Abstract
Phosphoinositide (PI)‐binding domains recruit a variety of signaling and trafficking proteins to the distinct intracellular membranes. In the plasma membrane, PtdIns(4,5)P2 and PtdIns(3,4,5)P3 lipids are recognized by the PH (pleckstrin homology) and ENTH (Epsin N‐terminal homology) domains. Here, the molecular basis of membrane anchoring and penetration by the PH domain of general receptor for phosphoinositides isoform 1 (GRP1) and Epsin ENTH domain is detailed. The specificities and binding affinities for PI‐containing SUVs and soluble metabolically‐stabilized analogues of PIs, insertion into monolayers and bilayers, and regulation of the lipid binding and membrane penetration by pH are investigated using nuclear magnetic resonance spectroscopy, surface plasmon resonance, liposome‐binding and surface tension experiments. The significance of the pH sensitivity and the effect of the acidic and basic media on the PI recognition, hydrophobic insertion and non‐specific electrostatic contacts is established.
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