The Library
Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self assembly
Tools
Tools
Tools
Morris, Kyle L., Jones, Joseph Reuben, Halebian, Mary, Wu, Shenping, Baker, Michael, Armache, Jean-Paul, Avila Ibarra, Amaurys, Sessions, Richard B., Cameron, Alexander, Cheng, Yifan and Smith, Corinne J. (2019) Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self assembly. Nature Structural & Molecular Biology, 26 . pp. 890-898. doi:10.1038/s41594-019-0292-0
|
PDF
WRAP-Cryo-EM-multiple-cage-architectures-universal-clathrin-Morris-2019.pdf - Accepted Version - Requires a PDF viewer. Download (994Kb) | Preview |
|
![[img]](http://wrap.warwick.ac.uk/style/images/fileicons/application_pdf.png) |
PDF
WRAP-supporting-information-1.pdf - Supplemental Material Embargoed item. Restricted access to Repository staff only - Requires a PDF viewer. Download (506Kb) |
|
|
PDF
WRAP-Supporting-information-2.pdf - Supplemental Material Embargoed item. Restricted access to Repository staff only - Requires a PDF viewer. Download (6Mb) |
|
|
PDF
Video Legends.pdf - Supplemental Material Embargoed item. Restricted access to Repository staff only - Requires a PDF viewer. Download (5Kb) |
|
![[img]](http://wrap.warwick.ac.uk/style/images/fileicons/video.png) |
Video (QuickTime)
videoS1.mov - Supplemental Material Embargoed item. Restricted access to Repository staff only Download (185Mb) |
|
|
Video (QuickTime)
videoS2.mov - Supplemental Material Embargoed item. Restricted access to Repository staff only Download (60Mb) |
|
|
Video (QuickTime)
videoS3.mov - Supplemental Material Embargoed item. Restricted access to Repository staff only Download (130Mb) |
|
![[img]](http://wrap.warwick.ac.uk/style/images/fileicons/application_postscript.png) |
Postscript
Figure_1.eps - Supplemental Material Embargoed item. Restricted access to Repository staff only - Requires a viewer, such as GSview Download (58Mb) |
|
|
Postscript
figure_2.eps - Supplemental Material Embargoed item. Restricted access to Repository staff only - Requires a viewer, such as GSview Download (23Mb) |
|
|
Postscript
figure_3.eps - Supplemental Material Embargoed item. Restricted access to Repository staff only - Requires a viewer, such as GSview Download (17Mb) |
|
|
Postscript
Figure_4.eps - Supplemental Material Embargoed item. Restricted access to Repository staff only - Requires a viewer, such as GSview Download (64Mb) |
|
|
Postscript
figure_5.eps - Supplemental Material Embargoed item. Restricted access to Repository staff only - Requires a viewer, such as GSview Download (38Mb) |
Official URL: https://doi.org/10.1038/s41594-019-0292-0
Abstract
Clathrin forms diverse lattice and cage structures that change size and shape rapidly in response to the needs of eukaryotic cells during clathrin-mediated endocytosis and intracellular trafficking. We present the cryo-EM structure and molecular model of assembled porcine clathrin, providing insights into interactions that stabilize key elements of the clathrin lattice, namely, between adjacent heavy chains, at the light chain–heavy chain interface and within the trimerization domain. Furthermore, we report cryo-EM maps for five different clathrin cage architectures. Fitting structural models to three of these maps shows that their assembly requires only a limited range of triskelion leg conformations, yet inherent flexibility is required to maintain contacts. Analysis of the protein–protein interfaces shows remarkable conservation of contact sites despite architectural variation. These data reveal a universal mode of clathrin assembly that allows variable cage architecture and adaptation of coated vesicle size and shape during clathrin-mediated vesicular trafficking or endocytosis.
| Item Type: | Journal Article | |||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Subjects: | Q Science > QH Natural history Q Science > QP Physiology |
|||||||||||||||||||||||||||||||||
| Divisions: | Faculty of Science > Life Sciences (2010- ) | |||||||||||||||||||||||||||||||||
| Library of Congress Subject Headings (LCSH): | Cell membranes , Endocytosis , Eukaryotic cells, Carrier proteins, Protein binding, Coated vesicles | |||||||||||||||||||||||||||||||||
| Journal or Publication Title: | Nature Structural & Molecular Biology | |||||||||||||||||||||||||||||||||
| Publisher: | Nature Publishing Group | |||||||||||||||||||||||||||||||||
| ISSN: | 1545-9993 | |||||||||||||||||||||||||||||||||
| Official Date: | 3 October 2019 | |||||||||||||||||||||||||||||||||
| Dates: |
|
|||||||||||||||||||||||||||||||||
| Date of first compliant deposit: | 27 September 2019 | |||||||||||||||||||||||||||||||||
| Volume: | 26 | |||||||||||||||||||||||||||||||||
| Page Range: | pp. 890-898 | |||||||||||||||||||||||||||||||||
| DOI: | 10.1038/s41594-019-0292-0 | |||||||||||||||||||||||||||||||||
| Status: | Peer Reviewed | |||||||||||||||||||||||||||||||||
| Publication Status: | Published | |||||||||||||||||||||||||||||||||
| Access rights to Published version: | Restricted or Subscription Access | |||||||||||||||||||||||||||||||||
| RIOXX Funder/Project Grant: |
|
|||||||||||||||||||||||||||||||||
| Related URLs: |
Request changes or add full text files to a record
Repository staff actions (login required)
 |
View Item |
