Gene Symbol: AP3M1
Description: adaptor related protein complex 3 subunit mu 1
Alias: AP-3 complex subunit mu-1, AP-3 adapter complex mu3A subunit, adapter-related protein complex 3 mu-1 subunit, adaptor related protein complex 3 mu 1 subunit, clathrin adaptor complex AP3, mu-3A subunit, mu-adaptin 3A, mu3A-adaptin
Species: human
Products:     AP3M1

Top Publications

  1. Dell Angelica E, Shotelersuk V, Aguilar R, Gahl W, Bonifacino J. 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;3:11-21 pubmed
    ..Our results suggest that AP-3 functions in protein sorting to lysosomes and provide an example of a human disease in which altered trafficking of integral membrane proteins is due to mutations in a component of the sorting machinery. ..
  2. Martinez Arca S, Rudge R, Vacca M, Raposo G, Camonis J, Proux Gillardeaux V, et al. A dual mechanism controlling the localization and function of exocytic v-SNAREs. Proc Natl Acad Sci U S A. 2003;100:9011-6 pubmed
    ..Moreover, they point to the amino-terminal domains of SNARE proteins as multifunctional modules responsible for the fine tuning of SNARE function. ..
  3. Mardones G, Burgos P, Lin Y, Kloer D, Magadán J, Hurley J, et al. Structural basis for the recognition of tyrosine-based sorting signals by the μ3A subunit of the AP-3 adaptor complex. J Biol Chem. 2013;288:9563-71 pubmed publisher
    ..The surface electrostatic potential of μ3A is less basic than that of μ2, in part explaining the association of AP-3 with intracellular membranes having less acidic phosphoinositides. ..
  4. Petrenko A, Pavlova L, Karseladze A, Kisseljov F, Kisseljova N. Downregulation of genes encoding for subunits of adaptor complex-3 in cervical carcinomas. Biochemistry (Mosc). 2006;71:1153-60 pubmed
    ..Using RT-PCR we demonstrated more than twofold decrease in the levels of mRNA of AP3D1, AP3B1, AP3M1, and AP3S1 in 32, 28, 23, and 26% tumors in comparison with normal tissues of uterine cervix, respectively...
  5. Gonçalves E, Fragoulis A, Garcia Alonso L, Cramer T, Saez Rodriguez J, Beltrao P. Widespread Post-transcriptional Attenuation of Genomic Copy-Number Variation in Cancer. Cell Syst. 2017;5:386-398.e4 pubmed publisher
    ..48 such rate-limiting interactions and experimentally confirmed our predictions on the interactions of AP3B1 with AP3M1 and GTF2E2 with GTF2E1...
  6. Stephens D, Banting G. Specificity of interaction between adaptor-complex medium chains and the tyrosine-based sorting motifs of TGN38 and lgp120. Biochem J. 1998;335 ( Pt 3):567-72 pubmed
    ..We also show that the newly identified mu-adaptin-related protein 2 (mu4) only interacts weakly with tyrosine-based sorting motifs. ..
  7. Lavezzari G, McCallum J, Dewey C, Roche K. Subunit-specific regulation of NMDA receptor endocytosis. J Neurosci. 2004;24:6383-91 pubmed
    ..Our findings demonstrate fundamental differences between NR2A and NR2B that help clarify developmental changes in NMDA receptor trafficking and surface expression. ..
  8. Craig H, Reddy T, Riggs N, Dao P, Guatelli J. Interactions of HIV-1 nef with the mu subunits of adaptor protein complexes 1, 2, and 3: role of the dileucine-based sorting motif. Virology. 2000;271:9-17 pubmed
  9. Vermeire J, Vanbillemont G, Witkowski W, Verhasselt B. The Nef-infectivity enigma: mechanisms of enhanced lentiviral infection. Curr HIV Res. 2011;9:474-89 pubmed
    ..Hereby we aim to contribute to a better understanding of this highly conserved and therapeutically attractive Nef function. ..

More Information


  1. Duvall Noelle N, Karwandyar A, Richmond A, Raman D. LASP-1: a nuclear hub for the UHRF1-DNMT1-G9a-Snail1 complex. Oncogene. 2016;35:1122-33 pubmed publisher
    ..LASP-1 also directly bound to Snail1 which may stabilize Snail1. Thus, nuclear LASP-1 appears to functionally serve as a hub for the epigenetic machinery. ..
  2. Coleman S, Van Damme N, Day J, Noviello C, Hitchin D, Madrid R, et al. Leucine-specific, functional interactions between human immunodeficiency virus type 1 Nef and adaptor protein complexes. J Virol. 2005;79:2066-78 pubmed
    ..This binding likely underlies the unusual ability of Nef to induce the stabilization of these complexes on endosomal membranes, an activity that correlates with enhancement of viral replication. ..
  3. Ivan V, Martinez Sanchez E, Sima L, Oorschot V, Klumperman J, Petrescu S, et al. AP-3 and Rabip4' coordinately regulate spatial distribution of lysosomes. PLoS ONE. 2012;7:e48142 pubmed publisher
    ..The most peripheral lysosomes were localized beyond microtubules, within the cortical actin network. Our results uncover a novel function for AP-3 and rabip4' in regulating lysosome positioning through an interorganellar pathway. ..
  4. Honing S, Sandoval I, Von Figura K. A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3. EMBO J. 1998;17:1304-14 pubmed
    ..This points to a function of AP-3 in intracellular sorting to lysosomes and melanosomes of a subset of cargo proteins via di-leucine-based sorting motifs. ..
  5. Dores M, Paing M, Lin H, Montagne W, Marchese A, Trejo J. AP-3 regulates PAR1 ubiquitin-independent MVB/lysosomal sorting via an ALIX-mediated pathway. Mol Biol Cell. 2012;23:3612-23 pubmed publisher
    ..Moreover, AP-3 facilitates PAR1 interaction with ALIX, suggesting that AP-3 functions before PAR1 engagement of ALIX and MVB/lysosomal sorting. ..
  6. Liu L, Sutton J, Woodruff E, Villalta F, Spearman P, Dong X. Defective HIV-1 particle assembly in AP-3-deficient cells derived from patients with Hermansky-Pudlak syndrome type 2. J Virol. 2012;86:11242-53 pubmed
  7. Sitaram A, Piccirillo R, Palmisano I, Harper D, Dell Angelica E, Schiaffino M, et al. Localization to mature melanosomes by virtue of cytoplasmic dileucine motifs is required for human OCA2 function. Mol Biol Cell. 2009;20:1464-77 pubmed publisher
    ..We conclude that OCA2 is targeted to and functions within melanosomes but that residence within melanosomes may be regulated by secondary or alternative targeting to lysosomes. ..
  8. Kimpler L, Glosson N, Downs D, Gonyo P, May N, Hudson A. Adaptor protein complexes AP-1 and AP-3 are required by the HHV-7 Immunoevasin U21 for rerouting of class I MHC molecules to the lysosomal compartment. PLoS ONE. 2014;9:e99139 pubmed publisher
    ..We also examine the impact of transient versus chronic knockdown of these adaptor protein complexes, and show that the few remaining ? subunits in the cells are eventually able to reroute class I molecules to lysosomes. ..
  9. Bultema J, Ambrosio A, Burek C, Di Pietro S. BLOC-2, AP-3, and AP-1 proteins function in concert with Rab38 and Rab32 proteins to mediate protein trafficking to lysosome-related organelles. J Biol Chem. 2012;287:19550-63 pubmed publisher
    ..Additionally, analysis of tyrosinase-related protein-2 and total melanin production indicates that Rab32 has unique functions that cannot be carried out by Rab38 in melanosome biogenesis. ..
  10. Van Damme N, Guatelli J. HIV-1 Vpu inhibits accumulation of the envelope glycoprotein within clathrin-coated, Gag-containing endosomes. Cell Microbiol. 2008;10:1040-57 pubmed
  11. Dell Angelica E, Ooi C, Bonifacino J. Beta3A-adaptin, a subunit of the adaptor-like complex AP-3. J Biol Chem. 1997;272:15078-84 pubmed
    ..The characteristics of beta3A-adaptin reported here lend support to the idea that AP-3 is a structural and functional homolog of the clathrin-associated adaptors AP-1 and AP-2. ..
  12. Madrid R, Le Maout S, Barrault M, Janvier K, Benichou S, Merot J. Polarized trafficking and surface expression of the AQP4 water channel are coordinated by serial and regulated interactions with different clathrin-adaptor complexes. EMBO J. 2001;20:7008-21 pubmed
    ..AQP4 phosphorylation by CKII may thus provide a mechanism that regulates AQP4 cell surface expression. ..
  13. Meng B, Lever A. Wrapping up the bad news: HIV assembly and release. Retrovirology. 2013;10:5 pubmed publisher
  14. Hashimoto R, Ohi K, Okada T, Yasuda Y, Yamamori H, Hori H, et al. Association analysis between schizophrenia and the AP-3 complex genes. Neurosci Res. 2009;65:113-5 pubmed publisher
    ..Nominal association between rs6688 in the AP3M1 gene and schizophrenia (chi(2)=6.33, P=0.012, odds ratio=0...
  15. Fatemifar G, Hoggart C, Paternoster L, Kemp J, Prokopenko I, Horikoshi M, et al. Genome-wide association study of primary tooth eruption identifies pleiotropic loci associated with height and craniofacial distances. Hum Mol Genet. 2013;22:3807-17 pubmed publisher
    ..Our results suggest that the genome-wide association approach is a powerful strategy for detecting variants involved in tooth eruption, and potentially craniofacial growth and more generally organ development. ..
  16. Drake M, Zhu Y, Kornfeld S. The assembly of AP-3 adaptor complex-containing clathrin-coated vesicles on synthetic liposomes. Mol Biol Cell. 2000;11:3723-36 pubmed
    ..These results establish that AP-3-containing clathrin-coated vesicles form in vitro and are consistent with AP-3-dependent protein transport being mediated by clathrin-coated vesicles...