Key result
She3p acts as an adapter protein that directly binds the myosin motor Myo4p and links it to Ash1 mRNA, while She2p is required to dock the She3p-Myo4p complex onto the mRNA.
Elucidates yeast mRNA-motor linkage; extends prior models and leaves open conservation in mammals.
In Saccharomyces cerevisiae, mRNA encoding the cell-fate determinant Ash1p is localized to the distal tip of daughter cells. Five SHE genes are required for proper Ash1 mRNA localization, one of which encodes the myosin Myo4p. We show that three of the five She proteins, She2p, She3p, and Myo4p, colocalize with Ash1 mRNA in vivo and coimmunoprecipitate with Ash1 mRNA from cell extracts. We also find that She3p binds to Myo4p in the absence of RNA and She2p is required for binding She3p-Myo4p to Ash1 mRNA. These results suggest that She3p acts as an adapter protein that docks the myosin motor onto an Ash1-She2p ribonucleoprotein complex.
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Takizawa et al. (2000) studied Saccharomyces cerevisiae mRNA localization. SHE gene deletion and tagging vs. Wild-type cells was evaluated on Colocalization and coimmunoprecipitation of She proteins with Ash1 mRNA. She3p acts as an adapter protein that directly binds the myosin motor Myo4p and links it to Ash1 mRNA, while She2p is required to dock the She3p-Myo4p complex onto the mRNA.
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