[{"day":"01","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","type":"journal_article","page":"38 - 46","status":"public","publist_id":"5094","month":"01","year":"2014","extern":"1","date_created":"2018-12-11T11:55:05Z","publisher":"Nature Publishing Group","date_published":"2014-01-01T00:00:00Z","article_processing_charge":"No","_id":"1990","date_updated":"2025-08-05T14:41:58Z","volume":16,"language":[{"iso":"eng"}],"author":[{"full_name":"Loose, Martin","orcid":"0000-0001-7309-9724","last_name":"Loose","id":"462D4284-F248-11E8-B48F-1D18A9856A87","first_name":"Martin"},{"last_name":"Mitchison","full_name":"Mitchison, Timothy","first_name":"Timothy"}],"title":"The bacterial cell division proteins ftsA and ftsZ self-organize into dynamic cytoskeletal patterns","publication_status":"published","external_id":{"pmid":["24316672"]},"acknowledgement":"M.L. is supported by fellowships from EMBO (ALTF 394-2011) and HFSP (LT000466/2012). Cytoskeleton dynamics research in the T.J.M. group is supported by NIH-GM39565.","oa_version":"None","abstract":[{"text":"Bacterial cytokinesis is commonly initiated by the Z-ring, a cytoskeletal structure that assembles at the site of division. Its primary component is FtsZ, a tubulin superfamily GTPase, which is recruited to the membrane by the actin-related protein FtsA. Both proteins are required for the formation of the Z-ring, but if and how they influence each other's assembly dynamics is not known. Here, we reconstituted FtsA-dependent recruitment of FtsZ polymers to supported membranes, where both proteins self-organize into complex patterns, such as fast-moving filament bundles and chirally rotating rings. Using fluorescence microscopy and biochemical perturbations, we found that these large-scale rearrangements of FtsZ emerge from its polymerization dynamics and a dual, antagonistic role of FtsA: recruitment of FtsZ filaments to the membrane and negative regulation of FtsZ organization. Our findings provide a model for the initial steps of bacterial cell division and illustrate how dynamic polymers can self-organize into large-scale structures.","lang":"eng"}],"doi":"10.1038/ncb2885","pmid":1,"citation":{"short":"M. Loose, T. Mitchison, Nature Cell Biology 16 (2014) 38–46.","ieee":"M. Loose and T. Mitchison, “The bacterial cell division proteins ftsA and ftsZ self-organize into dynamic cytoskeletal patterns,” <i>Nature Cell Biology</i>, vol. 16. Nature Publishing Group, pp. 38–46, 2014.","ama":"Loose M, Mitchison T. The bacterial cell division proteins ftsA and ftsZ self-organize into dynamic cytoskeletal patterns. <i>Nature Cell Biology</i>. 2014;16:38-46. doi:<a href=\"https://doi.org/10.1038/ncb2885\">10.1038/ncb2885</a>","ista":"Loose M, Mitchison T. 2014. The bacterial cell division proteins ftsA and ftsZ self-organize into dynamic cytoskeletal patterns. Nature Cell Biology. 16, 38–46.","apa":"Loose, M., &#38; Mitchison, T. (2014). The bacterial cell division proteins ftsA and ftsZ self-organize into dynamic cytoskeletal patterns. <i>Nature Cell Biology</i>. Nature Publishing Group. <a href=\"https://doi.org/10.1038/ncb2885\">https://doi.org/10.1038/ncb2885</a>","mla":"Loose, Martin, and Timothy Mitchison. “The Bacterial Cell Division Proteins FtsA and FtsZ Self-Organize into Dynamic Cytoskeletal Patterns.” <i>Nature Cell Biology</i>, vol. 16, Nature Publishing Group, 2014, pp. 38–46, doi:<a href=\"https://doi.org/10.1038/ncb2885\">10.1038/ncb2885</a>.","chicago":"Loose, Martin, and Timothy Mitchison. “The Bacterial Cell Division Proteins FtsA and FtsZ Self-Organize into Dynamic Cytoskeletal Patterns.” <i>Nature Cell Biology</i>. Nature Publishing Group, 2014. <a href=\"https://doi.org/10.1038/ncb2885\">https://doi.org/10.1038/ncb2885</a>."},"intvolume":"        16","publication":"Nature Cell Biology"}]