Allostery in membrane proteins

Abstract

Membrane proteins are an integral part of signal transduction. To signal, membrane proteins must interact with a variety of lipid species, effectors, and other proteins in the biological membrane leading to an immense number of possible interactions. Despite this inherent complexity, accurate control of signaling must take place. By allowing proteins to adopt a multiplicity of conformations in a process known as allostery, nature is able to transmit a signal from one protein site to another distal, functional site, allowing for modulation of protein properties and regulation of activity. In recent years, an increasing number of reports have pointed to common mechanisms governing the allosteric modulation of membrane proteins, including conformational selection, oligomerization, and the modulation of allosteric sites. In this report, we summarize recent advances in membrane protein allostery.