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A correction to this article has been published: Raykhel et al., J. Cell Biol. 180 (3) 645
Published online
doi:10.1083/jcb.200705180
The Journal of Cell Biology, Vol. 179, No. 6, 1193-1204
The Rockefeller University Press, 0021-9525 $30.00
© Raykhel et al.
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Article

A molecular specificity code for the three mammalian KDEL receptors



Irina Raykhel, Heli Alanen, Kirsi Salo, Jaana Jurvansuu, Van Dat Nguyen, Maria Latva-Ranta, and Lloyd Ruddock

Department of Biochemistry, Biocenter Oulu, University of Oulu, 90570 Oulu, Finland

Correspondence to Lloyd Ruddock: Lloyd.ruddock{at}oulu.fi

AC-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.

Abbreviations used in this paper: BiFC, bimolecular fluorescence complementation; COP, coat protein; CRT, calreticulin; ERD, ER retention-defective complementation group; PDI, protein disulphide isomerase.


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