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A more recent version of this article appeared on April 1, 2002
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Submitted on November 9, 2001
Revised on December 17, 2001
Accepted on January 8, 2002
1 Departments of Medicine and Biochemistry and Molecular Biology, University of Calgary, Calgary, Alberta, Canada
2 W.M. Keck Autoimmune Disease Center, Department of Molecular and Experimental Medicine, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California, 92037
3 Department of Microbiology, Duke University Medical Center, Durham, NC, 27710
* Corresponding author. E-mail address: fritzler{at}ucalgary.ca.
A novel human cellular structure has been identified that contains a unique autoimmune antigen and multiple messenger RNAs. This complex was discovered using an autoimmune serum from a patient with motor and sensory neuropathy and contains a protein of 182 kDa. The gene and cDNA encoding the protein indicated an open reading frame with glycine-tryptophan (GW) repeats and a single RNA recognition motif (RRM)1. Both the patient's serum and a rabbit serum raised against the recombinant GW protein costained discrete cytoplasmic speckles designated as GW bodies (GWBs) that do not overlap with the Golgi complex, endosomes, lysosomes or peroxisomes. The mRNAs associated with GW182 represent a clustered set of transcripts that are presumed to reside within the GW complexes. We propose that the GW ribonucleoprotein complex is involved in the post-transcriptional regulation of gene expression by sequestering a specific subset of gene transcripts involved in cell growth and homeostasis.
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