Phosphatidylinositol 4,5-biphosphate (PIP(2)) lipids regulate the phosphorylation of syntaxin N-terminus by modulating both its position and local structure.

ABSTRACT: Syntaxin (STX) is a N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) protein that binds to the plasma membrane and regulates ion channels and neurotransmitter transporters. Experiments have established the involvement of the N-terminal segment of STX in direct protein-protein interactions and have suggested a critical role for the phosphorylation of serine 14 (S14) by casein kinase-2 (CK2). Because the organization of STX in the plasma membrane was shown to be regulated by phosphatidylinositol 4,5-biphosphate (PIP(2)) lipids, we investigated the mechanistic involvement of PIP(2) lipids in modulating both the membrane interaction and the phosphorylation of STX, using a computational strategy that integrates mesoscale continuum modeling of protein-membrane interactions,

SUBMITTER: Khelashvili G 

PROVIDER: S-EPMC3462474 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature