RT Journal Article
SR Electronic
T1 Association of the AP-3 Adaptor Complex with Clathrin
JF Science
JO Science
FD American Association for the Advancement of Science
SP 431
OP 434
DO 10.1126/science.280.5362.431
VO 280
IS 5362
A1 Dell'Angelica, Esteban C.
A1 Klumperman, Judith
A1 Stoorvogel, Willem
A1 Bonifacino, Juan S.
YR 1998
UL http://science.sciencemag.org/content/280/5362/431.abstract
AB 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.