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Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane

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Item Type:Article
Title:Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
Creators Name:Goerlich, D. and Rapoport, T.A.
Abstract:We have reproduced the process of protein transport across and of protein integration into the mammalian endoplasmic reticulum membrane by the use of proteoliposomes reconstituted from pure phospholipids and purified membrane proteins. The transport of some proteins requires only two membrane protein complexes: the signal recognition particle receptor, needed for targeting of a nascent chain to the membrane, and a novel complex, the Sec61p complex, that consists of Sec61p and two smaller polypeptides. The translocation of other proteins also needs the presence of the translocating chain-association membrane (TRAM) protein. The integration of two membrane proteins of different topologies into the membrane does not require additional components. These results indicate a surprising simplicity of the basic translocation machinery. They suggest that the Sec61p complex binds the ribosome during translocation and forms the postulated protein-conducting channel.
Keywords:Asialoglycoprotein Receptor, Biological Transport, Cell Compartmentation, Endopeptidases, Endoplasmic Reticulum, Intracellular Membranes, Macromolecular Substances, Membrane Glycoproteins, Membrane Proteins, Prolactin, Protein Precursors, Proteolipids, Cell Surface Receptors, Cytoplasmic and Nuclear Receptors, Peptide Receptors, Serine Endopeptidases, Viral Envelope Proteins, Animals, Dogs
Source:Cell
ISSN:0092-8674
Publisher:Cell Press (U.S.A.)
Volume:75
Number:4
Page Range:615-630
Date:19 November 1993
Official Publication:https://doi.org/10.1016/0092-8674(93)90483-7
PubMed:View item in PubMed

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