Abstract:
:A functional assay for proteolytic processing of the amyloid precursor protein (APP) was set up in yeast. This consisted of a membrane-bound chimeric protein containing the beta-secretase cleaved C-terminal fragment of APP fused to the Ga14 transcription factor. Using this chimera in a GAL-reporter yeast strain, an expression library of human cDNAs was screened for clones that could activate the GAL-reporter genes by proteolytic processing of the membrane-bound APP-Gal4. Two human proteases, caspase-3 and caspase-8, were identified and confirmed to act by a mechanism that involved proteolysis at the site in the APP-Gal4 chimera that corresponded to the natural caspase cleavage site in APP, thus linking a readily scorable phenotype to proteolytic processing of APP. The activation of caspase-3 involved a mechanism that was independent of aspartic acid residue 175 at the cleavage site normally required for processing of caspase-3.
journal_name
Mol Biotechnoljournal_title
Molecular biotechnologyauthors
Gunyuzlu PL,White WH,Davis GL,Hollis GF,Toyn JHdoi
10.1385/MB:15:1:29keywords:
subject
Has Abstractpub_date
2000-05-01 00:00:00pages
29-37issue
1eissn
1073-6085issn
1559-0305pii
MB:15:1:29journal_volume
15pub_type
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