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  Architecture of the AP2/clathrin coat on the membranes of clathrin-coated vesicles

Kovtun, O., Dickson, V. K., Kelly, B. T., Owen, D. J., & Briggs, J. A. G. (2020). Architecture of the AP2/clathrin coat on the membranes of clathrin-coated vesicles. Science Advances, 6(30): e1008277. doi:10.1126/sciadv.aba8381.

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Kovtun, O., Author
Dickson, V. K., Author
Kelly, B. T., Author
Owen, D. J., Author
Briggs, John A. G.1, 2, Author              
Affiliations:
1MRC Laboratory of Molecular Biology, External Organizations, ou_3346673              
2European Molecular Biology Laboratory, External Organizations, Heidelberg, DE, ou_3346677              

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Free keywords: n-terminal domain cryo-em auxilin model visualization resolution mechanism reveals binding sites Science & Technology - Other Topics
 Abstract: Clathrin-mediated endocytosis (CME) is crucial for modulating the protein composition of a cell's plasma membrane. Clathrin forms a cage-like, polyhedral outer scaffold around a vesicle, to which cargo-selecting clathrin adaptors are attached. Adaptor protein complex (AP2) is the key adaptor in CME. Crystallography has shown AP2 to adopt a range of conformations. Here, we used cryo-electron microscopy, tomography, and subtomogram averaging to determine structures, interactions, and arrangements of clathrin and AP2 at the key steps of coat assembly, from AP2 in solution to membrane-assembled clathrin-coated vesicles (CCVs). AP2 binds cargo and Ptdlns(4,5)P-2 (phosphatidylinositol 4,5-bisphosphate)-containing membranes via multiple interfaces, undergoing conformational rearrangement from its cytosolic state. The binding mode of AP2 beta(2) appendage into the clathrin lattice in CCVs and buds implies how the adaptor structurally modulates coat curvature and coat disassembly.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: WOS:000552228100029
DOI: 10.1126/sciadv.aba8381
ISSN: 2375-2548
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Title: Science Advances
  Alternative Title : Sci. Adv.
Source Genre: Journal
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Pages: - Volume / Issue: 6 (30) Sequence Number: e1008277 Start / End Page: - Identifier: -