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Presenilins interact with armadillo proteins including neural-specific plakophilin-related protein and beta-catenin |
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| Authors: | 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 |
| Institution: | Centre for Research in Neurodegenerative Diseases, Departments of Medicine (Neurology), Medical Biophysics, Pathology, and Medical and Molecular Genetics, University of Toronto, Toronto, Ontario, Canada; Department of Medicine (Division of Neurology), Toronto Hospital, Toronto, Ontario, Canada; Research Institute, Hospital for Sick Children, Toronto, Ontario, Canada; Departments of CNS/Cardiovascular Research and Human Genomic Research, Schering-Plough Research Institute, Kenilworth, New Jersey, U.S.A. |
| Abstract: | 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: | Presenilin proteins Presenilin binding proteins Armadillo proteins Yeast-two-hybrid Alzheimer's disease |
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