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Vol. 15, Issue 3, 1011-1023, March 2004

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The - and '-COP WD40 Domains Mediate Cargo-selective Interactions with Distinct Di-lysine Motifs

Anne Eugster ^*, Gabriella Frigerio ^*, Martin Dale, and Rainer Duden 

Department of Clinical Biochemistry, Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 2XY, United Kingdom

Submitted October 8, 2003; Revised November 19, 2003; Accepted November 24, 2003
Monitoring Editor: Benjamin Glick

Coatomer is required for the retrieval of proteins from an early Golgi compartment back to the endoplasmic reticulum. The WD40 domain of -COP is required for the recruitment of KKTN-tagged proteins into coatomer-coated vesicles. However, lack of the domain has only minor effects on growth in yeast. Here, we show that the WD40 domain of '-COP is required for the recycling of the KTKLL-tagged Golgi protein Emp47p. The protein is degraded more rapidly in cells with a point mutation in the WD40 domain of '-COP (sec27-95) or in cells lacking the domain altogether, whereas a point mutation in the Clathrin Heavy Chain Repeat (sec27-1) does not affect the turnover of Emp47p. Lack of the WD40 domain of '-COP has only minor effects on growth of yeast cells; however, absence of both WD40 domains of - and '-COP is lethal. Two hybrid studies together with our analysis of the maturation of KKTN-tagged invertase and the turnover of Emp47p in - and '-COP mutants suggest that the two WD40 domains of - and '-COP bind distinct but overlapping sets of di-lysine signals and hence both contribute to recycling of proteins with di-lysine signals.

^* These authors contributed equally to this study.

Corresponding author. E-mail address: rd217{at}cam.ac.uk.

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