GW bodies (GWBs) are cytoplasmic foci initially identified through the use of an autoimmune serum targeting the marker protein GW182. GWBs were first considered as both storage centers for a specific subset of mRNAs and degradation sites for mRNAs.
Interestingly, they are known to vary in size and number throughout the cell cycle and are largest in size and most abundant in number during the late S and G2 phases. Recent studies have linked RNA interference to GWBs, in that disruption or disassembly of GWBs was demonstrated to impair siRNA and miRNA silencing activity. As miRNAs are implicated in the regulation of cell cycle progression and cell proliferation, it is very likely that GWBs, the critical intracellular structures for miRNA function, may very well be linked to this cellular process.
Fredenburg, K.M. and Chan, E.K. Our journey from the study of human autoantibodies to the microRNA world. Front Immunol. 6:110.
Yao, B., La, L.B., Chen, Y.C., Chang, L.J., and Chan, E.K. Defining a new role of GW182 in maintaining miRNA stability. EMBO Rep. 13:1102-8.
Yao, B., Li, S., Lian, S.L., Fritzler, M.J., and Chan, E.K. Mapping of Ago2-GW182 functional interactions. Methods Mol. Biol. 725:45-62.
Yao, B., Li. S., Jung, H.M., Lian, S.L., Abadal, G.X., Han, F., Fritzler, M.J., and Chan, E.K. Divergent GW182 functional domains in the regulation of translational silencing. Nucleic Acids Res. 39:2534-47.
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Pauley, K.M., Satoh, M., Pauley, B.A., Dominguez-Gutierrez, P.R., Wallet, S.M., Holliday, L.S., Cha, S., Reeves, W.H., and Chan, E.K. Formation of GW/P bodies as marker for microRNA-mediated regulation of innate immune signaling in THP-1 cells. Immunol. Cell Biol. 88:205-12.
Lian, S.L., Li. S., Abadal, G.X., Pauley, B.A., Fritzler, M.J., and Chan, E.K. The C-terminal half of human Ago2 binds to multiple GW-rich regions of GW182 and requires GW182 to mediate silencing. RNA 15:804-13.
Moser, J.J., Chan, E.K., and Fritzler, M.J. Optimization of immunoprecipitation-western blot analysis in detecting GW182-associated components of GW/P Bodies. Nat Protoc. 4:674-85.
Li, S., Lian, S.L., Moser, J.J., Fritzler, M.L., Fritzler, M.J., Satoh, M., and Chan, E.K. Identification of GW182 and its novel isoform TNGW1 as translational repressors in Ago2 mediated silencing. J. Cell Sci. 121:4134-44.
Moser, J.J., Eystathioy, T., Chan, E.K., and Fritzler, M.J. Markers of mRNA stabilization, degradation and RNAi within astrocytoma GW bodies. J. Neuroscience Research, 85:3619-3631.
Bhanji, R.A., Eystathioy, T., Chan, E.K., Bloch, D.B., and Fritzler, M.J. Clinical and serological features of patients with autoantibodies to GW/P Bodies. Clin. Immunol., 125:247-25.
Lian, S., Fritzler, M.J., Katz, J., Hamazaki, T., Terada, N., Satoh, M., and Chan, E.K. Small interfering RNA-mediated silencing induces target-dependent assembly of GW/P bodies. Mol. Biol. Cell, 18:3375-87.
Jakymiw, A., Pauley, K.M., Li, S., Lian, S., Ikeda, K., Eystathioy, T., Satoh, M., Fritzler, M.J., and Chan, E.K. The role of GW/P-bodies in RNA processing and silencing. J. Cell Sci., 120:1317-23.
Ikeda, K., Satoh, M., Pauley, K.M., Fritzler, M.J., Reeves, W.H., and Chan, E.K. Detection of the argonaute protein Ago2 and microRNAs in the RNA induced silencing complex (RISC) using a monoclonal antibody. J. Immunol. Methods, 317:38-44.
Pauley, K.M., Eystathioy, T., Jakymiw, A., Hamel J.C., Fritzler, M.J., and Chan, E.K. Formation of GW bodies is a consequence of miRNA genesis. EMBO Reports. 7:904-910.
Jakymiw, A., Ikeda, K., Fritzler, M.J., Reeves, W.H., Satoh, M., and Chan, E.K. Autoimmune targeting of key components of RNA interference. Arthritis Res. Ther., 8:R87.
Lian, S., Jakymiw, A., Eystathioy, T., Hamel, J.C., Fritzler, M.J., and Chan, E.K. GW bodies, microRNAs and the cell cycle. Cell Cycle 5:242-5.
Jakymiw, A., Lian, S., Eystathioy, T., Li, S., Satoh, M., Hamel J.C., Fritzler, M.J., and Chan, E.K. Disruption of GW bodies impairs mammalian RNA Interference. Nature Cell Biology 7:1167-74.
Yang, Z., Jakymiw, A., Wood, M.R., Eystathioy, T., Rubin, R.L., Fritzler, M.J., and Chan, E.K. GW182 is critical for the stability of GW bodies expressed during the cell cycle and cell proliferation. J. Cell Science 117:5567-78.
Eystathioy, T., Chan, E.K., Mahler, M., Luft, L.M., Fritzler, M.L., and Fritzler, M.J. A panel of monoclonal antibodies to cytoplasmic GW bodies and the mRNA binding protein GW182. Hybridoma & Hybridomics, 22:79-86.
Eystathioy, T., Jakymiw, A., Chan, E.K., Séraphin, B., Cougot, N., and Fritzler, M.J. The GW182 protein co-localizes with mRNA degradation associated proteins hDcp1 and hLSm4 in cytoplasmic GW bodies. RNA 9:1171-1173.
Eystathioy, T., Chan, E.K., Takeuchi, K., Mahler, M., Luft, L.M., Zochodne, D.W., and Fritzler, M.J. Clinical and serological associations of autoantibodies to GW bodies and a novel cytoplasmic autoantigen GW182. J. Mol. Med., 81:811-818.
Eystathioy, T., Chan, E.K., Tenenbaum, S.A., Keene, J.D., Griffith, K., and Fritzler, M.J. A phosphorylated cytoplasmic autoantigen, GW182, associates with a unique population of human mRNAs within novel cytoplasmic speckles. Mol. Biol. Cell 13: 1338-51.