Imperial College London
Alternate

Professor Molly Stevens

Faculty of Engineering, Department of Materials

Professor of Biomedical Materials and Regenerative Medicine
 
 
 
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Contact

 

+44 (0)20 7594 6804m.stevens

 
 
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Location

 

208Royal School of MinesSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Belessiotis-Richards:2022:10.1021/acs.jpcb.2c00239,
author = {Belessiotis-Richards, A and Larsen, AH and Higgins, SG and Stevens, MM and Alexander-Katz, A},
doi = {10.1021/acs.jpcb.2c00239},
journal = {The Journal of Physical Chemistry B: Biophysical Chemistry, Biomaterials, Liquids, and Soft Matter},
pages = {2789--2797},
title = {Coarse-grained simulations suggest potential competing roles of phosphoinositides and amphipathic helix structures in membrane curvature sensing of the AP180 N-terminal homology domain},
url = {http://dx.doi.org/10.1021/acs.jpcb.2c00239},
volume = {126},
year = {2022}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - The generation and sensing of membrane curvature by proteins has become of increasing interest to researchers with multiple mechanisms, from hydrophobic insertion to protein crowding, being identified. However, the role of charged lipids in the membrane curvature-sensing process is still far from understood. Many proteins involved in endocytosis bind phosphatidylinositol 4,5-bisphosphate (PIP2) lipids, allowing these proteins to accumulate at regions of local curvature. Here, using coarse-grained molecular dynamics simulations, we study the curvature-sensing behavior of the ANTH domain, a protein crucial for endocytosis. We selected three ANTH crystal structures containing either an intact, split, or truncated terminal amphipathic helix. On neutral membranes, the ANTH domain has innate curvature-sensing ability. In the presence of PIP2, however, only the domain with an intact helix senses curvature. Our work sheds light on the role of PIP2 and its modulation of membrane curvature sensing by proteins.
AU  - Belessiotis-Richards,A
AU  - Larsen,AH
AU  - Higgins,SG
AU  - Stevens,MM
AU  - Alexander-Katz,A
DO  - 10.1021/acs.jpcb.2c00239
EP  - 2797
PY  - 2022///
SN  - 1520-5207
SP  - 2789
TI  - Coarse-grained simulations suggest potential competing roles of phosphoinositides and amphipathic helix structures in membrane curvature sensing of the AP180 N-terminal homology domain
T2  - The Journal of Physical Chemistry B: Biophysical Chemistry, Biomaterials, Liquids, and Soft Matter
UR  - http://dx.doi.org/10.1021/acs.jpcb.2c00239
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000790816100002&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - https://pubs.acs.org/doi/10.1021/acs.jpcb.2c00239
UR  - http://hdl.handle.net/10044/1/97363
VL  - 126
ER  -
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