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Gene Review

Apbb1  -  amyloid beta (A4) precursor protein...

Rattus norvegicus

Synonyms: Amyloid beta A4 precursor protein-binding family B member 1, Fe65, Protein Fe65
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Disease relevance of Apbb1


Psychiatry related information on Apbb1

  • A role for Fe65 in the pathogenesis of familial Alzheimer's disease is suggested by the finding that mutant APP, responsible for some cases of familial Alzheimer's disease, shows an altered in vivo interaction with Fe65 [2].

High impact information on Apbb1

  • No interaction was observed between Fe65 and the naturally occurring P2X(2) splice variant P2X(2(b)), indicating that alternative splicing can regulate the receptor complex assembly [3].
  • We confirmed the direct interaction of Fe65 and the P2X(2) C-terminal domain by glutathione S-transferase pull-down experiments [3].
  • Using a yeast two-hybrid approach with the P2X(2) subunit C-terminal domain as bait we isolated the beta-amyloid precursor protein-binding proteins Fe65 and Fe65-like 1 as the first identified proteins interacting with neuronal P2X receptors [3].
  • We found labeling for Fe65 at the pre- and postsynaptic specialization of CA1 hippocampal pyramidal cell/Schaffer collateral synapses [3].
  • Thus, the time- and activation-dependent change in ionic selectivity of P2X(2) receptors was inhibited by coexpression of Fe65, suggesting a novel role for Fe65 in regulating P2X receptor function and ATP-mediated synaptic transmission [3].

Biological context of Apbb1

  • Like Fe65, Fe65L1 and Fe65L2 genes encode two different protein isoforms, derived from the alternative splicing of a very small exon of only six nucleotides, which results, within the N-terminal PID/PTB domain, in the presence or absence of two acidic/basic amino acids [4].
  • Subsequently, phosphorylation of the APP cytoplasmic domain at threonine 668 appears to disrupt the stabilizing interaction with Fe65 and thus downregulate AICD-mediated signaling [5].

Anatomical context of Apbb1

  • Furthermore, the isolation of nuclei from untransfected PC12 cells allowed us to observe that a part of the endogenous Fe65 is present in the nuclear extract [6].

Associations of Apbb1 with chemical compounds


Other interactions of Apbb1

  • We previously demonstrated that Fe65 protein is one of the ligands of the cytoplasmic domain of beta-amyloid precursor protein (APP) [4].
  • Fe65L2: a new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's beta-amyloid precursor protein [4].
  • In recent, the C-terminal fragments of amyloid precursor protein (APP-CTs) have been reported to form a complex with Fe65 and the histone acetyltransferase Tip60 and are thought to be involved in gene transcription [9].

Analytical, diagnostic and therapeutic context of Apbb1

  • Furthermore, laser scanner microscopy and co-immunoprecipitation experiments provide preliminary evidence of possible complex(es) involving Tau, Fe65, APP [10].
  • We generated two antibodies to Fe65 to determine its subcellular localization using postembedding immunogold labeling electron microscopy [3].


  1. Probing the secondary structure of a recombinant neuronal adaptor protein and its phosphotyrosine binding domains. Lamberti, A., Longo, O., Del Vecchio, P., Zambrano, N., Barone, G., Russo, T., Arcari, P. Biosci. Biotechnol. Biochem. (2005) [Pubmed]
  2. Interaction of the phosphotyrosine interaction/phosphotyrosine binding-related domains of Fe65 with wild-type and mutant Alzheimer's beta-amyloid precursor proteins. Zambrano, N., Buxbaum, J.D., Minopoli, G., Fiore, F., De Candia, P., De Renzis, S., Faraonio, R., Sabo, S., Cheetham, J., Sudol, M., Russo, T. J. Biol. Chem. (1997) [Pubmed]
  3. Fe65 interacts with P2X2 subunits at excitatory synapses and modulates receptor function. Masin, M., Kerschensteiner, D., Dümke, K., Rubio, M.E., Soto, F. J. Biol. Chem. (2006) [Pubmed]
  4. Fe65L2: a new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's beta-amyloid precursor protein. Duilio, A., Faraonio, R., Minopoli, G., Zambrano, N., Russo, T. Biochem. J. (1998) [Pubmed]
  5. Physiological regulation of the beta-amyloid precursor protein signaling domain by c-Jun N-terminal kinase JNK3 during neuronal differentiation. Kimberly, W.T., Zheng, J.B., Town, T., Flavell, R.A., Selkoe, D.J. J. Neurosci. (2005) [Pubmed]
  6. The beta-amyloid precursor protein functions as a cytosolic anchoring site that prevents Fe65 nuclear translocation. Minopoli, G., de Candia, P., Bonetti, A., Faraonio, R., Zambrano, N., Russo, T. J. Biol. Chem. (2001) [Pubmed]
  7. The regions of the Fe65 protein homologous to the phosphotyrosine interaction/phosphotyrosine binding domain of Shc bind the intracellular domain of the Alzheimer's amyloid precursor protein. Fiore, F., Zambrano, N., Minopoli, G., Donini, V., Duilio, A., Russo, T. J. Biol. Chem. (1995) [Pubmed]
  8. A long acidic domain affects the chromatographic behaviour of a neuronal adaptor protein on DEAE-Sepharose. Longo, O., Lamberti, A., Zambrano, N., Arcari, P. Biosci. Biotechnol. Biochem. (2003) [Pubmed]
  9. Inhibition of histone deacetylation enhances the neurotoxicity induced by the C-terminal fragments of amyloid precursor protein. Kim, H.S., Kim, E.M., Kim, N.J., Chang, K.A., Choi, Y., Ahn, K.W., Lee, J.H., Kim, S., Park, C.H., Suh, Y.H. J. Neurosci. Res. (2004) [Pubmed]
  10. Interaction of Tau with Fe65 links tau to APP. Barbato, C., Canu, N., Zambrano, N., Serafino, A., Minopoli, G., Ciotti, M.T., Amadoro, G., Russo, T., Calissano, P. Neurobiol. Dis. (2005) [Pubmed]
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