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Gene Review

APBA2  -  amyloid beta (A4) precursor protein...

Homo sapiens

Synonyms: Adapter protein X11beta, Amyloid beta A4 precursor protein-binding family A member 2, D15S1518E, HsT16821, LIN-10, ...
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Disease relevance of APBA2


Psychiatry related information on APBA2

  • Because expression of the human X11L gene is specific to brain, the present observations should contribute to shedding light on the molecular mechanism of APP processing in Alzheimer's disease [4].

High impact information on APBA2

  • Methylation of p16 and hMLH1 promoters was determined by methylation-specific polymerase chain reaction (PCR), whereas methylation at methylated-in-tumor loci (MINT)1, MINT2, MINT12, and MINT31 loci were assessed by bisulfite-PCR [5].
  • RNAi silencing of APBA2 also lowered Abeta levels, but apparently not via attenuation of gamma-secretase cleavage of APP [6].
  • Together, our data suggest that LIN-10 uses distinct modular domains for its functions in neurons and epithelial cells and that during evolution its vertebrate ortholog Mint2 has retained the ability to direct AMPAR localization in neurons [7].
  • X11L stabilizes APP metabolism and suppresses the secretion of the amyloid beta-protein (Abeta) that are the pathogenic agents of Alzheimer's disease (AD) [8].
  • The mammalian homologue, mLin-7, forms a ternary complex with the mammalian homologues of LIN-2 and LIN-10 and localizes at cell-cell junctions in epithelial cells, but the mechanism of this localization of mLin-7 is unknown [9].

Biological context of APBA2

  • Partial duplication of the APBA2 gene in chromosome 15q13 corresponds to duplicon structures [10].
  • The duplicated copies, containing the first coding exon of APBA2, can be distinguished by single nucleotide sequence differences and are transcriptionally inactive [10].
  • The gene encoding an amyloid precursor protein-binding protein (APBA2) was previously mapped to the distal portion of the interval commonly deleted in Prader-Willi and Angelman syndromes and duplicated in cases of autism [10].
  • Overexpression of hX11L and the PDZ domain of dX11L resulted in identical eye phenotypes [11].
  • Our findings suggest that the X11L family may be involved with the regulation of apoptosis during neural cell development and that aberrant X11L function could be contribute in this way to the neuronal degeneration observed in Alzheimer's disease [11].

Anatomical context of APBA2


Associations of APBA2 with chemical compounds

  • LIN-7 is known to play an essential role in the basolateral localization of the LET-23 tyrosine kinase receptor, by linking the receptor to LIN-2 and LIN-10 proteins [14].

Regulatory relationships of APBA2

  • X11L is a neuron-specific adaptor protein that is known to down-regulate APP (beta-amyloid precursor protein) metabolism by associating with the cytoplasmic domain of APP, but the detailed mechanisms are still unknown [15].

Other interactions of APBA2


  1. Frequent CpG island methylation in serrated adenomas of the colorectum. Park, S.J., Rashid, A., Lee, J.H., Kim, S.G., Hamilton, S.R., Wu, T.T. Am. J. Pathol. (2003) [Pubmed]
  2. Hypermethylation of multiple genes in pancreatic adenocarcinoma. Ueki, T., Toyota, M., Sohn, T., Yeo, C.J., Issa, J.P., Hruban, R.H., Goggins, M. Cancer Res. (2000) [Pubmed]
  3. CpG island methylation in colorectal adenomas. Rashid, A., Shen, L., Morris, J.S., Issa, J.P., Hamilton, S.R. Am. J. Pathol. (2001) [Pubmed]
  4. Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein. Tomita, S., Ozaki, T., Taru, H., Oguchi, S., Takeda, S., Yagi, Y., Sakiyama, S., Kirino, Y., Suzuki, T. J. Biol. Chem. (1999) [Pubmed]
  5. Adverse prognostic effect of methylation in colorectal cancer is reversed by microsatellite instability. Ward, R.L., Cheong, K., Ku, S.L., Meagher, A., O'Connor, T., Hawkins, N.J. J. Clin. Oncol. (2003) [Pubmed]
  6. RNA interference-mediated silencing of X11alpha and X11beta attenuates amyloid beta-protein levels via differential effects on beta-amyloid precursor protein processing. Xie, Z., Romano, D.M., Tanzi, R.E. J. Biol. Chem. (2005) [Pubmed]
  7. Distinct LIN-10 domains are required for its neuronal function, its epithelial function, and its synaptic localization. Glodowski, D.R., Wright, T., Martinowich, K., Chang, H.C., Beach, D., Rongo, C. Mol. Biol. Cell (2005) [Pubmed]
  8. Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta-protein precursor metabolism. Araki, Y., Tomita, S., Yamaguchi, H., Miyagi, N., Sumioka, A., Kirino, Y., Suzuki, T. J. Biol. Chem. (2003) [Pubmed]
  9. Localization of mLin-7 at nectin-based cell-cell junctions. Yamamoto, Y., Mandai, K., Okabe, N., Hoshino, T., Nakanishi, H., Takai, Y. Oncogene (2002) [Pubmed]
  10. Partial duplication of the APBA2 gene in chromosome 15q13 corresponds to duplicon structures. Sutcliffe, J.S., Han, M.K., Amin, T., Kesterson, R.A., Nurmi, E.L. BMC Genomics (2003) [Pubmed]
  11. Expression and characterization of the Drosophila X11-like/Mint protein during neural development. Hase, M., Yagi, Y., Taru, H., Tomita, S., Sumioka, A., Hori, K., Miyamoto, K., Sasamura, T., Nakamura, M., Matsuno, K., Suzuki, T. J. Neurochem. (2002) [Pubmed]
  12. Mint2/X11-like colocalizes with the Alzheimer's disease amyloid precursor protein and is associated with neuritic plaques in Alzheimer's disease. McLoughlin, D.M., Irving, N.G., Brownlees, J., Brion, J.P., Leroy, K., Miller, C.C. Eur. J. Neurosci. (1999) [Pubmed]
  13. Amyloid precursor protein associates independently and collaboratively with PTB and PDZ domains of mint on vesicles and at cell membrane. Okamoto, M., Nakajima, Y., Matsuyama, T., Sugita, M. Neuroscience (2001) [Pubmed]
  14. VAM-1: a new member of the MAGUK family binds to human Veli-1 through a conserved domain. Tseng, T.C., Marfatia, S.M., Bryant, P.J., Pack, S., Zhuang, Z., O'Brien, J.E., Lin, L., Hanada, T., Chishti, A.H. Biochim. Biophys. Acta (2001) [Pubmed]
  15. XB51 isoforms mediate Alzheimer's beta-amyloid peptide production by X11L (X11-like protein)-dependent and -independent mechanisms. Sumioka, A., Imoto, S., Martins, R.N., Kirino, Y., Suzuki, T. Biochem. J. (2003) [Pubmed]
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