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ACAP1 assembles into an unusual protein lattice for membrane deformation through multiple stages
Chun Chan1, Xiaoyun Pang2, Yan Zhang2
1Department of Materials Science and Engineering, City University of Hong Kong, Hong Kong, China.
Plos Computational Biology
|July 11, 2019
Summary
ACAP1, an unconventional BAR protein, forms an unusual lattice structure to deform cell membranes. Dynamic simulations and EM studies reveal its asymmetric membrane recruitment and assembly, expanding understanding of protein-driven membrane shaping.
Area of Science:
- Biochemistry
- Structural Biology
- Cell Biology
Background:
- Bin-Amphiphysin-Rvs (BAR) domain proteins are crucial for membrane deformation.
- ACAP1 (Arfgap with Coil-coil, Ankryin repeat, and PH domain I) exhibits an unusual lattice structure mediated by its BAR and Pleckstrin Homology (PH) domains.
Purpose of the Study:
- To computationally refine the ACAP1 lattice structure and identify key protein contacts.
- To investigate the dynamic recruitment and assembly of ACAP1 on membranes.
- To elucidate the structural basis of ACAP1-mediated membrane deformation.
Main Methods:
- Computational refinement of the ACAP1 lattice structure.
- Molecular dynamics simulations to study protein-membrane interactions.
- Electron microscopy (EM) for structural analysis of ACAP1 assembly.
Main Results:
- Identification of critical protein contacts within the ACAP1 lattice.
- Demonstration of asymmetric membrane recruitment of ACAP1 through dynamic behavior.
- Structural insights into the dynamic assembly of the ACAP1 lattice.
Conclusions:
- ACAP1's assembly into an unconventional lattice provides a new paradigm for BAR protein-mediated membrane deformation.
- The study broadens the understanding of how proteins form higher-ordered structures for membrane shaping.
- Findings highlight the dynamic nature of protein assembly in cellular processes.
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