| Abstract: | HnRNP A2 is an RNA trafficking protein that binds to a specific cis‐acting RNA trafficking element (A2RE) in myelin basic protein RNA and other transported RNAs. A2RE/hnRNPA2 determinants mediate several different steps in RNA trafficking including granule assembly, transport to the plus ends of microtubules and translational activation. A yeast two hybrid screen designed to identify proteins that interact with hnRNP A2 selected a clone corresponding to the carboxyl terminal portion of TOG (tumor overexpressed gene), a microtubule‐associated protein that regulates microtubule dynamics. Co‐immunostaining of oligodendrocytes with antibody to hnRNPA2 and TOG revealed extensive colocalization of TOG with hnRNP A2 granules in the dendrites. A small population of hnRNP A2 granules lacked TOG and some regions of TOG staining lacked hnRNP A2. In oligodendrocytes injected with fluorescent A2RE RNA and stained for TOG, granules containing fluorescent RNA colocalized with TOG. Co‐injection of anti‐TOG antibody with fluorescent A2RE RNA decreased colocalization with TOG and increased transport of the injected RNA. These observations suggest that molecular interaction between hnRNP A2 and TOG serves to anchor A2RE mRNAs/hnRNPA2 granules at plus ends of microtubules. Acknowledgements: Supported by NIH NS19943 (EB) and NS15190 (JHC), and NMSS RG2843 (EB). |
