Biology:APBA1
 Generic protein structure example |
Amyloid beta A4 precursor protein-binding family A member 1 is a protein that in humans is encoded by the APBA1 gene.[1][2][3]
Function
The protein encoded by this gene is a member of the X11 protein family. It is a neuronal adaptor protein that interacts with the Alzheimer's disease amyloid precursor protein (APP). It stabilises APP and inhibits production of proteolytic APP fragments including the A beta peptide that is deposited in the brains of Alzheimer's disease patients. This gene product is believed to be involved in signal transduction processes. It is also regarded as a putative vesicular trafficking protein in the brain that can form a complex with the potential to couple synaptic vesicle exocytosis to neuronal cell adhesion.[3]
Interactions
APBA1 has been shown to interact with KCNJ12,[4][5] CCS,[6] CASK[7][8] and Amyloid precursor protein.[9][10]
References
- ↑ "Gene in the region of the Friedreich ataxia locus encodes a putative transmembrane protein expressed in the nervous system". Proc Natl Acad Sci U S A 90 (1): 109–13. February 1993. doi:10.1073/pnas.90.1.109. PMID 7678331. Bibcode: 1993PNAS...90..109D.
- ↑ "Comparison of primary structure of a neuron-specific protein, X11, between human and mouse". Mamm Genome 6 (1): 57–8. May 1995. doi:10.1007/BF00350899. PMID 7719031.
- ↑ 3.0 3.1 "Entrez Gene: APBA1 amyloid beta (A4) precursor protein-binding, family A, member 1 (X11)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=320.
- ↑ "Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins". J. Biol. Chem. 279 (21): 22331–46. May 2004. doi:10.1074/jbc.M400285200. PMID 15024025.
- ↑ "A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium channels". J. Biol. Chem. 279 (18): 19051–63. April 2004. doi:10.1074/jbc.M400284200. PMID 14960569.
- ↑ "The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity". J. Biol. Chem. 276 (12): 9303–7. March 2001. doi:10.1074/jbc.M010023200. PMID 11115513.
- ↑ "Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting". J. Biol. Chem. 273 (48): 31633–6. November 1998. doi:10.1074/jbc.273.48.31633. PMID 9822620.
- ↑ "Molecular analysis of the X11-mLin-2/CASK complex in brain". J. Neurosci. 19 (4): 1307–16. February 1999. doi:10.1523/JNEUROSCI.19-04-01307.1999. PMID 9952408.
- ↑ "Regulation of APP-dependent transcription complexes by Mint/X11s: differential functions of Mint isoforms". J. Neurosci. 22 (17): 7340–51. September 2002. doi:10.1523/JNEUROSCI.22-17-07340.2002. PMID 12196555.
- ↑ "The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein". Mol. Cell. Biol. 16 (11): 6229–41. November 1996. doi:10.1128/mcb.16.11.6229. PMID 8887653.
Further reading
- "The PTB domain: a new protein module implicated in signal transduction.". Trends Biochem. Sci. 20 (7): 277–80. 1995. doi:10.1016/S0968-0004(00)89043-X. PMID 7545337.
- "NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor.". J. Biol. Chem. 265 (6): 3116–23. 1990. doi:10.1016/S0021-9258(19)39742-X. PMID 1968060.
- "The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein.". Mol. Cell. Biol. 16 (11): 6229–41. 1996. doi:10.1128/mcb.16.11.6229. PMID 8887653.
- "Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain.". EMBO J. 16 (20): 6141–50. 1997. doi:10.1093/emboj/16.20.6141. PMID 9321393.
- "Mints, Munc18-interacting proteins in synaptic vesicle exocytosis.". J. Biol. Chem. 272 (50): 31459–64. 1998. doi:10.1074/jbc.272.50.31459. PMID 9395480.
- "Mapping of the human and murine X11-like genes (APBA2 and apba2), the murine Fe65 gene (Apbb1), and the human Fe65-like gene (APBB2): genes encoding phosphotyrosine-binding domain proteins that interact with the Alzheimer's disease amyloid precursor protein.". Mamm. Genome 9 (6): 473–5. 1998. doi:10.1007/s003359900800. PMID 9585438.
- "The X11alpha protein slows cellular amyloid precursor protein processing and reduces Abeta40 and Abeta42 secretion.". J. Biol. Chem. 273 (24): 14761–6. 1998. doi:10.1074/jbc.273.24.14761. PMID 9614075.
- "A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain.". Cell 94 (6): 773–82. 1998. doi:10.1016/S0092-8674(00)81736-5. PMID 9753324.
- "Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting.". J. Biol. Chem. 273 (48): 31633–6. 1998. doi:10.1074/jbc.273.48.31633. PMID 9822620.
- "Molecular analysis of the X11-mLin-2/CASK complex in brain.". J. Neurosci. 19 (4): 1307–16. 1999. doi:10.1523/JNEUROSCI.19-04-01307.1999. PMID 9952408.
- "Association of neuronal calcium channels with modular adaptor proteins.". J. Biol. Chem. 274 (35): 24453–6. 1999. doi:10.1074/jbc.274.35.24453. PMID 10455105.
- "Modulation of amyloid precursor protein metabolism by X11alpha /Mint-1. A deletion analysis of protein-protein interaction domains.". J. Biol. Chem. 275 (50): 39302–6. 2001. doi:10.1074/jbc.M008453200. PMID 11010978.
- "Mints as adaptors. Direct binding to neurexins and recruitment of munc18.". J. Biol. Chem. 275 (51): 39803–6. 2001. doi:10.1074/jbc.C000656200. PMID 11036064.
- "X11 alpha and x11 beta interact with presenilin-1 via their PDZ domains.". Mol. Cell. Neurosci. 16 (5): 557–65. 2001. doi:10.1006/mcne.2000.0898. PMID 11083918.
- "The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity.". J. Biol. Chem. 276 (12): 9303–7. 2001. doi:10.1074/jbc.M010023200. PMID 11115513.
- "Synaptic multiprotein complexes associated with 5-HT(2C) receptors: a proteomic approach.". EMBO J. 21 (10): 2332–42. 2002. doi:10.1093/emboj/21.10.2332. PMID 12006486.
- "Synergistic effects of Munc18a and X11 proteins on amyloid precursor protein metabolism.". J. Biol. Chem. 277 (30): 27021–8. 2002. doi:10.1074/jbc.M201823200. PMID 12016213.
External links
- Human APBA1 genome location and APBA1 gene details page in the UCSC Genome Browser.
- Overview of all the structural information available in the PDB for UniProt: Q02410 (Amyloid-beta A4 precursor protein-binding family A member 1) at the PDBe-KB.
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