The Sec20/Tip20p complex is involved in ER retrieval of dilysine-tagged proteins.

P Cosson, S Schröder-Köhne, D S Sweet, C Démollière, S Hennecke, G Frigerio, F Letourneur

Basel Institute for Immunology, Switzerland.

European journal of cell biology 1997 Jun

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Sec20p and Tip20p were previously identified as two interacting proteins involved in early steps of the secretory pathway in Saccharomyces cerevisiae. Here we describe a novel temperature-sensitive allele of TIP20 and analyze its phenotype. While sec20 and tip20 mutants exhibited a defect in forward ER-to-Golgi transport at the non-permissive temperature, both were also defective for retrieval of various dilysine-tagged proteins from the Golgi back to the endoplasmic reticulum (ER) at lower temperature. Dilysine-dependent Golgi localization of Emp47p was also defective in both mutants. These results suggest a role for the Sec20/Tip20p complex in retrieval of dilysine-tagged proteins back to the ER.

Citation

P Cosson, S Schröder-Köhne, D S Sweet, C Démollière, S Hennecke, G Frigerio, F Letourneur. The Sec20/Tip20p complex is involved in ER retrieval of dilysine-tagged proteins. European journal of cell biology. 1997 Jun;73(2):93-7