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Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self assembly

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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

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Official URL: https://doi.org/10.1038/s41594-019-0292-0

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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:
DateEvent
3 October 2019Published
2 August 2019Accepted
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:
Project/Grant IDRIOXX Funder NameFunder ID
BB/K003461/1 [BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/N008391/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/L018888/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
UNSPECIFIEDLeverhulme Trusthttp://dx.doi.org/10.13039/501100000275
R01GM098672 National Institutes of Healthhttp://dx.doi.org/10.13039/100000002
P50GM082250National Institutes of Healthhttp://dx.doi.org/10.13039/100000002
EP/N013573/1[EPSRC] Engineering and Physical Sciences Research Councilhttp://dx.doi.org/10.13039/501100000266
MOAC Doctoral Training [EPSRC] Engineering and Physical Sciences Research Councilhttp://dx.doi.org/10.13039/501100000266
MR/J003964/1[MRC] Medical Research Councilhttp://dx.doi.org/10.13039/501100000265
BB/J014532/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
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