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Review
. 1989 Aug;1(4):617-23.
doi: 10.1016/0955-0674(89)90024-0.

Sorting signals

Affiliations
Review

Sorting signals

P P Breitfeld et al. Curr Opin Cell Biol. 1989 Aug.
No abstract available

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References

    1. Kornfeld S. Trafficking of lysomal enzymes. FASEB J. 1987;1:462–468. Of interest. - PubMed
    2. Very readable review of the M-6-P signal and its receptor, which target enzymes to lysosomes. The authors' laboratory has been the source of much of our knowledge in this field.

    1. Bartles J.R., Hubbard A.L. Plasma membrane protein sorting in epithelial cells: do secretory pathways hold the key? Trends Biochem Sci. 1988;13:181–184. Of interest. - PubMed
    2. Compares data on secretion and membrane traffic in the cannonical MDCK system with the authors' observations on hepatocytes. Raises several useful questions about the relationship between traffic of membrane and soluble proteins.

    1. Kelly R.B. The cell biology of the nerve terminal - review. Neuron. 1988;1:431–437. Of interest. - PMC - PubMed
    2. Although this review is officially about neuronal cells, it is from a strong cell biological perspective. It synthesizes a wealth of information on targeting, exocytosis and endocytosis, especially in cells with a regulated pathway.

    1. Simons K., Van Meer G. Lipid sorting in epithelial cells. Biochemistry. 1988;27:6197–6202. Of outstanding interest. - PubMed
    2. Summarizes work, primarily from the authors' laboratories, on the specific sorting of glycolipids to the apical surface of epithelial cells. They make the provocative hypothesis that these lipids self-aggregate into sorted domains and that these mediate the apical targeting of proteins. They also argue that the default pathway for membrane proteins is generally to the basolateral surface.

    1. Brodsky F.M. Living with clathrin: its role in intracellular membrane traffic. Science. 1988;242:1396–1402. Of interest. - PubMed
    2. The role of clathrin has been controversial, because certain yeast mutants can survive without it. The author presents a balanced view of the structure and function of clathrin.

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