Membrane protein insertion at the endoplasmic reticulum.

@article{Shao2011MembranePI,
  title={Membrane protein insertion at the endoplasmic reticulum.},
  author={Sichen Shao and Ramanujan S. Hegde},
  journal={Annual review of cell and developmental biology},
  year={2011},
  volume={27},
  pages={
          25-56
        }
}
  • S. Shao, R. Hegde
  • Published 10 October 2011
  • Biology
  • Annual review of cell and developmental biology
Integral membrane proteins of the cell surface and most intracellular compartments of eukaryotic cells are assembled at the endoplasmic reticulum. Two highly conserved and parallel pathways mediate membrane protein targeting to and insertion into this organelle. The classical cotranslational pathway, utilized by most membrane proteins, involves targeting by the signal recognition particle followed by insertion via the Sec61 translocon. A more specialized posttranslational pathway, employed by… 

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References

SHOWING 1-10 OF 183 REFERENCES
Cotranslational Membrane Protein Biogenesis at the Endoplasmic Reticulum*
TLDR
The most recent advances in the understanding of cotranslational integration at the ER membrane are highlighted, focusing on four overlapping areas: translocon structural and functional states; nascent chain topogenesis; insertion of TMSs into the bilayer; and nascent chain regulation of integration.
Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
TLDR
Structural, genetic and biochemical data show how the channel opens across the membrane, releases hydrophobic segments of membrane proteins laterally into lipid, and maintains the membrane barrier for small molecules.
Slow translocon gating causes cytosolic exposure of transmembrane and lumenal domains during membrane protein integration
TLDR
In vivo kinetics of integration of model membrane proteins in Saccharomyces cerevisiae are analyzed using ubiquitin translocation assay reporters to indicate that the conformational changes in the translocon that permit opening of the lumenal and lateral channel gates occur less rapidly than elongation of the nascent polypeptide.
Molecular Mechanism of Membrane Protein Integration into the Endoplasmic Reticulum
Membrane-protein integration and the role of the translocation channel.
How translocons select transmembrane helices.
TLDR
This work considers the connection between the physical principles of membrane protein stability and translocon selection of transmembrane helices, and reviews the progress made during the past several years toward understanding the physical chemistry of membraneprotein stability, the structure of the translocon machine, and the mechanisms by which the translcon selects and inserts transmem BR helices.
Cellular mechanisms of membrane protein folding
  • W. Skach
  • Biology
    Nature Structural &Molecular Biology
  • 2009
TLDR
This Perspective will focus on emerging evidence that the RTC functions as a protein-folding machine that restricts conformational space by establishing transmembrane topology and yet provides a permissive environment that enables nascent trans Membrane domains to efficiently progress down their folding energy landscape.
Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins
TLDR
It is shown here that newly synthesised RAMP4 and Sec61β can accumulate in a cytosolic, soluble complex with the ATPase Asna1 before insertion into ER-derived membranes.
Topogenesis of membrane proteins at the endoplasmic reticulum.
TLDR
A model emerges in which the translocon allows the lateral partitioning of hydrophobic segments between the aqueous pore and the lipid membrane, and signals may return into the pore for reorientation until translation is terminated.
...
1
2
3
4
5
...