Premium
An in vivo assay for the identification of target proteases which cleave membrane‐associated substrates
Author(s) -
Steiner Harald,
Pesold Brigitte,
Haass Christian
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01627-0
Subject(s) - proteases , cleave , protease , transmembrane protein , biochemistry , amyloid precursor protein , saccharomyces cerevisiae , biology , transmembrane domain , microbiology and biotechnology , chemistry , enzyme , gene , alzheimer's disease , medicine , receptor , disease , pathology
Proteases not only play a fundamental role in numerous physiological processes, but are also involved in several human diseases including Alzheimer's disease (AD). A key protease implicated in AD is the so far unidentified γ‐secretase, which cleaves the membrane‐bound β‐amyloid precursor protein (βAPP) at the C‐terminus of its amyloid domain within the membrane to release the neurotoxic amyloid β‐peptide. In order to allow the isolation of proteases, which specifically cleave membrane‐bound substrates within or in the vicinity of a transmembrane domain, we developed a reporter gene assay in Saccharomyces cerevisiae . This assay may allow the identification of genes encoding target proteases that specifically cleave membrane bound substrates by transforming expression libraries.