Phosphoinositide Control of Membrane Protein Function: A Frontier Led by Studies on Ion Channels
Document Type
Article
Publication Date
2-2015
Abstract
Anionic phospholipids are critical constituents of the inner leaflet of the plasma membrane, ensuring appropriate membrane topology of transmembrane proteins. Additionally, in eukaryotes, the negatively charged phosphoinositides serve as key signals not only through their hydrolysis products but also through direct control of transmembrane protein function. Direct phosphoinositide control of the activity of ion channels and transporters has been the most convincing case of the critical importance of phospholipid-protein interactions in the functional control of membrane proteins. Furthermore, second messengers, such as [Ca2+]i, or posttranslational modifications, such as phosphorylation, can directly or allosterically fine-tune phospholipid-protein interactions and modulate activity. Recent advances in structure determination of membrane proteins have allowed investigators to obtain complexes of ion channels with phosphoinositides and to use computational and experimental approaches to probe the dynamic mechanisms by which lipid-protein interactions control active and inactive protein states.
Recommended Citation
Logothetis DE, Petrou VI, Zhang M, Mahajan R, Meng XY, Adney SK, Cui M, Baki L. Phosphoinositide control of membrane protein function: a frontier led by studies on ion channels. Annual Review of Physiology. 2015 Feb; 77: 81-104.
DOI: 10.1146/annurev-physiol-021113-170358
Copyright
Annual Reviews
Comments
This article was originally published in Annual Review of Physiology, volume 77, in 2015. DOI: 10.1146/annurev-physiol-021113-170358