Membrane protein retrieval from the Golgi apparatus to the endoplasmic reticulum (ER): characterization of the RER1 gene product as a component involved in ER localization of Sec12p.

doi:10.1091/mbc.6.11.1459

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Article

Membrane protein retrieval from the Golgi apparatus to the endoplasmic reticulum (ER): characterization of the RER1 gene product as a component involved in ER localization of Sec12p.

Molecular biology of the cell - 1 Nov 1995

Sato K, Nishikawa S, Nakano A

Abstract excerpt

Yeast Sec12p, a type II transmembrane glycoprotein, is required for formation of transport vesicles from the endoplasmic reticulum (ER). Biochemical and morphological analyses have suggested that Sec12p is localized to the ER by two mechanisms: static retention in the ER and dynamic retrieval from the early region of the Golgi apparatus. The rer1 mutant we isolated in a previous study mislocalizes the authentic...

Topics

Amino Acid Sequence
Base Sequence
Endoplasmic Reticulum
Fluorescent Antibody Technique
Fungal Proteins
Genes, Fungal
Genotype
Golgi Apparatus
Guanine Nucleotide Exchange Factors
Membrane Glycoproteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Membrane Proteins

Molecular Sequence Data

Mutagenesis, Site-Directed

Oligodeoxyribonucleotides

Restriction Mapping

Saccharomyces cerevisiae

Saccharomyces cerevisiae Proteins

Vesicular Transport Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 8589449
DOI: 10.1091/mbc.6.11.1459
PMCID: PMC301304

Genes

RER1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8589449-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Membrane protein retrieval from the Golgi apparatus to the endoplasmic reticulum (ER): characterization of the RER1 gene product as a component involved in ER localization of Sec12p.PMID 8589449Read ↗

Endoplasmic reticulum localization of Sec12p is achieved by two mechanisms: Rer1p-dependent retrieval that requires the transmembrane domain and Rer1p-independent retention that involves the cytoplasmic domain.Semantic proximity Read ↗

Rer1p, a retrieval receptor for ER membrane proteins, recognizes transmembrane domains in multiple modes.Semantic proximity Read ↗

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

Structural and functional dissection of a membrane glycoprotein required for vesicle budding from the endoplasmic reticulum.Semantic proximity Read ↗

Active and specific recruitment of a soluble cargo protein for endoplasmic reticulum exit in the absence of functional COPII component Sec24p.Semantic proximity Read ↗

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

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Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway in Saccharomyces cerevisiae.Semantic proximity Read ↗

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