Epsin and Sla2 form assemblies through phospholipid interfaces

Maria M. Garcia-Alai, Johannes Heidemann, Michal Skruzny, Anna Gieras, Haydyn D. T. Mertens, Dmitri I. Svergun, Marko Kaksonen, Charlotte Uetrecht () and Rob Meijers ()
Additional contact information
Maria M. Garcia-Alai: European Molecular Biology Laboratory (EMBL), Hamburg Outstation
Johannes Heidemann: Leibniz Institute for Experimental Virology
Michal Skruzny: Max Planck Institute for Terrestrial Microbiology
Anna Gieras: European Molecular Biology Laboratory (EMBL), Hamburg Outstation
Haydyn D. T. Mertens: European Molecular Biology Laboratory (EMBL), Hamburg Outstation
Dmitri I. Svergun: European Molecular Biology Laboratory (EMBL), Hamburg Outstation
Marko Kaksonen: University of Geneva
Charlotte Uetrecht: Leibniz Institute for Experimental Virology
Rob Meijers: European Molecular Biology Laboratory (EMBL), Hamburg Outstation

Nature Communications, 2018, vol. 9, issue 1, 1-13

Abstract: 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.

Date: 2018
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41467-017-02443-x Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-017-02443-x

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-017-02443-x

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().