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Vol. 10, Issue 9, 3015-3033, September 1999
and
*Terry Fox Molecular Oncology Group, Lady Davis Institute for
Medical Research, Sir Mortimer B. Davis Jewish General Hospital, and
Departments of Oncology, Medicine, and Microbiology and Immunology,
McGill University, Montréal, Québec H3T 1E2, Canada; and
The GSG (GRP33, Sam68, GLD-1) domain is a protein module found in
an expanding family of RNA-binding proteins. The numerous missense
mutations identified genetically in the GSG domain support its
physiological role. Although the exact function of the GSG domain is
not known, it has been shown to be required for RNA binding and
oligomerization. Here it is shown that the Sam68 GSG domain plays a
role in protein localization. We show that Sam68 concentrates into
novel nuclear structures that are predominantly found in transformed
cells. These Sam68 nuclear bodies (SNBs) are distinct from coiled
bodies, gems, and promyelocytic nuclear bodies. Electron
microscopic studies show that SNBs are distinct structures that are
enriched in phosphorus and nitrogen, indicating the presence of nucleic
acids. A GFP-Sam68 fusion protein had a similar localization as
endogenous Sam68 in HeLa cells, diffusely nuclear with two to five
SNBs. Two other GSG proteins, the Sam68-like mammalian proteins SLM-1
and SLM-2, colocalized with endogenous Sam68 in SNBs. Different GSG
domain missense mutations were investigated for Sam68 protein
localization. Six separate classes of cellular patterns were obtained,
including exclusive SNB localization and association with microtubules.
These findings demonstrate that the GSG domain is involved in protein
localization and define a new compartment for Sam68, SLM-1, and SLM-2
in cancer cell lines.
Department of Cell Biology and Anatomy, University of
Calgary, Calgary, Alberta T2N 4N1, Canada
Corresponding author. E-mail address:
mcrd{at}musica.mcgill.ca.
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