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Anomalous dynamics of a lipid recognition protein on a membrane surface

Abstract:
Pleckstrin homology (PH) domains are lipid-binding modules present in peripheral membrane proteins which interact with phosphatidyl-inositol phosphates (PIPs) in cell membranes. We use multiscale molecular dynamics simulations to characterize the localization and anomalous dynamics of the DAPP1 PH domain on the surface of a PIP-containing lipid bilayer. Both translational and rotational diffusion of the PH domain on the lipid membrane surface exhibit transient subdiffusion, with an exponent α ≈ 0.5 for times of less than 10 ns. In addition to a PIP3 molecule at the canonical binding site of the PH domain, we observe additional PIP molecules in contact with the protein. Fluctuations in the number of PIPs associated with the PH domain exhibit 1/f noise. We suggest that the anomalous diffusion and long-term correlated interaction of the PH domain with the membrane may contribute to an enhanced probability of encounter with target complexes on cell membrane surfaces.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/srep18245

Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author


Publisher:
Nature Publishing Group
Journal:
Scientific Reports More from this journal
Volume:
5
Article number:
18245
Publication date:
2015-01-01
DOI:
ISSN:
2045-2322


Pubs id:
pubs:573488
UUID:
uuid:b2895dfd-1968-47ff-b6c3-a3eeeb3b5edc
Local pid:
pubs:573488
Source identifiers:
573488
Deposit date:
2015-11-16

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