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.
Dell'Angelica
E C
EC
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
Klumperman
J
J
Stoorvogel
W
W
Bonifacino
J S
JS
D033942:Adaptor Proteins, Vesicular Transport; D000595:Amino Acid Sequence; D002966:Clathrin / Q000378:metabolism*; D011992:Endosomes / Q000737:chemistry; D005455:Fluorescent Antibody Technique; D006801:Humans; D007425:Intracellular Membranes / Q000737:chemistry; D019169:Jurkat Cells; D018613:Microscopy, Confocal; D016253:Microscopy, Immunoelectron; D008969:Molecular Sequence Data; D034041:Monomeric Clathrin Assembly Proteins; D009419:Nerve Tissue Proteins / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*; D010750:Phosphoproteins / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D016415:Sequence Alignment; D014617:Vacuoles / Q000737:chemistry
D033942:Adaptor Proteins, Vesicular Transport; D002966:Clathrin; D034041:Monomeric Clathrin Assembly Proteins; D009419:Nerve Tissue Proteins; D010750:Phosphoproteins; D011993:Recombinant Fusion Proteins; C439023:clathrin assembly protein AP180