Beta-amyloid protein converting enzyme 1 and brain-specific type II membrane protein BRI3: binding partners processed by furin.
Using a yeast two-hybrid system, we screened a human brain cDNA library for possible interacting proteins with the C-terminal cytosolic tail of the beta-secretase beta-amyloid protein converting enzyme (BACE)1. This identified seven potential candidates, including the brain-specific type II membrane protein BRI3. Co-localization and co-immunoprecipitation experiments confirmed that BACE1 and ... BRI3 co-localize and interact with each other via the cytosolic tail of BACE1. Furthermore, pulse and pulse-chase analyses revealed that the pro-protein convertases furin, and to a lesser extent PC7 and PC5A, process BRI3 into a C-terminal secreted approximately 4-kDa product. Thus, furin efficiently processes both pro-BACE1 and its novel interacting protein pro-BRI3.
Mesh Terms:
Amino Acid Sequence, Amyloid Precursor Protein Secretases, Amyloid beta-Peptides, Animals, Aspartic Acid Endopeptidases, Brain, Cell Line, Endopeptidases, Furin, Humans, Membrane Proteins, Mice, Mice, Transgenic, Molecular Sequence Data, Nerve Tissue Proteins, Protein Binding, Protein Interaction Mapping, Protein Processing, Post-Translational, Transfection
Amino Acid Sequence, Amyloid Precursor Protein Secretases, Amyloid beta-Peptides, Animals, Aspartic Acid Endopeptidases, Brain, Cell Line, Endopeptidases, Furin, Humans, Membrane Proteins, Mice, Mice, Transgenic, Molecular Sequence Data, Nerve Tissue Proteins, Protein Binding, Protein Interaction Mapping, Protein Processing, Post-Translational, Transfection
J. Neurochem.
Date: Jan. 01, 2005
PubMed ID: 15606899
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