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

      research-article
      The Journal of Cell Biology
      The Rockefeller University Press

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          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.

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          Author and article information

          Journal
          J Cell Biol
          The Journal of Cell Biology
          The Rockefeller University Press
          0021-9525
          1540-8140
          1 December 1993
          : 123
          : 5
          : 1107-1117
          Article
          94064774
          10.1083/jcb.123.5.1107
          2119875
          8245121
          3d204eff-c636-4f6d-895b-39bf2e329a6e
          History
          Categories
          Articles

          Cell biology
          Cell biology

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