A C-terminal signal prevents secretion of luminal ER proteins

@article{Munro1987ACS,
  title={A C-terminal signal prevents secretion of luminal ER proteins},
  author={Sean Munro and Hugh R. Pelham},
  journal={Cell},
  year={1987},
  volume={48},
  pages={899-907}
}

Figures from this paper

Signals and mechanisms for protein retention in the endoplasmic reticulum

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The retention signal for soluble proteins of the endoplasmic reticulum.

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Recently it was found that di-lysine motifs bind the complex of cytosolic coat proteins, COP I, and that this interaction functions in the retrieval of proteins from the Golgi to the ER, and the potential roles this interaction may have in vesicular trafficking.

A Short N-Terminal Sequence is Responsible for the Retention of Invariant Chain (Ii) in the Endoplasmic Reticulum

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The secretion of proteins by cells

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ERD2, a Yeast Gene Required for the Receptor-Mediated Retrieval Proteins from the Secretory Pathway of Luminal ER

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Retrieval of transmembrane proteins to the endoplasmic reticulum

Differences in the subcellular distribution and rate of post-translational modification of CD8 maintained in the ER by sequences derived from a variety of ER resident proteins suggested that the efficiency of retrieval was dependent on the sequence context of the double lysine motif and that retrieval may be initiated from multiple positions along the exocytotic pathway.
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References

SHOWING 1-10 OF 36 REFERENCES

Deletions into an NH2-terminal hydrophobic domain result in secretion of rotavirus VP7, a resident endoplasmic reticulum membrane glycoprotein

It is suggested that the second hydrophobic domain contributes to a positive signal for ER location and a membrane anchor function, and secretion of the mutant glycoprotein implies that transport can be constitutive with the destination being dictated by an overriding compartmentalization signal.

The glucose-regulated protein grp94 is related to heat shock protein hsp90.

Four secretory proteins synthesized by hepatocytes are transported from endoplasmic reticulum to Golgi complex at different rates.

The proteins were found to be transported from the endoplasmic reticulum (ER) to the Golgi complex (GC) at greatly different rates, indicating that transport of secretory proteins between these organelles is effected by a selective, possibly receptor‐mediated process and not through bulk phase transfers.

Endoplasmic reticulum contains a common, abundant calcium-binding glycoprotein, endoplasmin.

Calcium-binding studies show that endoplasmin is a major calcium-binding protein in cells, suggesting that at least one of its roles might be in the calcium-storage function of the endoplasmic reticulum.

What regulates secretion of non‐stored proteins by eukaryotic cells?

  • A. GebhartR. Ruddon
  • Biology
    BioEssays : news and reviews in molecular, cellular and developmental biology
  • 1986
The evidence reviewed here strongly suggests that there are post‐synthesis rate‐limiting steps for many proteins released by the ‘constitutive’ pathway and, hence, that regulation in some sense is involved here too.

Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin

The sequence of cloned rat liver PDI complementary DNA is described which predicts a protein with two distinct regions homologous with Escherichia coli thioredoxin, a known cofactor in oxidation–reduction reactions, suggesting that PDI, similar in action to thiOREDoxin, catalyses disulphide bond interchange via an internal disulPHide–sulphydryl interchange.

The golgi apparatus: two organelles in tandem.

The Golgi apparatus consists of distinct cis and trans compartments that may act sequentially to refine the protein export of the endoplasmic reticulum by removing escaped endoplasmic reticulum