CaltechAUTHORS
  A Caltech Library Service

Electron cryotomography of ESCRT assemblies and dividing Sulfolobus cells suggests that spiraling filaments are involved in membrane scission

Dobro, Megan J. and Samson, Rachel Y. and Yu, Zhiheng and McCullough, John and Ding, H. Jane and Chong, Parkson Lee-Gau and Bell, Stephen D. and Jensen, Grant J. (2013) Electron cryotomography of ESCRT assemblies and dividing Sulfolobus cells suggests that spiraling filaments are involved in membrane scission. Molecular Biology of the Cell, 24 (15). pp. 2319-2327. ISSN 1059-1524. PMCID PMC3727925. https://resolver.caltech.edu/CaltechAUTHORS:20130917-104519857

[img]
Preview
PDF - Published Version
Creative Commons Attribution Share Alike.

1860Kb
[img]
Preview
PDF (Supplemental Materials ) - Supplemental Material
Creative Commons Attribution Non-commercial Share Alike.

1100Kb
[img] Video (QuickTime) (Movie 1) - Supplemental Material
Creative Commons Attribution Non-commercial Share Alike.

1491Kb
[img] Video (WMV) (Movie 2) - Supplemental Material
Creative Commons Attribution Non-commercial Share Alike.

10Mb
[img] Video (QuickTime) (Movie 3) - Supplemental Material
Creative Commons Attribution Non-commercial Share Alike.

18Mb
[img] Video (QuickTime) (Movie 4) - Supplemental Material
Creative Commons Attribution Non-commercial Share Alike.

3765Kb
[img] Video (QuickTime) (Movie 5) - Supplemental Material
Creative Commons Attribution Non-commercial Share Alike.

3730Kb

Use this Persistent URL to link to this item: https://resolver.caltech.edu/CaltechAUTHORS:20130917-104519857

Abstract

The endosomal-sorting complex required for transport (ESCRT) is evolutionarily conserved from Archaea to eukaryotes. The complex drives membrane scission events in a range of processes, including cytokinesis in Metazoa and some Archaea. CdvA is the protein in Archaea that recruits ESCRT-III to the membrane. Using electron cryotomography (ECT), we find that CdvA polymerizes into helical filaments wrapped around liposomes. ESCRT-III proteins are responsible for the cinching of membranes and have been shown to assemble into helical tubes in vitro, but here we show that they also can form nested tubes and nested cones, which reveal surprisingly numerous and versatile contacts. To observe the ESCRT–CdvA complex in a physiological context, we used ECT to image the archaeon Sulfolobus acidocaldarius and observed a distinct protein belt at the leading edge of constriction furrows in dividing cells. The known dimensions of ESCRT-III proteins constrain their possible orientations within each of these structures and point to the involvement of spiraling filaments in membrane scission.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1091/mbc.E12-11-0785 DOIArticle
http://www.molbiolcell.org/content/24/15/2319PublisherArticle
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3727925/PubMed CentralArticle
ORCID:
AuthorORCID
Dobro, Megan J.0000-0002-6464-3932
Jensen, Grant J.0000-0003-1556-4864
Additional Information:© 2013 Dobro et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). Received: Nov 6, 2012; Revised: May 28, 2013; Accepted: May 31, 2013. This article was published online ahead of print in MBoC in Press (http://www .molbiolcell.org/cgi/doi/10.1091/mbc.E12-11-0785) on June 12, 2013. This work was supported in part by National Institutes of Heath Grant P50 GM082545 to G.J.J., National Science Foundation Grant DMR1105277 to P.L.C., and a gift to Caltech from the Gordon and Betty Moore Foundation. We thank Wesley I. Sundquist for advice and critical reading of the manuscript, Kay Grunewald for use of laboratory equipment, and Morgan Beeby, Jason Porath, and Jean Choi for their help with illustrations.
Funders:
Funding AgencyGrant Number
NIHP50 GM082545
NSFDMR1105277
Gordon and Betty Moore FoundationUNSPECIFIED
Issue or Number:15
PubMed Central ID:PMC3727925
Record Number:CaltechAUTHORS:20130917-104519857
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20130917-104519857
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:41364
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:17 Sep 2013 19:47
Last Modified:03 Oct 2019 05:48

Repository Staff Only: item control page