Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum

François Letourneur*, Erin C. Gaynor, Silke Hennecke, Corinne Démollière, Rainer Duden, Scott D. Emr, Howard Riezman, Pierre Cosson

*Corresponding author for this work
637 Citations (Scopus)


Dilysine motifs in cytoplasmic domains of transmembrane proteins are signals for their continuous retrieval from the Golgi back to the endoplasmic reticulum (ER). We describe a system to assess retrieval to the ER in yeast cells making use of a dilysine-tagged Ste2 protein. Whereas retrieval was unaffected in most sec mutants tested (sec7, sec12, sec13, sec16, sec17, sec18, sec19, sec22, and sec23), a defect in retrieval was observed in previously characterized coatomer mutants (sec21-1, sec27-1), as well as in newly isolated retrieval mutants (sec21-2, ret1-1). RET1 was cloned by complementation and found to encode the α subunit of coatomer. While temperature-sensitive for growth, the newly isolated coatomer mutants exhibited a very modest defect in secretion at the nonpermissive temperature. Coatomer from β'-COP (sec27-1) and α-COP (ret1-1) mutants, but not from γ-COP (sec21) mutants, had lost the ability to bind dilysine motifs in vitro. Together, these results suggest that coatomer plays an essential role in retrograde Golgi-to-ER transport and retrieval of dilysine-tagged proteins back to the ER.

Original languageEnglish
Issue number7
Pages (from-to)1199-1207
Number of pages9
Publication statusPublished - 30.12.1994

Research Areas and Centers

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


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