7OM8

Beta2 appendage domain of AP2 bound to terminal domains beneath the hub of the 28 triskelia mini clathrin coat complex, class 15

7OM8 の概要

• エントリーDOI: 10.2210/pdb7om8/pdb
• EMDBエントリー: 12984
• 分子名称: Clathrin heavy chain, AP-2 complex subunit beta (2 entities in total)
• 機能のキーワード: clathrin, clathrin adaptor, ap2, endocytosis
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 93500.60

構造登録者

Smith, S.M.,Smith, C.J. (登録日: 2021-05-21, 公開日: 2021-08-11, 最終更新日: 2024-07-10)

主引用文献

Smith, S.M.,Larocque, G.,Wood, K.M.,Morris, K.L.,Roseman, A.M.,Sessions, R.B.,Royle, S.J.,Smith, C.J.
Multi-modal adaptor-clathrin contacts drive coated vesicle assembly.
Embo J., 40:e108795-e108795, 2021

PubMed Abstract: Clathrin-coated pits are formed by the recognition of membrane and cargo by the AP2 complex and the subsequent recruitment of clathrin triskelia. A role for AP2 in coated-pit assembly beyond initial clathrin recruitment has not been explored. Clathrin binds the β2 subunit of AP2, and several binding sites have been identified, but our structural knowledge of these interactions is incomplete and their functional importance during endocytosis is unclear. Here, we analysed the cryo-EM structure of clathrin cages assembled in the presence of β2 hinge-appendage (β2HA). We find that the β2-appendage binds in at least two positions in the cage, demonstrating that multi-modal binding is a fundamental property of clathrin-AP2 interactions. In one position, β2-appendage cross-links two adjacent terminal domains from different triskelia. Functional analysis of β2HA-clathrin interactions reveals that endocytosis requires two clathrin interaction sites: a clathrin-box motif on the hinge and the "sandwich site" on the appendage. We propose that β2-appendage binding to more than one triskelion is a key feature of the system and likely explains why assembly is driven by AP2.

PubMed: 34487371
DOI: 10.15252/embj.2021108795

実験手法

ELECTRON MICROSCOPY (10.5 Å)