APBA2

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Amyloid beta (A4) precursor protein-binding, family A, member 2 (X11-like)
PDB rendering based on 1u39.
Available structures: 1u39, 1y7n
Identifiers
Symbol(s) APBA2; D15S1518E; HsT16821; LIN-10; MGC99508; MGC:14091; MINT2; X11L
External IDs OMIM: 602712 MGI: 1261791 HomoloGene: 4021
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 321 11784
Ensembl ENSG00000034053 ENSMUSG00000030519
Uniprot Q99767 Q9Z316
Refseq NM_005503 (mRNA)
NP_005494 (protein)		 NM_007461 (mRNA)
NP_031487 (protein)
Location Chr 15: 27 - 27.2 Mb Chr 7: 64.38 - 64.63 Mb
Pubmed search [1] [2]

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]

[edit] References

  1. ^ a b Entrez Gene: APBA2 amyloid beta (A4) precursor protein-binding, family A, member 2 (X11-like).

[edit] 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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