{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Noguchi T"],"funding":["NIGMS NIH HHS"],"pagination":["2559-71"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC1474903"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(6)"],"pubmed_abstract":["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, whereas overexpression of myosin VI leads to bigger cones with more F-actin. Myosin subfragment 1-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. Fluoresce"],"journal":["Molecular biology of the cell"],"pubmed_title":["Myosin VI stabilizes an actin network during Drosophila spermatid individualization."],"pmcid":["PMC1474903"],"funding_grant_id":["GM-60494","R01 GM060494"],"pubmed_authors":["Noguchi T","Lenartowska M","Miller KG"],"additional_accession":[]},"is_claimable":false,"name":"Myosin VI stabilizes an actin network during Drosophila spermatid individualization.","description":"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, whereas overexpression of myosin VI leads to bigger cones with more F-actin. Myosin subfragment 1-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. Fluoresce","dates":{"release":"2006-01-01T00:00:00Z","publication":"2006 Jun","modification":"2025-04-19T07:23:27.994Z","creation":"2019-03-27T01:45:27Z"},"accession":"S-EPMC1474903","cross_references":{"pubmed":["16571671"],"doi":["10.1091/mbc.e06-01-0031"]}}