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Publication Abstract from PubMed

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.

Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly.,Morris KL, Jones JR, Halebian M, Wu S, Baker M, Armache JP, Avila Ibarra A, Sessions RB, Cameron AD, Cheng Y, Smith CJ Nat Struct Mol Biol. 2019 Oct;26(10):890-898. doi: 10.1038/s41594-019-0292-0., Epub 2019 Oct 3. PMID:31582853^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.