Skip to main page content
U.S. flag

An official website of the United States government

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2003 Oct;9(10):1171-3.
doi: 10.1261/rna.5810203.

The GW182 protein colocalizes with mRNA degradation associated proteins hDcp1 and hLSm4 in cytoplasmic GW bodies

The GW182 protein colocalizes with mRNA degradation associated proteins hDcp1 and hLSm4 in cytoplasmic GW bodies

Theophany Eystathioy et al. RNA. 2003 Oct.

Abstract

A novel cytoplasmic compartment referred to as GW bodies (GWBs) was initially identified using antibodies specific to a 182-kD protein termed GW182. GW182 was characterized by multiple glycine(G)-tryptophan(W) repeats and an RNA recognition motif (RRM) that bound a subset of HeLa cell messenger RNAs (mRNAs). The function of GWBs was not known; however, more recent evidence suggested similarities between GWBs and cytoplasmic structures that contain hLSm proteins and hDcp1, the human homolog to a yeast decapping enzyme subunit. In this study, we used antibodies to hLSm4 and hDcp1 to show that both of these markers of an mRNA degradation pathway colocalize to the same structures as GW182. Our studies demonstrate that GW182, hLSm4, and hDcp1 are found in the same cytoplasmic structures and suggest that GW182 is involved in the same mRNA processing pathway as hLSm4 and hDcp1.

PubMed Disclaimer

Figures

FIGURE 1.
FIGURE 1.
Indirect immunofluorescence (IIF) studies demonstrating that GW bodies colocalize with LSm4 and hDcp1 in HEp-2 cells (Immuno Concepts Inc.) were performed as described previously (Eystathioy et al. 2002a). (A) Cytoplasmic bodies detected with the index human serum #18033 (diluted 1/600) and rabbit anti-hLSm4 antibodies (diluted 1/200). (B) Staining with the mAb anti-GW182 4B6 and rabbit anti-hLSm4 antibodies (diluted 1/200). (C) Staining with the index patient serum #18033 (1/600 dilution) and rabbit anti-hDcp1 antibodies (diluted 1/600). (D) IIF using the mAb 4B6 and the rabbit anti-hDcp1 antibodies (diluted 1/600). The secondary antibodies included Cy3-conjugated anti-human (IgG) and anti-mouse (IgG) antibodies (shown in the first column) and FITC-conjugated anti-rabbit IgG antibodies (shown in the second column). The merged images are shown in the third column, which includes the DAPI-stained nuclei. The scale bars in the left column are equal to 10 μm. The nuclei of cells were stained with DAPI dissolved in glycerol mounting medium (VectaShield: Vector Laboratories).

Similar articles

Cited by

References

    1. Achsel, T., Brahms, H., Kastner, B., Bachi, A., Wilm, M., and Luhrmann, R. 1999. A doughnut-shaped heteromer of human Sm-like proteins binds to the 3′-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro. EMBO J. 18: 5789–5802. - PMC - PubMed
    1. Bollig, F., Winzen, R., Gaestel, M., Kostka, S., Resch, K., and Holtmann, H. 2003. Affinity purification of ARE-binding proteins identifies poly(A)-binding protein 1 as a potential substrate in MK2-induced mRNA stabilization. Biochem. Biophys. Res. Commun. 301: 665–670. - PubMed
    1. Bouveret, E., Rigaut, G., Shevchenko, A., Wilm, M., and Séraphin, B. 2000. A Sm-like protein complex that participates in mRNA degradation. EMBO J. 19: 1661–1671. - PMC - PubMed
    1. Couttet, P., Fromont-Racine, M., Steel, D., Pictet, R., and Grange, T. 1997. Messenger RNA deadenylation precedes decapping in mammalian cells. Proc. Natl. Acad. Sci. 94: 5628–5633. - PMC - PubMed
    1. Denegri, M., Chiodi, I., Corioni, M., Cobianchi, F., Riva, S., and Biamonti, G. 2001. Stress-induced nuclear bodies are sites of accumulation of pre-mRNA processing factors. Mol. Biol. Cell 12: 3502–3514. - PMC - PubMed

Publication types

MeSH terms

LinkOut - more resources