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Review
. 1994 Aug;6(4):517-21.
doi: 10.1016/0955-0674(94)90070-1.

Retention and retrieval in the endoplasmic reticulum and the Golgi apparatus

T Nilsson  1 , G Warren
Affiliations
Review

Retention and retrieval in the endoplasmic reticulum and the Golgi apparatus

T Nilsson et al. Curr Opin Cell Biol. 1994 Aug.

Abstract

Resident proteins of the exocytic pathway contain at least two types of information in their primary sequence for determining their subcellular location. The first type of information is found at the carboxyl terminus of soluble proteins of the endoplasmic reticulum (ER) and in the cytoplasmic domain of some ER and Golgi membrane proteins. It acts as a retrieval signal, returning proteins that have left the compartment in which they reside. The second type of information has been found in the membrane-spanning domain of several ER and Golgi proteins and, though the mechanism by which it operates is still unclear, it acts as a retention signal, keeping the protein at a particular location within the organelle. The presence of both a retrieval signal and a retention signal in a trans-Golgi network resident protein suggests that more than one mechanism operates to ensure correct localization of resident proteins along the exocytic pathway.

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References

    1. Pfeffer S.R., Rothman J.E. Biosynthetic Protein Transport and Sorting by the Endoplasmic Reticulum and Golgi. Annu Rev Biochem. 1987;56:829–852. - PubMed
    1. Ahn K., Szczesna S.E., Kemper B. The Amino-Terminal 29 Amino Acids of Cytochrome P450 2C1 Are Sufficient for Retention in the Endoplasmic Reticulum. J Biol Chem. 1993;268:18726–18733. of special interest. - PubMed

    2. The hydrophobic amino terminus of P450 spans the membrane and is both necessary and sufficient to retain reporter molecules in the ER.

    1. Bangs J.D., Uyetake L., Brickman M.J., Balber A.E., Boothroyd J.C. Molecular Cloning and Cellular Localization of a BiP Homologue in Trypanosoma brucei. Divergent ER Retention Signals in a Lower Eukaryote. J Cell Sci. 1993;105:1101–1113. - PubMed
    1. David V., Hochstenbach F., Rajagopalan S., Brenner M.B. Interaction with Newly Synthesized and Retained Proteins in the Endoplasmic Reticulum Suggests a Chaperone Function for Human Integral Membrane Protein IP90 (Calnexin) J Biol Chem. 1993;268:9585–9592. of special interest. - PubMed

    2. Human calnexin has the carboxy-terminal sequence RKPRRE, which may act in a similar manner to the double-lysine motif to retain the protein in the ER.

    1. Delahunty M.D., Stafford F.J., Yuan L.C., Shaz D., Bonifacino J.S. Uncleaved Signals for Glycosylphosphatidylinositol Anchoring Cause Retention of Precursor Proteins in the Endoplasmic Reticulum. J Biol Chem. 1993;268:12017–12027. of special interest. - PubMed

    2. In the absence of transfer to glycosylphosphatidylinositol, the protein is retained in the ER by a carboxy-terminal membrane anchor that appears to work by oligomerization.

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