7RWC

AP2 bound to the APA domain of SGIP and heparin; partial signal subtraction and symmetry expansion

7RWC の概要

• エントリーDOI: 10.2210/pdb7rwc/pdb
• EMDBエントリー: 24714
• 分子名称: AP-2 complex subunit alpha-2, AP-2 complex subunit beta, AP-2 complex subunit mu, ... (5 entities in total)
• 機能のキーワード: ap2, clathrin vesicle, endocytosis, lipid-binding, adaptor, membrane, transport, muniscin, regulator
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 204990.70

構造登録者

Baker, R.W.,Hollopeter, G.,Partlow, E.A. (登録日: 2021-08-19, 公開日: 2022-03-30, 最終更新日: 2024-06-05)

主引用文献

Partlow, E.A.,Cannon, K.S.,Hollopeter, G.,Baker, R.W.
Structural basis of an endocytic checkpoint that primes the AP2 clathrin adaptor for cargo internalization.
Nat.Struct.Mol.Biol., 29:339-347, 2022

PubMed Abstract: Clathrin-mediated endocytosis (CME) is the main route of internalization from the plasma membrane. It is known that the heterotetrameric AP2 clathrin adaptor must open to simultaneously engage membrane and endocytic cargo, yet it is unclear how transmembrane cargos are captured to catalyze CME. Using cryogenic-electron microscopy, we discover a new way in which mouse AP2 can reorganize to expose membrane- and cargo-binding pockets, which is not observed in clathrin-coated structures. Instead, it is stimulated by endocytic pioneer proteins called muniscins, which do not enter vesicles. Muniscin-engaged AP2 is primed to rearrange into the vesicle-competent conformation on binding the tyrosine cargo internalization motif (YxxΦ). We propose adaptor priming as a checkpoint to ensure cargo internalization.

PubMed: 35347313
DOI: 10.1038/s41594-022-00749-z

実験手法

ELECTRON MICROSCOPY (3.8 Å)