Show simple item record

dc.contributor.authorDeMay, Bradley S.  Concept link
dc.contributor.authorBai, Xiaobo  Concept link
dc.contributor.authorHoward, Louisa  Concept link
dc.contributor.authorOcchipinti, Patricia  Concept link
dc.contributor.authorMeseroll, Rebecca A.  Concept link
dc.contributor.authorSpiliotis, Elias T.  Concept link
dc.contributor.authorOldenbourg, Rudolf  Concept link
dc.contributor.authorGladfelter, Amy S.  Concept link
dc.date.accessioned2011-06-22T15:13:31Z
dc.date.available2011-12-13T09:30:01Z
dc.date.issued2011-06-13
dc.identifier.citationJournal of Cell Biology 193 (2011): 1065-1081en_US
dc.identifier.urihttps://hdl.handle.net/1912/4649
dc.description© The Author(s), 2011. This article is distributed under the terms of the Creative Commons Attribution 3.0 License. The definitive version was published in Journal of Cell Biology 193 (2011): 1065-1081, doi:10.1083/jcb.201012143.en_US
dc.description.abstractThe septins are conserved, GTP-binding proteins important for cytokinesis, membrane compartmentalization, and exocytosis. However, it is unknown how septins are arranged within higher-order structures in cells. To determine the organization of septins in live cells, we developed a polarized fluorescence microscopy system to monitor the orientation of GFP dipole moments with high spatial and temporal resolution. When GFP was fused to septins, the arrangement of GFP dipoles reflected the underlying septin organization. We demonstrated in a filamentous fungus, a budding yeast, and a mammalian epithelial cell line that septin proteins were organized in an identical highly ordered fashion. Fluorescence anisotropy measurements indicated that septin filaments organized into pairs within live cells, just as has been observed in vitro. Additional support for the formation of pairs came from the observation of paired filaments at the cortex of cells using electron microscopy. Furthermore, we found that highly ordered septin structures exchanged subunits and rapidly rearranged. We conclude that septins assemble into dynamic, paired filaments in vivo and that this organization is conserved from yeast to mammals.en_US
dc.description.sponsorshipThis work was supported by the National Science Foundation under grant No. MCB-0719126 to A.S. Gladfelter, the National Institute of Biomedical Imaging and Bioengineering under grant No. EB002583 to R. Oldenbourg, a Drexel CURE grant from the State of Pennsylvania Tobacco Settlement Fund, and National Institute of Neurological Disorders and Stroke grant NS48090- 06A to E.T. Spiliotis.en_US
dc.format.mimetypeapplication/pdf
dc.language.isoen_USen_US
dc.publisherRockefeller University Pressen_US
dc.relation.hasparthttp://jcb.rupress.org/content/193/6/1065/suppl/DC1
dc.relation.urihttps://doi.org/10.1083/jcb.201012143
dc.rightsAttribution-NonCommercial-ShareAlike 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/us/*
dc.titleSeptin filaments exhibit a dynamic, paired organization that is conserved from yeast to mammalsen_US
dc.typeArticleen_US
dc.identifier.doi10.1083/jcb.201012143


Files in this item

Thumbnail
Thumbnail

This item appears in the following Collection(s)

Show simple item record

Attribution-NonCommercial-ShareAlike 3.0 United States
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-ShareAlike 3.0 United States