| First Author | Dell'Angelica EC | Year | 1998 |
| Journal | Science | Volume | 280 |
| Issue | 5362 | Pages | 431-4 |
| PubMed ID | 9545220 | Mgi Jnum | J:320336 |
| Mgi Id | MGI:6872264 | Doi | 10.1126/science.280.5362.431 |
| Citation | Dell'Angelica EC, et al. (1998) Association of the AP-3 adaptor complex with clathrin. Science 280(5362):431-4 |
| abstractText | 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 beta3 subunit with the amino-terminal domain of the clathrin heavy chain. The beta3 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. |
