Myosin VI Stabilizes an Actin Network during Drosophila Spermatid Individualization.

@article{citeulike:572941, abstract = {Monitoring Editor: David Drubin Here we demonstrate a new function of myosin VI using observations of Drosophila spermatid individualization in vivo. We find that myosin VI stabilizes a branched actin network in actin structures (cones) that mediate the separation of the syncytial spermatids. In a myosin VI mutant, the cones do not accumulate F-actin during cone movement, while over expression of myosin VI leads to bigger cones with more F-actin. Myosin S1-fragment decoration demonstrated that the actin cone is made up of two regions: a dense meshwork at the front and parallel bundles at the rear. The majority of the actin filaments were oriented with their pointed ends facing in the direction of cone movement. Our data also demonstrate that myosin VI binds to the cone front using its motor domain. FRAP experiments using GFP-myosin VI revealed that myosin VI remains bound to F-actin for minutes, suggesting its role is tethering, rather than transporting cargo. We hypothesize that myosin VI protects the actin cone structure either by cross-linking actin filaments or anchoring regulatory molecules at the cone front. These observations uncover a novel mechanism mediated by myosin VI for stabilizing long-lived actin structures in cells.}, address = {Department of Biology, Washington University in St. Louis, St. Louis, MO 63130; Laboratory of Developmental Biology, Institute of General and Molecular Biology, Nicolaus Copernicus University, 87-100 Torun, Poland.}, author = {Noguchi, Tatsuhiko and Lenartowska, Marta and Miller, Kathryn G G. }, citeulike-article-id = {572941}, doi = {http://dx.doi.org/10.1091/mbc.E06-01-0031}, issn = {1059-1524}, journal = {Mol Biol Cell}, keywords = {actin, cytoskeleton, drosophila, indivi, individualization, spermatogenesis}, month = {March}, posted-at = {2006-04-02 05:10:26}, priority = {4}, title = {Myosin VI Stabilizes an Actin Network during Drosophila Spermatid Individualization.}, url = {http://dx.doi.org/10.1091/mbc.E06-01-0031}, year = {2006} }

TY - JOUR ID - citeulike:572941 L3 - citeulike-article-id:572941 N2 - Monitoring Editor: David Drubin Here we demonstrate a new function of myosin VI using observations of Drosophila spermatid individualization in vivo. We find that myosin VI stabilizes a branched actin network in actin structures (cones) that mediate the separation of the syncytial spermatids. In a myosin VI mutant, the cones do not accumulate F-actin during cone movement, while over expression of myosin VI leads to bigger cones with more F-actin. Myosin S1-fragment decoration demonstrated that the actin cone is made up of two regions: a dense meshwork at the front and parallel bundles at the rear. The majority of the actin filaments were oriented with their pointed ends facing in the direction of cone movement. Our data also demonstrate that myosin VI binds to the cone front using its motor domain. FRAP experiments using GFP-myosin VI revealed that myosin VI remains bound to F-actin for minutes, suggesting its role is tethering, rather than transporting cargo. We hypothesize that myosin VI protects the actin cone structure either by cross-linking actin filaments or anchoring regulatory molecules at the cone front. These observations uncover a novel mechanism mediated by myosin VI for stabilizing long-lived actin structures in cells. JF - Mol Biol Cell SN - 1059-1524 AD - Department of Biology, Washington University in St. Louis, St. Louis, MO 63130; Laboratory of Developmental Biology, Institute of General and Molecular Biology, Nicolaus Copernicus University, 87-100 Torun, Poland. TI - Myosin VI Stabilizes an Actin Network during Drosophila Spermatid Individualization. KW - actin KW - cytoskeleton KW - drosophila KW - indivi KW - individualization KW - spermatogenesis AU - Noguchi, Tatsuhiko AU - Lenartowska, Marta AU - Miller, Kathryn G PY - 2006/03/29/ UR - http://dx.doi.org/10.1091/mbc.E06-01-0031 ER -