APP-BP1, a novel protein that binds to the carboxyl-terminal region of the amyloid precursor protein.
beta-Amyloid protein precursors (APPs, 695-770 amino acids) are the source of the 39-43 amino acid beta-amyloid (A beta) peptides that comprise diffuse and fibrillar deposits in the cerebral cortex and vasculature of Alzheimer's disease brains. A beta is thought to play a role in the pathogenesis of Alzheimer's disease, and, ... hence, considerable effort has been invested in defining the means by which A beta is generated from the APPs. Knowledge of the normal function of the APPs is sure to provide insights into the genesis and pathological persistence of A beta in Alzheimer's disease. APP is a cell surface protein with a large extracellular amino-terminal domain, a single transmembrane segment, and a short cytoplasmic tail. Its location and structural features characteristic of a receptor for signal transduction led us to search for potential effector proteins capable of binding and interacting with its cytoplasmic domain. Here, we report the cloning of a cDNA encoding one such protein. This ubiquitously expressed 59-kDa APP-binding protein, called APP-BP1, is 61% similar to a protein encoded by the Arabidopsis AXR1 gene, required for normal response to the hormone auxin, and is a relative of the ubiquitin activating enzyme E1.
Mesh Terms:
Adult, Alzheimer Disease, Amino Acid Sequence, Amyloid beta-Protein Precursor, Animals, Base Sequence, Binding Sites, Blotting, Northern, Brain, Cerebral Cortex, Chromosome Mapping, Chromosomes, Human, Pair 16, Cloning, Molecular, DNA Primers, DNA, Complementary, DNA-Binding Proteins, Fetus, Gene Library, Humans, In Situ Hybridization, Fluorescence, Mice, Molecular Sequence Data, Muscle, Skeletal, Organ Specificity, Polymerase Chain Reaction, Protein Binding, Recombinant Fusion Proteins, Sequence Homology, Amino Acid, Triticum
Adult, Alzheimer Disease, Amino Acid Sequence, Amyloid beta-Protein Precursor, Animals, Base Sequence, Binding Sites, Blotting, Northern, Brain, Cerebral Cortex, Chromosome Mapping, Chromosomes, Human, Pair 16, Cloning, Molecular, DNA Primers, DNA, Complementary, DNA-Binding Proteins, Fetus, Gene Library, Humans, In Situ Hybridization, Fluorescence, Mice, Molecular Sequence Data, Muscle, Skeletal, Organ Specificity, Polymerase Chain Reaction, Protein Binding, Recombinant Fusion Proteins, Sequence Homology, Amino Acid, Triticum
J. Biol. Chem.
Date: May. 10, 1996
PubMed ID: 8626687
View in: Pubmed Google Scholar
Download Curated Data For This Publication
471
Switch View:
- Interactions 2