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Article

Retention of a co-translational translocated mutant protein of carboxypeptidase Y of Saccharomyces cerevisiae in endoplasmic reticulum.

FEMS microbiology letters - 1 Aug 1993

Ramezani Rad M, Katz H

Abstract excerpt

Co-translational translocation of Saccharomyces cerevisiae vacuolar glycoprotein carboxypeptidase Y (CpY) was highly efficient when studied with an in vivo and in vitro homologous system, comparison of limited proteolytic cleavage of immunoprecipitated translational products of CpY and subcellular localisation of a mutant CpY. The efficient segregation of CpY mRNA in highly purified fractions of rough microsomes...

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

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Identifiers

PMID: 8405926
DOI: 10.1111/j.1574-6968.1993.tb06380.x

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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

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Retention of a co-translational translocated mutant protein of carboxypeptidase Y of Saccharomyces cerevisiae in endoplasmic reticulum.PMID 8405926Read ↗

Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species.Semantic proximity Read ↗

Vacuolar carboxypeptidase Y of Saccharomyces cerevisiae is glycosylated, sorted and matured in the fission yeast Schizosaccharomyces pombe.Semantic proximity Read ↗

Use of CPY and its derivatives to study protein quality control in various cell compartments.Semantic proximity Read ↗

Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast.Semantic proximity Read ↗

Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids.Semantic proximity Read ↗

Multiple endoplasmic reticulum-associated pathways degrade mutant yeast carboxypeptidase Y in mammalian cells.Semantic proximity Read ↗

N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast.Semantic proximity Read ↗

Yeast carboxypeptidase Y requires glycosylation for efficient intracellular transport, but not for vacuolar sorting, in vivo stability, or activity.Semantic proximity Read ↗

Requirement of the propeptide for in vivo formation of active yeast carboxypeptidase Y.Semantic proximity Read ↗

Yeast vacuolar proenzymes are sorted in the late Golgi complex and transported to the vacuole via a prevacuolar endosome-like compartment.Semantic proximity Read ↗

Protein processing:Semantic proximity Read ↗

In vitro reconstitution of intercompartmental protein transport to the yeast vacuole.Semantic proximity Read ↗

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