Anomalous Dynamics of a Lipid Recognition Protein on a Membrane Surface

Eiji Yamamoto, Antreas C. Kalli, Takuma Akimoto, Kenji Yasuoka, Mark S.P. Sansom

Research output: Contribution to journalArticlepeer-review

35 Citations (Scopus)


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 PIP 3 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.

Original languageEnglish
Article number18245
JournalScientific reports
Publication statusPublished - 2015 Dec 14

ASJC Scopus subject areas

  • General


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