Structural basis for pH-dependent retrieval of ER proteins from the Golgi by the KDEL receptor

Abstract

Crystal structure of the KDEL receptor Eukaryotic cells concentrate chaperones in the lumen of the endoplasmic reticulum (ER). These chaperones can be swept along the secretory pathway to the Golgi apparatus, from where they must be returned. For 20 years, cell biologists have known the identity of the KDEL (Lys-Asp-Glu-Leu) receptor responsible for this process, but the molecular basis for its function has remained elusive. Now, Bräuer et al. present crystal structures of the KDEL receptor, in both the apo ER state and KDEL retrieval signal–bound Golgi state. Comparisons of these two states identify the conformational switch that exposes the ER retrieval motif. The authors recapitulated the binding and release cycle of the receptor using purified components, confirming that the receptor is the minimal component required to bind KDEL ligands in the Golgi. Science , this issue p. 1103