The cryo-EM structures of XKR9 define the architecture and caspase-mediated activation of a protein family that is involved in the exposure of phosphatidylserine during apoptosis leading to the engulfment of apoptotic cells by macrophages.
A spectroscopic analysis of the sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA)-phospholamban membrane complex reveals the importance of the relative transmembrane orientation for inhibition or activation of the ATPase.
An iron-sensitive gene cluster encodes proteins that co-localize with phytotransferrin endosomes and are involved in key intracellular iron transformation and trafficking processes in a model marine diatom.
Computation and experiment together demonstrate that nonspecific membrane–protein interactions could regulate transmembrane protein function and suggest that covalent linkers can be an integral component of the sensing apparatus.
Diverse KATP channel inhibitors occupy a common binding pocket and stabilize an interaction between Kir6.2 and SUR1 to allosterically control gating and promote the assembly and trafficking of nascent channels.