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Article

The Brl domain in Sec63p is required for assembly of functional endoplasmic reticulum translocons.

The Journal of biological chemistry - 24 Mar 2006

Jermy Andrew J, Willer Martin, Davis Elaine, Wilkinson Barrie M, Stirling Colin J

Abstract excerpt

Protein translocation into the endoplasmic reticulum occurs at pore-forming structures known as translocons. In yeast, two different targeting pathways converge at a translocation pore formed by the Sec61 complex. The signal recognition particle-dependent pathway targets nascent precursors co-translationally, whereas the Sec62p-dependent pathway targets polypeptides post-translationally. In addition to the Sec61...

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PMID: 16368690
DOI: 10.1074/jbc.M511402200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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The Brl domain in Sec63p is required for assembly of functional endoplasmic reticulum translocons.PMID 16368690Read ↗

Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo.Semantic proximity Read ↗

The Sec63p J-domain is required for ERAD of soluble proteins in yeast.Semantic proximity Read ↗

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

Distinct domains within yeast Sec61p involved in post-translational translocation and protein dislocation.Semantic proximity Read ↗

Genetic interactions between KAR2 and SEC63, encoding eukaryotic homologues of DnaK and DnaJ in the endoplasmic reticulum.Semantic proximity Read ↗

Two alternative binding mechanisms connect the protein translocation Sec71-Sec72 complex with heat shock proteins.Semantic proximity Read ↗

Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER.Semantic proximity Read ↗

Signal sequences specify the targeting route to the endoplasmic reticulum membrane.Semantic proximity Read ↗

Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae.Semantic proximity Read ↗

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

Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum.Semantic proximity Read ↗

Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP.Semantic proximity Read ↗

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