Historical Background
The cytoplasm of all eukaryotic cells is organized into a complex set of membrane-bound organelles with defined protein and lipid composition. Proteins and lipids of the endocytic and exocytic pathways are transported between these compartments by small vesicles and tubules which pinch off from one compartment and fuse with another and so deliver their contents. The budding of vesicles and tubules from membranes is driven by the recruitment of coat protein complexes from the cytoplasm. Coat complexes have two main functions in this process: First, they select cargo proteins to be packaged into the vesicle, and second, they recruit accessory proteins that help deform the membrane into a bud and bind machinery required for vesicle fission.
In mammalian cells, there are five related adaptor protein (AP) complexes (AP-1 through 5) (Hirst et al. 2011). Each complex is localized to a specific post-Golgi compartment and is required for the transport of a defined set of...
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References
Azevedo C, Burton A, Ruiz-Mateos E, Marsh M, Saiardi A. Inositol pyrophosphate mediated pyrophosphorylation of AP3B1 regulates HIV-1 Gag release. Proc Natl Acad Sci USA. 2009;106(50):21161–6.
Badolato R, Parolini S. Novel insights from adaptor protein 3 complex deficiency. J Allergy Clin Immunol. 2007;120(4):735–41. quiz 42–3.
Baust T, Anitei M, Czupalla C, Parshyna I, Bourel L, Thiele C, et al. Protein networks supporting AP-3 function in targeting lysosomal membrane proteins. Mol Biol Cell. 2008;19(5):1942–51.
Bonifacino JS, Traub LM. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu Rev Biochem. 2003;72:395–447.
Craige B, Salazar G, Faundez V. Phosphatidylinositol-4-kinase type II alpha contains an AP-3-sorting motif and a kinase domain that are both required for endosome traffic. Mol Biol Cell. 2008;19(4):1415–26.
Danglot L, Galli T. What is the function of neuronal AP-3? Biol Cell. 2007;99(7):349–61.
Dell’Angelica EC. AP-3-dependent trafficking and disease: the first decade. Curr Opin Cell Biol. 2009;21(4):552–9.
Dell’Angelica EC, Klumperman J, Stoorvogel W, Bonifacino JS. Association of the AP-3 adaptor complex with clathrin. Science. 1998;280(5362):431–4.
Dell’Angelica EC, Shotelersuk V, Aguilar RC, Gahl WA, Bonifacino JS. Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor. Mol Cell. 1999;3(1):11–21.
Di Pietro SM, Falcon-Perez JM, Tenza D, Setty SR, Marks MS, Raposo G, et al. BLOC-1 interacts with BLOC-2 and the AP-3 complex to facilitate protein trafficking on endosomes. Mol Biol Cell. 2006;17(9):4027–38.
Faundez VV, Kelly RB. The AP-3 complex required for endosomal synaptic vesicle biogenesis is associated with a casein kinase Ialpha-like isoform. Mol Biol Cell. 2000;11(8):2591–604.
Hirst J, Barlow LD, Francisco GC, Sahlender DA, Seaman MN, Dacks JB, et al. The fifth adaptor protein complex. PLoS Biol. 2011;9(10):e1001170.
Jackson LP, Kelly BT, McCoy AJ, Gaffry T, James LC, Collins BM, et al. A large-scale conformational change couples membrane recruitment to cargo binding in the AP2 clathrin adaptor complex. Cell. 2010;141(7):1220–9.
Janvier K, Kato Y, Boehm M, Rose JR, Martina JA, Kim BY, et al. Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1 gamma-sigma1 and AP-3 delta-sigma3 hemicomplexes. J Cell Biol. 2003;163(6):1281–90.
Lefrancois S, Janvier K, Boehm M, Ooi CE, Bonifacino JS. An ear-core interaction regulates the recruitment of the AP-3 complex to membranes. Dev Cell. 2004;7(4):619–25.
Nie Z, Boehm M, Boja ES, Vass WC, Bonifacino JS, Fales HM, et al. Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1. Dev Cell. 2003;5(3):513–21.
Odorizzi G, Cowles CR, Emr SD. The AP-3 complex: a coat of many colours. Trends Cell Biol. 1998;8(7):282–8.
Ohno H, Aguilar RC, Yeh D, Taura D, Saito T, Bonifacino JS. The medium subunits of adaptor complexes recognize distinct but overlapping sets of tyrosine-based sorting signals. J Biol Chem. 1998;273(40):25915–21.
Raposo G, Marks MS. Melanosomes – dark organelles enlighten endosomal membrane transport. Nat Rev Mol Cell Biol. 2007;8(10):786–97.
Simpson F, Peden AA, Christopoulou L, Robinson MS. Characterization of the adaptor-related protein complex, AP-3. J Cell Biol. 1997;137(4):835–45.
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Peden, A.A. (2018). AP-3. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_548
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DOI: https://doi.org/10.1007/978-3-319-67199-4_548
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