Molecular mechanism of membrane protein integration into the endoplasmic reticulum.

W Mothes, S U Heinrich, R Graf, I Nilsson, G von Heijne, J Brunner, T A Rapoport
Author Information
  1. W Mothes: Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.

Abstract

As proteins are integrated into the membrane of the endoplasmic reticulum, some hydrophilic polypeptide segments are transported through the translocation channel, others remain in the cytosol, and hydrophobic transmembrane sequences are released into the lipid phase. We have addressed the molecular mechanism by which these events occur. We demonstrate that both the lumenal and the cytosolic domains of a membrane protein are synthesized while the ribosome is membrane bound, so that even cytosolic domains come in contact with the translocation channel. We also find that, before translation of the protein is terminated, transmembrane sequences can laterally exit the translocation channel and enter the lipid environment. These results have significant implications for the folding and assembly of membrane proteins.

MeSH Term

Animals
Binding Sites
Cytosol
Endoplasmic Reticulum
In Vitro Techniques
Membrane Lipids
Membrane Proteins
Models, Biological
Molecular Structure
Protein Biosynthesis
Protein Folding
Ribosomes

Chemicals

Membrane Lipids
Membrane Proteins

Word Cloud

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