APBA2

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Amyloid beta (A4) precursor protein-binding, family A, member 2 (X11-like)
PDB rendering based on 1u39.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols APBA2 ; D15S1518E; HsT16821; LIN-10; MGC99508; MGC:14091; MINT2; X11L
External IDs Template:OMIM5 Template:MGI HomoloGene: 4021
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 2 (X11-like), also known as APBA2, 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: APBA2 amyloid beta (A4) precursor protein-binding, family A, member 2 (X11-like)".

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.
  • Andersson B, Wentland MA, Ricafrente JY; et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  • McLoughlin DM, Miller CC (1997). "The intracellular cytoplasmic domain of the Alzheimer's disease amyloid precursor protein interacts with phosphotyrosine-binding domain proteins in the yeast two-hybrid system". FEBS Lett. 397 (2–3): 197–200. PMID 8955346.
  • Yu W, Andersson B, Worley KC; et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. PMID 9110174.
  • 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.
  • 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.
  • Okamoto M, Südhof TC (1999). "Mint 3: a ubiquitous mint isoform that does not bind to munc18-1 or -2". Eur. J. Cell Biol. 77 (3): 161–5. PMID 9860131.
  • Tomita S, Ozaki T, Taru H; et al. (1999). "Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein". J. Biol. Chem. 274 (4): 2243–54. PMID 9890987.
  • McLoughlin DM, Irving NG, Brownlees J; et al. (1999). "Mint2/X11-like colocalizes with the Alzheimer's disease amyloid precursor protein and is associated with neuritic plaques in Alzheimer's disease". Eur. J. Neurosci. 11 (6): 1988–94. PMID 10336668.
  • Tomita S, Fujita T, Kirino Y, Suzuki T (2000). "PDZ domain-dependent suppression of NF-kappaB/p65-induced Abeta42 production by a neuron-specific X11-like protein". J. Biol. Chem. 275 (17): 13056–60. PMID 10777610.
  • Gotthardt M, Trommsdorff M, Nevitt MF; et al. (2000). "Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction". J. Biol. Chem. 275 (33): 25616–24. doi:10.1074/jbc.M000955200. PMID 10827173.
  • Lee DS, Tomita S, Kirino Y, Suzuki T (2000). "Regulation of X11L-dependent amyloid precursor protein metabolism by XB51, a novel X11L-binding protein". J. Biol. Chem. 275 (30): 23134–8. doi:10.1074/jbc.C000302200. PMID 10833507.
  • 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.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Sutcliffe JS, Han MK, Amin T; et al. (2003). "Partial duplication of the APBA2 gene in chromosome 15q13 corresponds to duplicon structures". BMC Genomics. 4 (1): 15. doi:10.1186/1471-2164-4-15. PMID 12720574.
  • Sumioka A, Imoto S, Martins RN; et al. (2003). "XB51 isoforms mediate Alzheimer's beta-amyloid peptide production by X11L (X11-like protein)-dependent and -independent mechanisms". Biochem. J. 374 (Pt 1): 261–8. doi:10.1042/BJ20030489. PMID 12780348.

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