Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation - PubMed (original) (raw)

Comparative Study

Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation

L H Wang et al. J Cell Biol. 1993 Dec.

Abstract

The clathrin-coated pit lattice is held onto the plasma membrane by an integral membrane protein that binds the clathrin AP-2 subunit with high affinity. In vitro studies have suggested that this protein controls the assembly of the pit because membrane bound AP-2 is required for lattice assembly. If so, the AP-2 binding site must be a resident protein of the coated pit and recycle with other receptors that enter cells through this pathway. Proper recycling, however, would require the switching off of AP-2 binding to allow the binding site to travel through the endocytic pathway unencumbered. Evidence for this hypothesis has been revealed by the cationic amphiphilic class of drugs (CAD), which have previously been found to inhibit receptor recycling. Incubation of human fibroblasts in the presence of these drugs caused clathrin lattices to assemble on endosomal membranes and at the same time prevented coated pit assembly at the cell surface. These effects suggest that CADs reverse an on/off switch that controls AP-2 binding to membranes. We conclude that cells have a mechanism for switching on and off AP-2 binding during the endocytic cycle.

PubMed Disclaimer

References

    1. J Biol Chem. 1981 Nov 25;256(22):11923-31 - PubMed
    1. Cell. 1981 May;24(2):493-502 - PubMed
    1. Dev Biol. 1983 Oct;99(2):456-72 - PubMed
    1. J Cell Physiol. 1984 Feb;118(2):193-202 - PubMed
    1. Methods Enzymol. 1983;98:241-60 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources