A molecular specificity code for the three mammalian KDEL receptors

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Abstract

A C-terminal KDEL-like motif prevents secretion of soluble endoplasmic reticulum (ER)-resident proteins. This motif interacts with KDEL receptors localized in the intermediate compartment and Golgi apparatus. Such binding triggers retrieval back to the ER via a coat protein I-dependent pathway. To date, two human KDEL receptors have been reported. Here, we report the Golgi localization of a third human KDEL receptor. Using a reporter construct system from a screen of 152 variants, we identified 35 KDEL-like variants that result in efficient ER localization but do not match the current Prosite motif for ER localization ([KRHQSA]-[DENQ]-E-L). We cloned 16 human proteins with one of these motifs and all were found in the ER. A subsequent screen by bimolecular fluorescence complementation determined the specificities of the three human KDEL receptors. Each KDEL receptor has a unique pattern of motifs with which it interacts. This suggests a specificity in the retrieval of human proteins that contain different KDEL variants. © The Rockefeller University Press.

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APA

Raykhel, I., Alanen, H., Salo, K., Jurvansuu, J., Van, D. N., Latva-Ranta, M., & Ruddock, L. (2007). A molecular specificity code for the three mammalian KDEL receptors. Journal of Cell Biology, 179(6), 1193–1204. https://doi.org/10.1083/jcb.200705180

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