. PMID: 28768202 Free PMC article. - Molecular basis for the distinct cellular functions of the Lsm1-7 and Lsm2-8 complexes.
Montemayor EJ, Virta JM, Hayes SM, Nomura Y, Brow DA, Butcher SE. Montemayor EJ, et al. RNA. 2020 Oct;26(10):1400-1413. doi: 10.1261/rna.075879.120. Epub 2020 Jun 9. RNA. 2020. PMID: 32518066 Free PMC article. - mRNA decapping activities and their biological roles.
LaGrandeur TE, Parker R. LaGrandeur TE, et al. Biochimie. 1996;78(11-12):1049-55. doi: 10.1016/s0300-9084(97)86729-6. Biochimie. 1996. PMID: 9150884 Review.
Cited by
- Who Regulates Whom? An Overview of RNA Granules and Viral Infections.
Poblete-Durán N, Prades-Pérez Y, Vera-Otarola J, Soto-Rifo R, Valiente-Echeverría F. Poblete-Durán N, et al. Viruses. 2016 Jun 28;8(7):180. doi: 10.3390/v8070180. Viruses. 2016. PMID: 27367717 Free PMC article. Review. - Cytoplasmic Ribonucleoprotein Foci in Eukaryotes: Hotspots of Bio(chemical)Diversity.
Layana C, Ferrero P, Rivera-Pomar R. Layana C, et al. Comp Funct Genomics. 2012;2012:504292. doi: 10.1155/2012/504292. Epub 2012 May 27. Comp Funct Genomics. 2012. PMID: 22693427 Free PMC article. - New insights into the regulation of RNP granule assembly in oocytes.
Schisa JA. Schisa JA. Int Rev Cell Mol Biol. 2012;295:233-89. doi: 10.1016/B978-0-12-394306-4.00013-7. Int Rev Cell Mol Biol. 2012. PMID: 22449492 Free PMC article. Review. - Rpm2p, a protein subunit of mitochondrial RNase P, physically and genetically interacts with cytoplasmic processing bodies.
Stribinskis V, Ramos KS. Stribinskis V, et al. Nucleic Acids Res. 2007;35(4):1301-11. doi: 10.1093/nar/gkm023. Epub 2007 Jan 31. Nucleic Acids Res. 2007. PMID: 17267405 Free PMC article. - Identification and characterization of human Mex-3 proteins, a novel family of evolutionarily conserved RNA-binding proteins differentially localized to processing bodies.
Buchet-Poyau K, Courchet J, Le Hir H, Séraphin B, Scoazec JY, Duret L, Domon-Dell C, Freund JN, Billaud M. Buchet-Poyau K, et al. Nucleic Acids Res. 2007;35(4):1289-300. doi: 10.1093/nar/gkm016. Epub 2007 Jan 31. Nucleic Acids Res. 2007. PMID: 17267406 Free PMC article.
References
- J Cell Biol. 1997 Feb 24;136(4):761-73 - PubMed
- EMBO J. 1996 May 1;15(9):2256-69 - PubMed
- Cell. 1997 Sep 19;90(6):1023-9 - PubMed
- Mol Cell Biol. 1998 Apr;18(4):1956-66 - PubMed
- Mol Cell Biol. 1998 Sep;18(9):5062-72 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous