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Association of the AP-3 Adaptor Complex with Clathrin

Science  17 Apr 1998:
Vol. 280, Issue 5362, pp. 431-434
DOI: 10.1126/science.280.5362.431

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Abstract

A heterotetrameric complex termed AP-3 is involved in signal-mediated protein sorting to endosomal-lysosomal organelles. AP-3 has been proposed to be a component of a nonclathrin coat. In vitro binding assays showed that mammalian AP-3 did associate with clathrin by interaction of the appendage domain of its β3 subunit with the amino-terminal domain of the clathrin heavy chain. The β3 appendage domain contained a conserved consensus motif for clathrin binding. AP-3 colocalized with clathrin in cells as observed by immunofluorescence and immunoelectron microscopy. Thus, AP-3 function in protein sorting may depend on clathrin.

  • * To whom correspondence should be addressed. E-mail: juan{at}helix.nih.gov

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