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LETTER TO THE EDITOR |
1 Departments of Medicine and Biochemistry and Molecular Biology, University of Calgary, Calgary, Alberta T2N 4N1, Canada
2 Department of Oral Biology, University of Florida, Gainesville, Florida 32611, USA
3 Centre de Génétique Moléculaire, CNRS, Yvette, France
Reprint requests to: Marvin J. Fritzler, Professor, Faculty of Medicine: HRB410B, University of Calgary, 3330 Hospital Dr. NW, Calgary, AB, T2N 4N1 Canada; e-mail: fritzler{at}ucalgary.ca; fax: (403) 283-5666.
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.
Keywords: mRNA; degradation; decapping; GW bodies; LSm
Abbreviations: ARE, AU rich elements; ARED, AU rich element database; DAPI, 4',6-diamidino-2-phenylindole; FRAP, fluorescence resonance after photobleaching; GWBs, glycine tryptophan rich cytoplasmic structures; hDcp, human homolog to a yeast decapping enzyme subunit; IIF, indirect immunofluorescence; IP, immunoprecipitation; LSm, like Sm; mAb, monoclonal antibody; NHS, normal human serum; PBS-T, phosphate buffered saline containing Tween 20; TnT, transcription and translation
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