Microplate-based characterization of protein-phosphoinositide binding interactions using a synthetic biotinylated headgroup analogue.

ABSTRACT: Membrane lipids act as important regulators of a litany of important physiological and pathophysiological events. Many of them act as site-specific ligands for cytosolic proteins in binding events that recruit receptors to the cell surface and control both protein function and subcellular localization. Phosphatidylinositol phosphates (PIP(n)s) are a family of signaling lipids that regulate numerous cellular processes by interacting with a myriad of protein binding modules. Characterization of PIP(n)-binding proteins has been hampered by the lack of a rapid and convenient quantitative assay. Herein, microplate-based detection is presented as an effective approach to characterizing protein-PIP(n) binding interactions at the molecular level. With this assay, the binding of proteins to isolate

SUBMITTER: Gong D 

PROVIDER: S-EPMC2656446 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature