Litcius/Paper detail

Multiple lipid binding sites determine the affinity of PH domains for phosphoinositide-containing membranes

Eiji Yamamoto, Jan Domański, Fiona B. Naughton, Robert B. Best, Antreas C. Kalli, Phillip J. Stansfeld, Mark S.P. Sansom

2020Science Advances62 citationsDOIOpen Access PDF

Abstract

molecules is comparable to experimental values, suggesting that PH domain binding involves local clustering of PIP molecules within membranes. We describe a mechanism of PH binding proceeding via an encounter state to two bound states which differ in the orientation of the protein relative to the membrane, these orientations depending on the local PIP concentration. These results suggest that nanoscale clustering of PIP molecules can control the strength and orientation of PH domain interaction in a concentration-dependent manner.

Topics & Concepts

Pleckstrin homology domainMembranePhosphatidylinositolChemistryLipid bilayerBiophysicsMolecular dynamicsBiochemistryBiologySignal transductionComputational chemistryLipid Membrane Structure and BehaviorCellular transport and secretionErythrocyte Function and Pathophysiology