Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 26, Issue 10, Pages 890-+Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41594-019-0292-0
Keywords
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Funding
- BBSRC [BB/K003461/1, BB/N008391/1, BB/L018888/1]
- National Institute of Health (NIH) [R01GM098672, P50GM082250]
- EPSRC [EP/N013573/1]
- EPSRC via the MOAC Doctoral Training Centre
- Medical Research Council Doctoral Training Partnership [MR/J003964/1]
- BBSRC (MIBTP) [BB/J014532/1]
- Wellcome Trust [EM13142, EM13909, 055663/Z/98/Z]
- MRC
- BBSRC
- BBSRC [BB/L018888/1, BB/K003461/1, BB/N008391/1, BB/J014532/1] Funding Source: UKRI
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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.
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