Coordination of bilayer properties by an inward-rectifier K⁺ channel is a cooperative process driven by protein-lipid interaction.

ABSTRACT: Physical properties of biological membranes directly or indirectly govern biological processes. Yet, the interplay between membrane and integral membrane proteins is difficult to assess due to reciprocal effects between membrane proteins, individual lipids, and membrane architecture. Using solid-state NMR (SSNMR) we previously showed that KirBac1.1, a bacterial Inward-Rectifier K⁺ channel, nucleates bilayer ordering and microdomain formation through tethering anionic lipids. Conversely, these lipids cooperatively bind cationic residues to activate the channel and initiate K⁺ flux. The mechanistic details governing the relationship between cooperative lipid loading and bilayer ordering are, however, unknown. To investigate, we generated KirBac1.1 samples with different

SUBMITTER: van Aalst EJ 

PROVIDER: S-EPMC11176924 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature