Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Cell - 30 Dec 1994

Letourneur F, Gaynor E C, Hennecke S, Démollière C, Duden R, Emr S D, Riezman H, Cosson P

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Fungal Proteins
Share to Membrane Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Recombinant Fusion Proteins

Share to Saccharomyces cerevisiae

Share to Transcription Factors

Source

Identifiers

PMID: 8001155
DOI: 10.1016/0092-8674(94)90011-6

Provenance

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

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum.PMID 8001155Read ↗

Delta- and zeta-COP, two coatomer subunits homologous to clathrin-associated proteins, are involved in ER retrieval.Semantic proximity Read ↗

Alpha-COP can discriminate between distinct, functional di-lysine signals in vitro and regulates access into retrograde transport.Semantic proximity Read ↗

epsilon-COP is a structural component of coatomer that functions to stabilize alpha-COP.Semantic proximity Read ↗

Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane.Semantic proximity Read ↗

Yeast beta- and beta'-coat proteins (COP). Two coatomer subunits essential for endoplasmic reticulum-to-Golgi protein traffic.Semantic proximity Read ↗

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

Suppression of coatomer mutants by a new protein family with COPI and COPII binding motifs in Saccharomyces cerevisiae.Semantic proximity Read ↗

Sec12p requires Rer1p for sorting to coatomer (COPI)-coated vesicles and retrieval to the ER.Semantic proximity Read ↗

The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast.Semantic proximity Read ↗

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

COPI-independent anterograde transport: cargo-selective ER to Golgi protein transport in yeast COPI mutants.Semantic proximity Read ↗

The alpha- and beta'-COP WD40 domains mediate cargo-selective interactions with distinct di-lysine motifs.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.