heterogeneous nuclear ribonucleoprotein group m

Summary

Summary: A group of closely-related 72-74-kDa heterogeneous-nuclear ribonucleoproteins that are involved in RNA SPLICING events.

Top Publications

  1. Hovhannisyan R, Carstens R. Heterogeneous ribonucleoprotein m is a splicing regulatory protein that can enhance or silence splicing of alternatively spliced exons. J Biol Chem. 2007;282:36265-74 pubmed
  2. Laguinge L, Bajenova O, Bowden E, Sayyah J, Thomas P, Juhl H. Surface expression and CEA binding of hnRNP M4 protein in HT29 colon cancer cells. Anticancer Res. 2005;25:23-31 pubmed
    ..Future experiments will elucidate whether the CEA-CEAR interaction is involved in CEA's antiapoptotic role and mediates the prometastatic properties of CEA in colon cancer cells. ..
  3. Datar K, Dreyfuss G, Swanson M. The human hnRNP M proteins: identification of a methionine/arginine-rich repeat motif in ribonucleoproteins. Nucleic Acids Res. 1993;21:439-46 pubmed
    ..Proteins immunologically related to M exist in divergent eukaryotes ranging from human to yeast. ..
  4. Gattoni R, Mahe D, Mahl P, Fischer N, Mattei M, Stevenin J, et al. The human hnRNP-M proteins: structure and relation with early heat shock-induced splicing arrest and chromosome mapping. Nucleic Acids Res. 1996;24:2535-42 pubmed
    ..Taken together, our data suggest that these proteins are involved in splicing as well as in early stress-induced splicing arrest. Further in situ hybridization assays located the hnRNP-M encoding gene on human chromosome 19. ..
  5. Vertegaal A, Ogg S, Jaffray E, Rodriguez M, Hay R, Andersen J, et al. A proteomic study of SUMO-2 target proteins. J Biol Chem. 2004;279:33791-8 pubmed
    ..SART1 and heterogeneous nuclear RNP M were both shown to be genuine SUMO targets, confirming the validity of the approach. ..
  6. Blanck O, Perrin C, Mziaut H, Darbon H, Mattei M, Miquelis R. Molecular cloning, cDNA analysis, and localization of a monomer of the N-acetylglucosamine-specific receptor of the thyroid, NAGR1, to chromosome 19p13.3-13.2. Genomics. 1994;21:18-26 pubmed
    ..The intracellular domain contained what appeared to be a tyrosine internalization signal. The usefulness of this clone in glycobiology, cell biology, and thyroid pathology studies is discussed. ..
  7. Llères D, Denegri M, Biggiogera M, Ajuh P, Lamond A. Direct interaction between hnRNP-M and CDC5L/PLRG1 proteins affects alternative splice site choice. EMBO Rep. 2010;11:445-51 pubmed publisher
    ..hnRNP-M affects both 5' and 3' alternative splice site choices, and an hnRNP-M mutant lacking the CDC5L/PLRG1 interaction domain is unable to modulate alternative splicing of an adeno-E1A mini-gene substrate. ..
  8. Blanck O, Perrin C, Mziaut H, Darbon H, Mattei M, Miquelis R. Molecular cloning, cDNA analysis, and localization of a monomer of the N-acetylglucosamine-specific receptor of the thyroid, NAGR1, to chromosome 19p13.3-13.2. Genomics. 1995;27:561 pubmed
  9. Marko M, Leichter M, Patrinou Georgoula M, Guialis A. hnRNP M interacts with PSF and p54(nrb) and co-localizes within defined nuclear structures. Exp Cell Res. 2010;316:390-400 pubmed publisher
    ..Together our data provide new insights and some functional implications on the hnRNP M network of interactions. ..

More Information

Publications21

  1. Hutten S, Wälde S, Spillner C, Hauber J, Kehlenbach R. The nuclear pore component Nup358 promotes transportin-dependent nuclear import. J Cell Sci. 2009;122:1100-10 pubmed publisher
    ..Importantly, the import rate of other transportin-dependent proteins was also significantly reduced in Nup358-depleted cells. Our data therefore suggest a general role for Nup358 in transportin-mediated nuclear import. ..
  2. Russo A, Cirulli C, Amoresano A, Pucci P, Pietropaolo C, Russo G. cis-acting sequences and trans-acting factors in the localization of mRNA for mitochondrial ribosomal proteins. Biochim Biophys Acta. 2008;1779:820-9 pubmed publisher
  3. Jorba N, Juarez S, Torreira E, Gastaminza P, Zamarreño N, Albar J, et al. Analysis of the interaction of influenza virus polymerase complex with human cell factors. Proteomics. 2008;8:2077-88 pubmed publisher
    ..The interactions recognised in this proteomic approach suggest that the influenza polymerase might be involved in steps of the infection cycle other than RNA replication and transcription. ..
  4. Mahe D, Fischer N, Decimo D, Fuchs J. Spatiotemporal regulation of hnRNP M and 2H9 gene expression during mouse embryonic development. Biochim Biophys Acta. 2000;1492:414-24 pubmed
    ..The complex spatiotemporal variations we observed might well anticipate a role for these two hnRNPs also in modulating splicing, thereby influencing gene expression and further many physiological processes. ..
  5. Hase M, Yalamanchili P, Visa N. The Drosophila heterogeneous nuclear ribonucleoprotein M protein, HRP59, regulates alternative splicing and controls the production of its own mRNA. J Biol Chem. 2006;281:39135-41 pubmed
    ..We propose that the ability of HRP59 to regulate the alternative splicing of its own pre-mRNA serves in a negative feedback loop that controls the levels of the HRP59 protein and maintains the homeostasis of the splicing environment. ..
  6. Forsman A, Ruetschi U, Ekholm J, Rymo L. Identification of intracellular proteins associated with the EBV-encoded nuclear antigen 5 using an efficient TAP procedure and FT-ICR mass spectrometry. J Proteome Res. 2008;7:2309-19 pubmed publisher
    ..Our study also confirms previously identified interactors including HA95, Hsp70, Hsc70, Hsp27, HAX-1, Prolyl 4-hydroxylase, S3a, and alpha- and beta-tubulin. ..
  7. Kiesler E, Hase M, Brodin D, Visa N. Hrp59, an hnRNP M protein in Chironomus and Drosophila, binds to exonic splicing enhancers and is required for expression of a subset of mRNAs. J Cell Biol. 2005;168:1013-25 pubmed
    ..We also show that Hrp59 binds preferentially to exonic splicing enhancers and our results provide new insights into the role of hnRNP M in splicing regulation...
  8. Bajenova O, Stolper E, Gapon S, Sundina N, Zimmer R, Thomas P. Surface expression of heterogeneous nuclear RNA binding protein M4 on Kupffer cell relates to its function as a carcinoembryonic antigen receptor. Exp Cell Res. 2003;291:228-41 pubmed
  9. Gulesserian T, Engidawork E, Fountoulakis M, Lubec G. Decreased brain levels of Lupus La protein and increased U5 small ribonucleoprotein-specific 40 kDa protein in fetal Down syndrome. Cell Mol Biol (Noisy-le-grand). 2003;49:733-8 pubmed
    ..Aberrant expression of these proteins points to the fact that dysregulation of the splicing and translation processes is apparent early in prenatal life, and may contribute to the defective growth and differentiation in Down syndrome. ..
  10. Hung C, Lee Y, Chen D, Li C. Proteomic analysis of methylarginine-containing proteins in HeLa cells by two-dimensional gel electrophoresis and immunoblotting with a methylarginine-specific antibody. Protein J. 2009;28:139-47 pubmed publisher
    ..In this study we identified methylarginine-containing proteins in HeLa cells through proteomic approaches and the method is fast and robust for further applications. ..
  11. Pahlich S, Quero L, Roschitzki B, Leemann Zakaryan R, Gehring H. Analysis of Ewing sarcoma (EWS)-binding proteins: interaction with hnRNP M, U, and RNA-helicases p68/72 within protein-RNA complexes. J Proteome Res. 2009;8:4455-65 pubmed publisher
  12. Chiodi I, Biggiogera M, Denegri M, Corioni M, Weighardt F, Cobianchi F, et al. Structure and dynamics of hnRNP-labelled nuclear bodies induced by stress treatments. J Cell Sci. 2000;113 ( Pt 22):4043-53 pubmed
    ..BrU incorporation experiments demonstrate that no transcription occurs within the stress-induced clusters of perichromatin granules, which are depots for RNAs synthesised both before and after heat shock. ..