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A more recent version of this article appeared on April 1, 2005
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Submitted on August 17, 2004
Revised on December 27, 2004
Accepted on January 26, 2005
*Department of Neuroscience, Neuroscience Graduate Program, and Department of Molecular, Microbial, and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030
Monitoring Editor: Marvin P. Wickens
In neural cells, such as oligodendrocytes and neurons, transport of certain RNAs along microtubules is mediated by the cis-acting A2RE trafficking element and the cognate trans-acting hnRNP A2 trafficking factor. Using a yeast two-hybrid screen we have identified a microtubule associated protein, TOG2, as an hnRNP A2 binding partner. The C-terminal third of TOG2 is sufficient for hnRNP A2 binding. TOG2, the large protein isoform of the tumor overexpressed gene (TOG), is the only isoform detected in oligodendrocytes in culture. TOG coimmunoprecipitates with hnRNP A2 present in the cytoskeleton (CSK) fraction of neural cells, and both coprecipitate with microtubule stabilized pellets. Staining with anti-TOG reveals puncta that are localized in proximity to microtubules, often at the plus ends. TOG is colocalized with hnRNP A2 and A2RE-mRNA in trafficking granules that remain associated with CSK-insoluble tissue. These data suggest that TOG mediates the association of hnRNP A2-positive granules with microtubules during transport and/or localization.
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