APBA1

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Amyloid beta (A4) precursor protein-binding, family A, member 1 (X11)
PDB rendering based on 1aqc.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols APBA1 ; D9S411E; MINT1; X11; X11A; X11ALPHA
External IDs Template:OMIM5 Template:MGI HomoloGene: 897
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Amyloid beta (A4) precursor protein-binding, family A, member 1 (X11), also known as APBA1, is a human gene.[1]

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.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: APBA1 amyloid beta (A4) precursor protein-binding, family A, member 1 (X11)".

Further reading

  • van der Geer P, Pawson T (1995). "The PTB domain: a new protein module implicated in signal transduction". Trends Biochem. Sci. 20 (7): 277–80. PMID 7545337.
  • Chen WJ, Goldstein JL, Brown MS (1990). "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. PMID 1968060.
  • Duclos F, Boschert U, Sirugo G; et al. (1993). "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. PMID 7678331.
  • Duclos F, Koenig M (1995). "Comparison of primary structure of a neuron-specific protein, X11, between human and mouse". Mamm. Genome. 6 (1): 57–8. PMID 7719031.
  • Borg JP, Ooi J, Levy E, Margolis B (1996). "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. PMID 8887653.
  • Zhang Z, Lee CH, Mandiyan V; et al. (1997). "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. doi:10.1093/emboj/16.20.6141. PMID 9321393.
  • Okamoto M, Südhof TC (1998). "Mints, Munc18-interacting proteins in synaptic vesicle exocytosis". J. Biol. Chem. 272 (50): 31459–64. PMID 9395480.
  • Blanco G, Irving NG, Brown SD; et al. (1998). "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. PMID 9585438.
  • Borg JP, Yang Y, De Taddéo-Borg M; et al. (1998). "The X11alpha protein slows cellular amyloid precursor protein processing and reduces Abeta40 and Abeta42 secretion". J. Biol. Chem. 273 (24): 14761–6. PMID 9614075.
  • Butz S, Okamoto M, Südhof TC (1998). "A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain". Cell. 94 (6): 773–82. PMID 9753324.
  • Borg JP, Straight SW, Kaech SM; et al. (1998). "Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting". J. Biol. Chem. 273 (48): 31633–6. PMID 9822620.
  • Borg JP, Lõpez-Figueroa MO, de Taddèo-Borg M; et al. (1999). "Molecular analysis of the X11-mLin-2/CASK complex in brain". J. Neurosci. 19 (4): 1307–16. PMID 9952408.
  • Maximov A, Südhof TC, Bezprozvanny I (1999). "Association of neuronal calcium channels with modular adaptor proteins". J. Biol. Chem. 274 (35): 24453–6. PMID 10455105.
  • Mueller HT, Borg JP, Margolis B, Turner RS (2001). "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. doi:10.1074/jbc.M008453200. PMID 11010978.
  • Biederer T, Südhof TC (2001). "Mints as adaptors. Direct binding to neurexins and recruitment of munc18". J. Biol. Chem. 275 (51): 39803–6. doi:10.1074/jbc.C000656200. PMID 11036064.
  • Lau KF, McLoughlin DM, Standen C, Miller CC (2001). "X11 alpha and x11 beta interact with presenilin-1 via their PDZ domains". Mol. Cell. Neurosci. 16 (5): 557–65. doi:10.1006/mcne.2000.0898. PMID 11083918.
  • McLoughlin DM, Standen CL, Lau KF; et al. (2001). "The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity". J. Biol. Chem. 276 (12): 9303–7. doi:10.1074/jbc.M010023200. PMID 11115513.
  • Bécamel C, Alonso G, Galéotti N; et al. (2002). "Synaptic multiprotein complexes associated with 5-HT(2C) receptors: a proteomic approach". EMBO J. 21 (10): 2332–42. doi:10.1093/emboj/21.10.2332. PMID 12006486.
  • Ho CS, Marinescu V, Steinhilb ML; et al. (2002). "Synergistic effects of Munc18a and X11 proteins on amyloid precursor protein metabolism". J. Biol. Chem. 277 (30): 27021–8. doi:10.1074/jbc.M201823200. PMID 12016213.

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