Inositol pentakisphosphate isomers bind PH domains with varying specificity and inhibit phosphoinositide interactions.

ABSTRACT:

Background

PH domains represent one of the most common domains in the human proteome. These domains are recognized as important mediators of protein-phosphoinositide and protein-protein interactions. Phosphoinositides are lipid components of the membrane that function as signaling molecules by targeting proteins to their sites of action. Phosphoinositide based signaling pathways govern a diverse range of important cellular processes including membrane remodeling, differentiation, proliferation and survival. Myo-Inositol phosphates are soluble signaling molecules that are structurally similar to the head groups of phosphoinositides. These molecules have been proposed to function, at least in part, by regulating PH domain-phosphoinositide interactions. Given the structural similarity

SUBMITTER: Jackson SG 

PROVIDER: S-EPMC3042905 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature