The AP-3 complex: a coat of many colours.
A new adaptor protein complex, termed AP-3, has recently been identified in mammalian cells, and genetic studies in yeast have revealed a functional role for the AP-3 complex in cargo-selective transport via a new alternative trafficking pathway from the Golgi to the vacuole/lysosome. Here, the authors review what is currently known about the AP-3 complex and discuss recent insight into its function in multicellular organisms that has come from the finding that mutations in AP-3 subunits correspond to classical mutations in Drosophila and mice.
Division of Cellular and Molecular Medicine, University of California, San Diego, La Jolla 92093-0668, USA.
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D033942:Adaptor Proteins, Vesicular Transport; D000818:Animals; D001692:Biological Transport / Q000502:physiology; D004791:Enzyme Inhibitors / Q000378:metabolism*; D005057:Eukaryotic Cells / Q000737:chemistry / Q000378:metabolism; D006056:Golgi Apparatus / Q000737:chemistry / Q000378:metabolism*; D008247:Lysosomes / Q000737:chemistry / Q000378:metabolism*; D034041:Monomeric Clathrin Assembly Proteins; D009419:Nerve Tissue Proteins / Q000502:physiology*; D010750:Phosphoproteins / Q000502:physiology*
D033942:Adaptor Proteins, Vesicular Transport; D004791:Enzyme Inhibitors; D034041:Monomeric Clathrin Assembly Proteins; D009419:Nerve Tissue Proteins; D010750:Phosphoproteins; C439023:clathrin assembly protein AP180