6YAF

AP2 on a membrane containing tyrosine-based cargo peptide

Summary for 6YAF

• Entry DOI: 10.2210/pdb6yaf/pdb
• Related: 6YAE 6YAH 6YAI
• EMDB information: 10747 10748 10749 10750 10751 10752 10753 10754
• Descriptor: AP-2 complex subunit alpha-2, AP-2 complex subunit beta, AP-2 complex subunit mu, ... (5 entities in total)
• Functional Keywords: clathrin, clathrin adaptor, ap2, clathrin assembly, endocytosis
• Biological source: Rattus norvegicus (Norway rat); More
• Total number of polymer chains: 5
• Total formula weight: 245952.46

Authors

Kovtun, O.,Kane Dickson, V.,Kelly, B.T.,Owen, D.,Briggs, J.A.G. (deposition date: 2020-03-12, release date: 2020-07-29, Last modification date: 2024-05-22)

Primary citation

Kovtun, O.,Dickson, V.K.,Kelly, B.T.,Owen, D.J.,Briggs, J.A.G.
Architecture of the AP2/clathrin coat on the membranes of clathrin-coated vesicles.
Sci Adv, 6:eaba8381-eaba8381, 2020

PubMed 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 PtdIns(4,5) (phosphatidylinositol 4,5-bisphosphate)-containing membranes via multiple interfaces, undergoing conformational rearrangement from its cytosolic state. The binding mode of AP2 β2 appendage into the clathrin lattice in CCVs and buds implies how the adaptor structurally modulates coat curvature and coat disassembly.

PubMed: 32743075
DOI: 10.1126/sciadv.aba8381

Experimental method

ELECTRON MICROSCOPY (9.1 Å)