Affiliation:
1. Department of Chemistry & Chemical Biology, The University of New Mexico, Albuquerque, New Mexico 87131, USA
Abstract
Introduction:
The proteins of the Bin/Amphiphysin/Rvs167 (BAR) domain superfamily are
believed to induce membrane curvature. PICK1 is a distinctive protein that consists of both a BAR and
a PDZ domain, and it has been associated with numerous diseases. It is known to facilitate membrane
curvature during receptor-mediated endocytosis. In addition to understanding how the BAR domain
facilitates membrane curvature, it's particularly interesting to unravel the hidden links between the
structural and mechanical properties of the PICK1 BAR domain.
Methods:
This paper employs steered molecular dynamics (SMD) to investigate the mechanical properties
associated with structural changes in the PICK1 BAR domains.
Results:
Our findings suggest that not only do helix kinks assist in generating curvature of BAR domains,
but they may also provide the additional flexibility required to initiate the binding between
BAR domains and the membrane
Conclusion:
We have observed a complex interaction network within the BAR monomer and at the
binding interface of the two BAR monomers. This network is crucial for maintaining the mechanical
properties of the BAR dimer. Owing to this interaction network, the PICK1 BAR dimer exhibits different
responses to external forces applied in opposite directions.
Funder
National Science Foundation
Publisher
Bentham Science Publishers Ltd.
Subject
Cell Biology,Molecular Biology,Biochemistry,General Medicine