The α- and β′-COP WD40 Domains Mediate Cargo-selective Interactions with Distinct Di-lysine Motifs

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

*Corresponding author for this work
62 Citations (Scopus)

Abstract

Coatomer is required for the retrieval of proteins from an early Golgi compartment back to the endoplasmic reticulum. The WD40 domain of α-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 β′-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 β′-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 β′-COP has only minor effects on growth of yeast cells; however, absence of both WD40 domains of α- and β′-COP is lethal. Two hybrid studies together with our analysis of the maturation of KKTN-tagged invertase and the turnover of Emp47p in α- and β′-COP mutants suggest that the two WD40 domains of α- and β′-COP bind distinct but overlapping sets of di-lysine signals and hence both contribute to recycling of proteins with di-lysine signals.

Original languageEnglish
JournalMolecular Biology of the Cell
Volume15
Issue number3
Pages (from-to)1011-1023
Number of pages13
ISSN1059-1524
DOIs
Publication statusPublished - 01.03.2004

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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