By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators discuss new findings in Cytoskeletal Proteins. According to news reporting originating in Burlington, Vermont, by NewsRx journalists, research stated, "A hallmark of class-V myosins is their processivity-the ability to take multiple steps along actin filaments without dissociating. Our previous work suggested, however, that the fission yeast myosin-V (Myo52p) is a nonprocessive motor whose activity is enhanced by tropomyosin (Cdc8p)."
The news reporters obtained a quote from the research from the University of Vermont, "Here we investigate the molecular mechanism and physiological relevance of tropomyosin-mediated regulation of Myo52p transport, using a combination of in vitro and in vivo approaches. Single molecules of Myo52p, visualized by total internal reflection fluorescence microscopy, moved processively only when Cdc8p was present on actin filaments. Small ensembles of Myo52p bound to a quantum dot, mimicking the number of motors bound to physiological cargo, also required Cdc8p for continuous motion. Although a truncated form of Myo52p that lacked a cargo-binding domain failed to support function in vivo, it still underwent actin-dependent movement to polarized growth sites. This result suggests that truncated Myo52p lacking cargo, or single molecules of wild-type Myo52p with small cargoes, can undergo processive movement along actin-Cdc8p cables in vivo."
According to the news reporters, the research concluded: "Our findings outline a mechanism by which tropomyosin facilitates sorting of transport to specific actin tracks within the cell by switching on myosin processivity."
For more information on this research see: Fission yeast tropomyosin specifies directed transport of myosin-V along actin cables. Molecular Biology of the Cell, 2014;25(1):66-75. Molecular Biology of the Cell can be contacted at: Amer Soc Cell Biology, 8120 Woodmont Ave, Ste 750, Bethesda, MD 20814-2755, USA (see also Cytoskeletal Proteins).
Our news correspondents report that additional information may be obtained by contacting J.E. Clayton, Univ Vermont, Dept. of Mol Physiol & Biophys, Burlington, VT 05405, United States. Additional authors for this research include L.W. Pollard, M. Sckolnick, C.S. Bookwalter, A.R. Hodges, K.M. Trybus and M. Lord.
Keywords for this news article include: Vermont, Burlington, Tropomyosin, United States, Muscle Proteins, Cytoskeletal Proteins, Microfilament Proteins, North and Central America
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