Structural highlights
Function
[ERD22_CHICK] Required for the retention of luminal endoplasmic reticulum proteins. Determines the specificity of the luminal ER protein retention system. Also required for normal vesicular traffic through the Golgi. This receptor recognizes K-D-E-L (By similarity).
Publication Abstract from PubMed
Selective export and retrieval of proteins between the endoplasmic reticulum (ER) and Golgi apparatus is indispensable for eukaryotic cell function. An essential step in the retrieval of ER luminal proteins from the Golgi is the pH-dependent recognition of a carboxyl-terminal Lys-Asp-Glu-Leu (KDEL) signal by the KDEL receptor. Here, we present crystal structures of the chicken KDEL receptor in the apo ER state, KDEL-bound Golgi state, and in complex with an antagonistic synthetic nanobody (sybody). These structures show a transporter-like architecture that undergoes conformational changes upon KDEL binding and reveal a pH-dependent interaction network crucial for recognition of the carboxyl terminus of the KDEL signal. Complementary in vitro binding and in vivo cell localization data explain how these features create a pH-dependent retrieval system in the secretory pathway.
Structural basis for pH-dependent retrieval of ER proteins from the Golgi by the KDEL receptor.,Brauer P, Parker JL, Gerondopoulos A, Zimmermann I, Seeger MA, Barr FA, Newstead S Science. 2019 Mar 8;363(6431):1103-1107. doi: 10.1126/science.aaw2859. PMID:30846601[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Brauer P, Parker JL, Gerondopoulos A, Zimmermann I, Seeger MA, Barr FA, Newstead S. Structural basis for pH-dependent retrieval of ER proteins from the Golgi by the KDEL receptor. Science. 2019 Mar 8;363(6431):1103-1107. doi: 10.1126/science.aaw2859. PMID:30846601 doi:http://dx.doi.org/10.1126/science.aaw2859
