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.
Mesh Terms:
Adaptor Proteins, Vesicular Transport, Amino Acid Sequence, Clathrin, Endosomes, Fluorescent Antibody Technique, Humans, Intracellular Membranes, Jurkat Cells, Microscopy, Confocal, Microscopy, Immunoelectron, Molecular Sequence Data, Monomeric Clathrin Assembly Proteins, Nerve Tissue Proteins, Phosphoproteins, Recombinant Fusion Proteins, Sequence Alignment, Vacuoles
Adaptor Proteins, Vesicular Transport, Amino Acid Sequence, Clathrin, Endosomes, Fluorescent Antibody Technique, Humans, Intracellular Membranes, Jurkat Cells, Microscopy, Confocal, Microscopy, Immunoelectron, Molecular Sequence Data, Monomeric Clathrin Assembly Proteins, Nerve Tissue Proteins, Phosphoproteins, Recombinant Fusion Proteins, Sequence Alignment, Vacuoles
Science
Date: Apr. 17, 1998
PubMed ID: 9545220
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