5OO7

The ENTH domain from epsin-2 in complex with phosphatidylinositol 4,5-bisphosphate (PIP2)

5OO7 の概要

• エントリーDOI: 10.2210/pdb5oo7/pdb
• 分子名称: SLA2, GLYCEROL (3 entities in total)
• 機能のキーワード: phospholipid binding, adaptor protein complex, endocytosis
• 由来する生物種: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59444.16

構造登録者

Garcia-Alai, M.,Meijers, R. (登録日: 2017-08-06, 公開日: 2018-03-07, 最終更新日: 2024-01-17)

主引用文献

Garcia-Alai, M.M.,Heidemann, J.,Skruzny, M.,Gieras, A.,Mertens, H.D.T.,Svergun, D.I.,Kaksonen, M.,Uetrecht, C.,Meijers, R.
Epsin and Sla2 form assemblies through phospholipid interfaces.
Nat Commun, 9:328-328, 2018

PubMed Abstract: In clathrin-mediated endocytosis, adapter proteins assemble together with clathrin through interactions with specific lipids on the plasma membrane. However, the precise mechanism of adapter protein assembly at the cell membrane is still unknown. Here, we show that the membrane-proximal domains ENTH of epsin and ANTH of Sla2 form complexes through phosphatidylinositol 4,5-bisphosphate (PIP2) lipid interfaces. Native mass spectrometry reveals how ENTH and ANTH domains form assemblies by sharing PIP2 molecules. Furthermore, crystal structures of epsin Ent2 ENTH domain from S. cerevisiae in complex with PIP2 and Sla2 ANTH domain from C. thermophilum illustrate how allosteric phospholipid binding occurs. A comparison with human ENTH and ANTH domains reveal only the human ENTH domain can form a stable hexameric core in presence of PIP2, which could explain functional differences between fungal and human epsins. We propose a general phospholipid-driven multifaceted assembly mechanism tolerating different adapter protein compositions to induce endocytosis.

PubMed: 29362354
DOI: 10.1038/s41467-017-02443-x

実験手法

X-RAY DIFFRACTION (1.84 Å)