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Gene Review:

APBB2 - amyloid beta (A4) precursor protein...

Homo sapiens

Synonyms: Amyloid beta A4 precursor protein-binding family B member 2, FE65L, FE65L1, MGC35575, Protein Fe65-like 1

Cao, H. et al., Chang, Y. et al., Guénette, S.Y. et al., Guénette, S.Y. et al., Li, Y. et al., et al.

Guénette, Chang, Hyman, Tanzi, Rebeck,

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High impact information on APBB2

Association of a novel human FE65-like protein with the cytoplasmic domain of the beta-amyloid precursor protein [1].
APLP2, but not APLP1, was found to interact with hFE65L [1].
To understand the mechanism for the observed increase in both A beta and APPs alpha given that alpha-secretase cleavage of a single APP molecule precludes A beta generation, we examined the effects of FE65L1 overexpression on APP C-terminal fragments (APP CTFs) [2].
Furthermore, enhanced APP CTF processing can be detected in early endosome vesicles but not in endoplasmic reticulum or Golgi membranes, suggesting that the effects of FE65L1 occur at or near the plasma membrane [2].
Low-density lipoprotein receptor-related protein levels and endocytic function are reduced by overexpression of the FE65 adaptor protein, FE65L1 [3].

Biological context of APBB2

Characterization of an apoptosis inhibitory domain at the C-termini of FE65-like protein [4].
A prolonged exposure of L929 cells to these inhibitors for 24 h resulted in cell death, whereas FE65L significantly blocked the cell death [4].
When L929 cells were stably transfected with the FE65L cDNA or its 3' end TR2(L) DNA sequence, these cells became resistant to TNF killing [4].
Ablation of the C-terminal TR2(L) sequence through frame-shift mutation resulted in a complete loss of the FE65L function against TNF [4].
Here we report results of the first genetic association study with APBB2, an APP binding protein (also known as FE65L), and LOAD, in three independently collected case-control series totaling approximately 2,000 samples [5].

Associations of APBB2 with chemical compounds

We show here that binding of APP to the C-terminal phosphotyrosine interaction domain of hFE65L requires an intact YENPTY clathrin-coated pit internalization sequence [6].
Various protein kinase inhibitors, including lavendustin A, tyrphostin, H7, and staurosporine, which may affect the PTB domain function, could not abolish the FE65L-mediated TNF resistance [4].

Regulatory relationships of APBB2

hFE65L influences amyloid precursor protein maturation and secretion [6].

Other interactions of APBB2

These data show that FE65L1 can differentially affect the metabolic fate of APP and LRP [3].
Replacement of the N-terminal PTB domain with GFP failed to abolish the FE65L-mediated TNF resistance [4].

References

Association of a novel human FE65-like protein with the cytoplasmic domain of the beta-amyloid precursor protein. Guénette, S.Y., Chen, J., Jondro, P.D., Tanzi, R.E. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
Generation of the beta-amyloid peptide and the amyloid precursor protein C-terminal fragment gamma are potentiated by FE65L1. Chang, Y., Tesco, G., Jeong, W.J., Lindsley, L., Eckman, E.A., Eckman, C.B., Tanzi, R.E., Guénette, S.Y. J. Biol. Chem. (2003) [Pubmed]
Low-density lipoprotein receptor-related protein levels and endocytic function are reduced by overexpression of the FE65 adaptor protein, FE65L1. Guénette, S.Y., Chang, Y., Hyman, B.T., Tanzi, R.E., Rebeck, G.W. J. Neurochem. (2002) [Pubmed]
Characterization of an apoptosis inhibitory domain at the C-termini of FE65-like protein. Cao, H., Pratt, N., Mattison, J., Zhao, Y., Chang, N.S. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
Genetic association of the APP binding protein 2 gene (APBB2) with late onset Alzheimer disease. Li, Y., Hollingworth, P., Moore, P., Foy, C., Archer, N., Powell, J., Nowotny, P., Holmans, P., O'Donovan, M., Tacey, K., Doil, L., van Luchene, R., Garcia, V., Rowland, C., Lau, K., Cantanese, J., Sninsky, J., Hardy, J., Thal, L., Morris, J.C., Goate, A., Lovestone, S., Owen, M., Williams, J., Grupe, A. Hum. Mutat. (2005) [Pubmed]
hFE65L influences amyloid precursor protein maturation and secretion. Guénette, S.Y., Chen, J., Ferland, A., Haass, C., Capell, A., Tanzi, R.E. J. Neurochem. (1999) [Pubmed]

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