Regulation of information flow by motor protein systems

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Our major goal of this project is to elucidate structures and functions of motor proteins, especially, unconventional myosin 6 and cytoplasmic dynein. We carried out the yeast two-hybrid screening of interacting partners of myosin 6. We identified several proteins including a membrane-bound tyrosine kinase. We examined in vivo functions of the kinase by using various cell- and molecular-biological techniques such as RNAi. We also examined structure and function of cytoplasmic dynein, using recombinant dynein motor domain. We identified interesting biochemical and structural properties of the motor domain by electron microscopy, rapid kinetics and FRET (fluorescence resonance energy transfer). The data obtained by these experiments will become the basis for understanding cellular functions of motor proteins.