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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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 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.[1]

References

  1. Association of the AP-3 adaptor complex with clathrin. Dell'Angelica, E.C., Klumperman, J., Stoorvogel, W., Bonifacino, J.S. Science (1998) [Pubmed]
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