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PMID:12354302
| Citation |
Li, J, Pauley, AM, Myers, RL, Shuang, R, Brashler, JR, Yan, R, Buhl, AE, Ruble, C and Gurney, ME (2002) SEL-10 interacts with presenilin 1, facilitates its ubiquitination, and alters A-beta peptide production. J. Neurochem. 82:1540-8 |
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| Abstract |
Mutations in the human presenilin genes (PS1 or PS2) have been linked to autosomal dominant, early onset Alzheimer's disease (AD). Presenilins, probably as an essential part of gamma-secretase, modulate gamma-cleavage of the amyloid protein precursor (APP) to the amyloid beta-peptide (Abeta). Mutations in sel-12, a Caenorhabditis elegans presenilin homologue, cause a defect in egg laying that can be suppressed by loss of function mutations in a second gene, SEL-10. SEL-10 protein is a homologue of yeast Cdc4, a member of the SCF (Skp1-Cdc53/CUL1-F-box protein) E2-E3 ubiquitin ligase family. In this study, we show that human SEL-10 interacts with PS1 and enhances PS1 ubiquitination, thus altering cellular levels of unprocessed PS1 and its N- and C-terminal fragments. Co-transfection of sel-10 and APP cDNAs in HEK293 cells leads to an alteration in the metabolism of APP and to an increase in the production of amyloid beta-peptide, the principal component of amyloid plaque in Alzheimer's disease. |
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| Keywords |
Amino Acid Sequence; Amyloid beta-Peptides/biosynthesis; Animals; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Cell Cycle Proteins/genetics; Cell Cycle Proteins/metabolism; Cell Cycle Proteins/pharmacology; Cell Line; Cloning, Molecular; DNA, Complementary/genetics; F-Box Proteins; Helminth Proteins/genetics; Helminth Proteins/metabolism; Helminth Proteins/pharmacology; Humans; Kidney/cytology; Kidney/metabolism; Membrane Proteins/metabolism; Mice; Molecular Sequence Data; Organ Specificity; Presenilin-1; Protein Binding/physiology; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Transfection; Ubiquitin/metabolism; Ubiquitin-Protein Ligases |
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Significance
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