Presenilins interact with armadillo proteins including neural- specific plakophilin-related protein and β-catenin

G. Levesque; G. Yu; M. Nishimura; D. M. Zhang; L. Levesque; H. Yu; D. Xu; Y. Liang; E. Rogaeva; M. Ikeda; M. Duthie; N. Murgolo; L. Wang; P. VanderVere; M. L. Bayne; C. D. Strader; J. M. Rommens; P. E. Fraser; P. St. George-Hyslop

doi:10.1046/j.1471-4159.1999.0720999.x

Presenilins interact with armadillo proteins including neural- specific plakophilin-related protein and β-catenin

G. Levesque, G. Yu, M. Nishimura, D. M. Zhang, L. Levesque, H. Yu, D. Xu, Y. Liang, E. Rogaeva, M. Ikeda, M. Duthie, N. Murgolo, L. Wang, P. VanderVere, M. L. Bayne, C. D. Strader, J. M. Rommens, P. E. Fraser, P. St. George-Hyslop

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99 Scopus citations

Abstract

Missense substitutions in the presenilin 1 (PS1) and presenilin 2 (PS2) proteins are associated with early-onset familial Alzheimer's disease. We have used yeast-two-hybrid and coimmunoprecipitation methods to show that the large cytoplasmic loop domains of PS1 and PS2 interact specifically with three members of the armadillo protein family, including β-catenin, p0071, and a novel neuronal-specific armadillo protein-neural plakophilin-related armadillo protein (NPRAP). The PS1:NPRAP interaction occurs between the arm repeats of NPRAP and residues 372-399 at the C-terminal end of the large cytoplasmic loop of PS1. The latter residues contain a single arm-like domain and are highly conserved in the presenilins, suggesting that they form a functional armadillo protein binding site for the presenilins.

Original language	English (US)
Pages (from-to)	999-1008
Number of pages	10
Journal	Journal of Neurochemistry
Volume	72
Issue number	3
DOIs	https://doi.org/10.1046/j.1471-4159.1999.0720999.x
State	Published - 1999

Keywords

Alzheimer's disease
Armadillo proteins
Presenilin binding proteins
Presenilin proteins
Yeast-two-hybrid

ASJC Scopus subject areas

Biochemistry
Cellular and Molecular Neuroscience

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10.1046/j.1471-4159.1999.0720999.x

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Levesque, G., Yu, G., Nishimura, M., Zhang, D. M., Levesque, L., Yu, H., Xu, D., Liang, Y., Rogaeva, E., Ikeda, M., Duthie, M., Murgolo, N., Wang, L., VanderVere, P., Bayne, M. L., Strader, C. D., Rommens, J. M., Fraser, P. E., & St. George-Hyslop, P. (1999). Presenilins interact with armadillo proteins including neural- specific plakophilin-related protein and β-catenin. Journal of Neurochemistry, 72(3), 999-1008. https://doi.org/10.1046/j.1471-4159.1999.0720999.x

Levesque, G, Yu, G, Nishimura, M, Zhang, DM, Levesque, L, Yu, H, Xu, D, Liang, Y, Rogaeva, E, Ikeda, M, Duthie, M, Murgolo, N, Wang, L, VanderVere, P, Bayne, ML, Strader, CD, Rommens, JM, Fraser, PE & St. George-Hyslop, P 1999, 'Presenilins interact with armadillo proteins including neural- specific plakophilin-related protein and β-catenin', Journal of Neurochemistry, vol. 72, no. 3, pp. 999-1008. https://doi.org/10.1046/j.1471-4159.1999.0720999.x

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abstract = "Missense substitutions in the presenilin 1 (PS1) and presenilin 2 (PS2) proteins are associated with early-onset familial Alzheimer's disease. We have used yeast-two-hybrid and coimmunoprecipitation methods to show that the large cytoplasmic loop domains of PS1 and PS2 interact specifically with three members of the armadillo protein family, including β-catenin, p0071, and a novel neuronal-specific armadillo protein-neural plakophilin-related armadillo protein (NPRAP). The PS1:NPRAP interaction occurs between the arm repeats of NPRAP and residues 372-399 at the C-terminal end of the large cytoplasmic loop of PS1. The latter residues contain a single arm-like domain and are highly conserved in the presenilins, suggesting that they form a functional armadillo protein binding site for the presenilins.",

keywords = "Alzheimer's disease, Armadillo proteins, Presenilin binding proteins, Presenilin proteins, Yeast-two-hybrid",

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AU - Yu, G.

AU - Nishimura, M.

AU - Zhang, D. M.

AU - Levesque, L.

AU - Yu, H.

AU - Xu, D.

AU - Liang, Y.

AU - Rogaeva, E.

AU - Ikeda, M.

AU - Duthie, M.

AU - Murgolo, N.

AU - Wang, L.

AU - VanderVere, P.

AU - Bayne, M. L.

AU - Strader, C. D.

AU - Rommens, J. M.

AU - Fraser, P. E.

AU - St. George-Hyslop, P.

PY - 1999

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N2 - Missense substitutions in the presenilin 1 (PS1) and presenilin 2 (PS2) proteins are associated with early-onset familial Alzheimer's disease. We have used yeast-two-hybrid and coimmunoprecipitation methods to show that the large cytoplasmic loop domains of PS1 and PS2 interact specifically with three members of the armadillo protein family, including β-catenin, p0071, and a novel neuronal-specific armadillo protein-neural plakophilin-related armadillo protein (NPRAP). The PS1:NPRAP interaction occurs between the arm repeats of NPRAP and residues 372-399 at the C-terminal end of the large cytoplasmic loop of PS1. The latter residues contain a single arm-like domain and are highly conserved in the presenilins, suggesting that they form a functional armadillo protein binding site for the presenilins.

AB - Missense substitutions in the presenilin 1 (PS1) and presenilin 2 (PS2) proteins are associated with early-onset familial Alzheimer's disease. We have used yeast-two-hybrid and coimmunoprecipitation methods to show that the large cytoplasmic loop domains of PS1 and PS2 interact specifically with three members of the armadillo protein family, including β-catenin, p0071, and a novel neuronal-specific armadillo protein-neural plakophilin-related armadillo protein (NPRAP). The PS1:NPRAP interaction occurs between the arm repeats of NPRAP and residues 372-399 at the C-terminal end of the large cytoplasmic loop of PS1. The latter residues contain a single arm-like domain and are highly conserved in the presenilins, suggesting that they form a functional armadillo protein binding site for the presenilins.

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KW - Presenilin binding proteins

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Presenilins interact with armadillo proteins including neural- specific plakophilin-related protein and β-catenin

Abstract

Keywords

ASJC Scopus subject areas

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