New insights into P2X7 receptor regulation: Ca²⁺-calmodulin and GDP bind to the soluble P2X7 ballast domain.

ABSTRACT: P2X7 receptors are nonselective cation channels that are activated by extracellular ATP and play important roles in inflammation. They differ from other P2X family members by a large intracellular C-terminus that mediates diverse signaling processes that are little understood. A recent cryo-EM study revealed that the C-terminus of the P2X7 receptor forms a unique cytoplasmic ballast domain that possesses a GDP-binding site as well as a dinuclear Zn²⁺ site. However, the molecular basis for the regulatory function of the ballast domain as well as the interplay between the various ligands remain unclear. Here, we successfully expressed a soluble trimeric P2X7 ballast domain (P2X7BD) and characterized its ligand binding properties using a biophysical approach. We identified calmodul

SUBMITTER: Sander S 

PROVIDER: S-EPMC9574498 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature