Structural insights into gap junction channels boosted by cryo-EM

Abstract

Regulating intercellular communication is essential for multicellular organisms. Gap junction channels are the major components mediating this function, but the molecular mechanisms underlying their opening and closing remain unclear. Single-particle cryo-electron microscopy (cryo-EM) is a powerful tool for investigating high-resolution protein structures that are difficult to crystallize, such as gap junction channels. Membrane protein structures are often determined in a detergent solubilized form, but lipid bilayers provide a near native environment for structural analysis. This review focuses on recent reports of gap junction channel structures visualized by cryo-EM. An overview of the differences observed in gap junction channel structures in the presence and absence of lipids is described, which may contribute to elucidating the regulation mechanisms of gap junction channel function.