{"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.","status":"public","quality_controlled":0,"title":"The bacterial cell division proteins ftsA and ftsZ self-organize into dynamic cytoskeletal patterns","volume":16,"date_created":"2018-12-11T11:55:05Z","publist_id":"5094","intvolume":"        16","publisher":"Nature Publishing Group","year":"2014","issue":"1","publication_status":"published","extern":1,"citation":{"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>.","ista":"Loose M, Mitchison T. 2014. The bacterial cell division proteins ftsA and ftsZ self-organize into dynamic cytoskeletal patterns. Nature Cell Biology. 16(1), 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>","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(1):38-46. doi:<a href=\"https://doi.org/10.1038/ncb2885\">10.1038/ncb2885</a>","short":"M. Loose, T. Mitchison, Nature Cell Biology 16 (2014) 38–46.","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, no. 1, Nature Publishing Group, 2014, pp. 38–46, doi:<a href=\"https://doi.org/10.1038/ncb2885\">10.1038/ncb2885</a>.","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, no. 1. Nature Publishing Group, pp. 38–46, 2014."},"date_published":"2014-01-01T00:00:00Z","abstract":[{"lang":"eng","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."}],"_id":"1990","page":"38 - 46","doi":"10.1038/ncb2885","day":"01","publication":"Nature Cell Biology","author":[{"orcid":"0000-0001-7309-9724","id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Martin Loose","first_name":"Martin","last_name":"Loose"},{"first_name":"Timothy","last_name":"Mitchison","full_name":"Mitchison, Timothy J"}],"type":"journal_article","date_updated":"2021-01-12T06:54:33Z","month":"01"}