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Epsin and Sla2 form assemblies through phospholipid interfaces.

Maria M Garcia-Alai1, Johannes Heidemann2, Michal Skruzny3

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Nature Communications
|January 25, 2018
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Summary
This summary is machine-generated.

Adapter proteins like epsin and Sla2 assemble via phosphatidylinositol 4,5-bisphosphate (PIP2) lipids. This phospholipid-driven mechanism explains how cells initiate endocytosis, with variations between species.

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Area of Science:

  • Cell Biology
  • Molecular Mechanisms of Endocytosis
  • Protein-Lipid Interactions

Background:

  • Clathrin-mediated endocytosis requires adapter protein assembly at the plasma membrane.
  • The precise mechanism of adapter protein assembly, particularly lipid interactions, remains unclear.
  • Understanding these interactions is crucial for deciphering endocytic pathway regulation.

Purpose of the Study:

  • To elucidate the mechanism of adapter protein assembly at the cell membrane.
  • To investigate the role of specific lipids, like phosphatidylinositol 4,5-bisphosphate (PIP2), in this process.
  • To compare the assembly mechanisms of fungal and human adapter protein domains.

Main Methods:

  • Utilized native mass spectrometry to analyze protein-lipid complex formation.
  • Determined crystal structures of epsin ENTH and Sla2 ANTH domains in complex with PIP2.
  • Compared structural and assembly properties of yeast and human ENTH/ANTH domains.

Main Results:

  • Demonstrated that ENTH (of epsin) and ANTH (of Sla2) domains form complexes via PIP2 lipid interfaces.
  • Revealed that PIP2 molecules are shared within these assemblies, elucidated by mass spectrometry.
  • Structural analysis showed allosteric phospholipid binding; human ENTH domains form stable hexamers with PIP2, unlike fungal counterparts.

Conclusions:

  • Proposed a general, phospholipid-driven assembly mechanism for adapter proteins in endocytosis.
  • This mechanism accommodates diverse adapter protein compositions, facilitating endocytic vesicle formation.
  • Identified species-specific differences in ENTH domain assembly, potentially explaining functional variations.