Biology:AP3D1
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AP-3 complex subunit delta-1 is a protein that in humans is encoded by the AP3D1 gene.[1][2][3]
Function
AP3D1 is a subunit of the AP3 adaptor-like complex, which is not associated with clathrin. The AP3D1 subunit is implicated in intracellular biogenesis and trafficking of pigment granules and possibly platelet dense granules and neurotransmitter vesicles.[supplied by OMIM][3]
Interactions
AP3D1 has been shown to interact with SYBL1.[4]
References
- ↑ "Characterization of the adaptor-related protein complex, AP-3". The Journal of Cell Biology 137 (4): 835–45. May 1997. doi:10.1083/jcb.137.4.835. PMID 9151686.
- ↑ "Altered expression of a novel adaptin leads to defective pigment granule biogenesis in the Drosophila eye color mutant garnet". The EMBO Journal 16 (15): 4508–18. Aug 1997. doi:10.1093/emboj/16.15.4508. PMID 9303295.
- ↑ 3.0 3.1 "Entrez Gene: AP3D1 adaptor-related protein complex 3, delta 1 subunit". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8943.
- ↑ "A dual mechanism controlling the localization and function of exocytic v-SNAREs". Proceedings of the National Academy of Sciences of the United States of America 100 (15): 9011–6. Jul 2003. doi:10.1073/pnas.1431910100. PMID 12853575.
External links
- Human AP3D1 genome location and AP3D1 gene details page in the UCSC Genome Browser.
Further reading
- "A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3". The EMBO Journal 17 (5): 1304–14. Aug 1998. doi:10.1093/emboj/17.5.1304. PMID 9482728.
- "Mutation in AP-3 delta in the mocha mouse links endosomal transport to storage deficiency in platelets, melanosomes, and synaptic vesicles". Neuron 21 (1): 111–22. Jul 1998. doi:10.1016/S0896-6273(00)80519-X. PMID 9697856.
- "Formation of AP-3 transport intermediates requires Vps41 function". Nature Cell Biology 1 (6): 346–53. 2000. doi:10.1038/14037. PMID 10559961.
- "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 271 (1): 9–17. May 2000. doi:10.1006/viro.2000.0277. PMID 10814565.
- "PACS-1 binding to adaptors is required for acidic cluster motif-mediated protein traffic". The EMBO Journal 20 (9): 2191–201. May 2001. doi:10.1093/emboj/20.9.2191. PMID 11331585.
- "Site-specific cross-linking reveals a differential direct interaction of class 1, 2, and 3 ADP-ribosylation factors with adaptor protein complexes 1 and 3". Biochemistry 41 (14): 4669–77. Apr 2002. doi:10.1021/bi016064j. PMID 11926829.
- "HIV-1 Nef stabilizes the association of adaptor protein complexes with membranes". The Journal of Biological Chemistry 278 (10): 8725–32. Mar 2003. doi:10.1074/jbc.M210115200. PMID 12486136.
- "Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1". Developmental Cell 5 (3): 513–21. Sep 2003. doi:10.1016/S1534-5807(03)00234-X. PMID 12967569.
- "The zinc transporter ZnT3 interacts with AP-3 and it is preferentially targeted to a distinct synaptic vesicle subpopulation". Molecular Biology of the Cell 15 (2): 575–87. Feb 2004. doi:10.1091/mbc.E03-06-0401. PMID 14657250.
- "An ear-core interaction regulates the recruitment of the AP-3 complex to membranes". Developmental Cell 7 (4): 619–25. Oct 2004. doi:10.1016/j.devcel.2004.08.009. PMID 15469849.
- "Leucine-specific, functional interactions between human immunodeficiency virus type 1 Nef and adaptor protein complexes". Journal of Virology 79 (4): 2066–78. Feb 2005. doi:10.1128/JVI.79.4.2066-2078.2005. PMID 15681409.
- "AP-3 directs the intracellular trafficking of HIV-1 Gag and plays a key role in particle assembly". Cell 120 (5): 663–74. Mar 2005. doi:10.1016/j.cell.2004.12.023. PMID 15766529.
- "Functions of adaptor protein (AP)-3 and AP-1 in tyrosinase sorting from endosomes to melanosomes". Molecular Biology of the Cell 16 (11): 5356–72. 2006. doi:10.1091/mbc.E05-07-0626. PMID 16162817.
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