Polypeptide-binding proteins mediate completion of co-translational protein translocation into the mammalian endoplasmic reticulum Journal Article


Authors: Tyedmers, J.; Lerner, M.; Wiedmann, M.; Volkmer, J.; Zimmermann, R.
Article Title: Polypeptide-binding proteins mediate completion of co-translational protein translocation into the mammalian endoplasmic reticulum
Abstract: The first step in the secretion of most mammalian proteins is their transport into the lumen of the endoplasmic reticulum (ER). Transport of pre-secretory proteins into the mammalian ER requires signal peptides in the precursor proteins and a protein translocase in the ER membrane. In addition, hitherto unidentified lumenal ER proteins have been shown to be required for vectorial protein translocation. This requirement was confirmed in this study by using proteoliposomes that were made from microsomal detergent extracts and contained either low or high concentrations of lumenal ER proteins. Furthermore, immunoglobulin-heavy-chain-binding protein (BiP) was shown to he able to substitute for the full set of lumenal proteins and, in the case of biotinylated precursor proteins, avidin was found to be able to substitute for lumenal proteins. Thus, the polypeptide-chain-binding protein BiP was identified as one lumenal protein that is involved in efficient vectorial protein translocation into the mammalian ER.
Keywords: signal transduction; controlled study; gene translocation; nonhuman; protein function; protein analysis; mammalia; animals; protein protein interaction; protein binding; membrane proteins; intracellular transport; rna; endoplasmic reticulum; immunoglobulin heavy chain; protein processing; protein processing, post-translational; dogs; mammal; protein transport; protein secretion; protein biosynthesis; binding protein; binding sites; concentration (parameters); biotinylation; molecular chaperones; heat-shock proteins; secretory protein; protein precursor; avidin; microsomes; priority journal; article; proteoliposome; proteolipids
Journal Title: EMBO Reports
Volume: 4
Issue: 5
ISSN: 1469-221X
Publisher: Wiley Blackwell  
Date Published: 2003-05-01
Start Page: 505
End Page: 510
Language: English
DOI: 10.1038/sj.embor.embor826
PUBMED: 12704426
PROVIDER: scopus
PMCID: PMC1319181
DOI/URL:
Notes: Export Date: 12 September 2014 -- Source: Scopus
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