Skip to main content

AP-3

  • Reference work entry
  • First Online:
Encyclopedia of Signaling Molecules
  • 358 Accesses

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...

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 4,499.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Hardcover Book
USD 4,499.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

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.

    Article  PubMed  PubMed Central  Google Scholar 

  • Badolato R, Parolini S. Novel insights from adaptor protein 3 complex deficiency. J Allergy Clin Immunol. 2007;120(4):735–41. quiz 42–3.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  • Bonifacino JS, Traub LM. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu Rev Biochem. 2003;72:395–447.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  • Danglot L, Galli T. What is the function of neuronal AP-3? Biol Cell. 2007;99(7):349–61.

    Article  PubMed  CAS  Google Scholar 

  • Dell’Angelica EC. AP-3-dependent trafficking and disease: the first decade. Curr Opin Cell Biol. 2009;21(4):552–9.

    Article  PubMed  CAS  Google Scholar 

  • Dell’Angelica EC, Klumperman J, Stoorvogel W, Bonifacino JS. Association of the AP-3 adaptor complex with clathrin. Science. 1998;280(5362):431–4.

    Article  PubMed  Google Scholar 

  • 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.

    Article  PubMed  Google Scholar 

  • 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.

    Article  PubMed  PubMed Central  Google Scholar 

  • 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.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  • 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.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  • 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.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  • 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.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • Odorizzi G, Cowles CR, Emr SD. The AP-3 complex: a coat of many colours. Trends Cell Biol. 1998;8(7):282–8.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • Raposo G, Marks MS. Melanosomes – dark organelles enlighten endosomal membrane transport. Nat Rev Mol Cell Biol. 2007;8(10):786–97.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  • 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.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Andrew A. Peden .

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2018 Springer International Publishing AG

About this entry

Check for updates. Verify currency and authenticity via CrossMark

Cite this entry

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

Download citation

Publish with us

Policies and ethics