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dc.contributor.authorBridges, Andrew A.  Concept link
dc.contributor.authorZhang, Huaiying  Concept link
dc.contributor.authorMehta, Shalin B.  Concept link
dc.contributor.authorOcchipinti, Patricia  Concept link
dc.contributor.authorTani, Tomomi  Concept link
dc.contributor.authorGladfelter, Amy S.  Concept link
dc.date.accessioned2014-03-28T19:43:06Z
dc.date.available2014-10-22T08:57:26Z
dc.date.issued2013-12
dc.identifier.urihttps://hdl.handle.net/1912/6518
dc.descriptionAuthor Posting. © The Author(s), 2013. This is the author's version of the work. It is posted here by permission of National Academy of Sciences for personal use, not for redistribution. The definitive version was published in Proceedings of the National Academy of Sciences of the United States of America 111 (2014): 2146-2151, doi:10.1073/pnas.1314138111.en_US
dc.description.abstractSeptins assemble into filaments and higher-order structures that act as scaffolds for diverse cell functions including cytokinesis, cell polarity, and membrane remodeling. Despite their conserved role in cell organization, little is known about how septin filaments elongate and are knit together into higher-order assemblies. Using fluorescence correlation spectroscopy (FCS), we determined that cytosolic septins are in small complexes suggesting that septin filaments are not formed in the cytosol. When the plasma membrane of live cells is monitored by total internal reflection fluorescence (TIRF) microscopy, we see that septin complexes of variable size diffuse in two dimensions. Diffusing septin complexes collide and make end-on associations to form elongated filaments and higher-order structures, an assembly process we call annealing. Septin assembly by annealing can be reconstituted in vitro on supported lipid bilayers with purified septin complexes. Using the reconstitution assay, we show that septin filaments are highly flexible, grow only from free filament ends and do not exchange subunits in the middle of filaments. This work shows for the first time that annealing is an intrinsic property of septins in the presence of membranes and demonstrates that cells exploit this mechanism to build large septin assemblies.en_US
dc.description.sponsorshipThis project was supported with funding from by NSF (MCB-507511, ASG) and NIH (GM100160, TT and ASG), and Colwin, Lemann and Spiegel summer fellowships and The Nikon Award for summer investigation at MBL in Woods Hole, MA (ASG) and instrument support from Micro Video Instruments (MVI).en_US
dc.format.mimetypeapplication/pdf
dc.language.isoen_USen_US
dc.relation.urihttps://doi.org/10.1073/pnas.1314138111
dc.subjectCytoskeletonen_US
dc.subjectSeptinen_US
dc.subjectPlasma membraneen_US
dc.subjectDiffusionen_US
dc.subjectAnnealingen_US
dc.titleSeptin assemblies form by diffusion-driven annealing on membranesen_US
dc.typePreprinten_US
dc.description.embargo2014-07-27en_US


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