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Article

A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae.

The EMBO journal - 1 Apr 1996

Finke K, Plath K, Panzner S, Prehn S, Rapoport T A, Hartmann E, Sommer T

Abstract excerpt

Yeast microsomes contain a heptameric Sec complex involved in post-translational protein transport that is composed of a heterotrimeric Sec61p complex and a tetrameric Sec62-Sec63 complex. The trimeric Sec61p complex also exists as a separate entity that probably functions in co-translational protein transport, like its homolog in mammals. We have now discovered in the yeast endoplasmic reticulum membrane a...

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PMID: 8612571
PMCID: PMC450055

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae.PMID 8612571Read ↗

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Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein.Semantic proximity Read ↗

Stability and function of the Sec61 translocation complex depends on the Sss1p tail-anchor sequence.Semantic proximity Read ↗

An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation.Semantic proximity Read ↗

The Brl domain in Sec63p is required for assembly of functional endoplasmic reticulum translocons.Semantic proximity Read ↗

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N-acetylation and phosphorylation of Sec complex subunits in the ER membrane.Semantic proximity Read ↗

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