Association of the AP-3 Adaptor Complex with Clathrin

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 doma...

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Veröffentlicht in:Science (American Association for the Advancement of Science) 1998-04, Vol.280 (5362), p.431-434
Hauptverfasser: Dell'Angelica, Esteban C., Klumperman, Judith, Stoorvogel, Willem, Bonifacino, Juan S.
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Sprache:eng
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Zusammenfassung: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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.280.5362.431