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Article

Coatomer interaction with di-lysine endoplasmic reticulum retention motifs.

Science (New York, N.Y.) - 18 Mar 1994

Cosson P, Letourneur F

Abstract excerpt

Although signals for retention in the endoplasmic reticulum (ER) have been identified in the cytoplasmic domain of various ER-resident type I transmembrane proteins, the mechanisms responsible for ER retention are still unknown. Yeast and mammalian ER retention motifs interacted specifically in cell lysates with the coatomer, a polypeptide complex implicated in membrane traffic. Mutations that affect the ER...

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Identifiers

PMID: 8128252
DOI: 10.1126/science.8128252

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Coatomer interaction with di-lysine endoplasmic reticulum retention motifs.PMID 8128252Read ↗

Targeting to the endoplasmic reticulum by dilysine motifs: role of coat proteins.Semantic proximity Read ↗

Coatopathies: Genetic Disorders of Protein CoatsSemantic proximity Read ↗

Assembly, organization, and function of the COPII coatSemantic proximity Read ↗

An intramembrane chaperone complex facilitates membrane protein biogenesis.Semantic proximity Read ↗

Novel cargo-binding site in the beta and delta subunits of coatomer.Semantic proximity Read ↗

Consequences of mutations in the genes of the ER export machinery COPII in vertebrates.Semantic proximity Read ↗

Identification and characterization of an endoplasmic reticulum localization motif.Semantic proximity Read ↗

Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum.Semantic proximity Read ↗

Rer1p, a retrieval receptor for endoplasmic reticulum membrane proteins, is dynamically localized to the Golgi apparatus by coatomer.Semantic proximity Read ↗

Polycystins as components of large multiprotein complexes of polycystin interactorsSemantic proximity Read ↗

Binding of coatomer by the PEX11 C-terminus is not required for function.Semantic proximity Read ↗

Endoplasmic reticulum protein targeting of phospholamban: a common role for an N-terminal di-arginine motif in ER retention?Semantic proximity Read ↗

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