Epsin and Sla2 Form Assemblies Through Phospholipid Interfaces

Overview

Journal Nat Commun

Specialty Biology

Date 2018 Jan 25

PMID 29362354

Citations 29

Authors

Maria M Garcia-Alai

Johannes Heidemann

Michal Skruzny

Anna Gieras

Haydyn D T Mertens

Dmitri I Svergun

Marko Kaksonen

Charlotte Uetrecht

Rob Meijers

Affiliations

Soon will be listed here.

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.

Citing Articles

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