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Cell cycle-dependent caspase-like activity that cleaves p27KIP1 is the ß1 subunit of the 20S proteasome
journal contribution
posted on 2023-06-08, 08:25 authored by Winston S. Tambyrajah, Lucas D. Bowler, Cahora Medina-Palazon, Alison SinclairWe previously described a caspase-like activity, which we termed KIPase that is implicated in the turnover of the mammalian cell cycle regulator p27KIP1. KIPase cleaves a tetra-peptide substrate, Ac-DPSD-AMC, which mimics the target site in p27KIP1, and inhibitors based on this tetra-peptide are ineffective against other known caspases. Here we describe the purification and characterization of KIPase, and trace its activity to the 1 subunit of the 20S proteasome. Further analyses revealed that the activity of the 1 subunit is up-regulated as cells enter the cell cycle without concomitant change in the levels of the proteasome 1, 2 or 5 subunits. To our knowledge, this is the first description of cell cycle regulation of the caspase-like activity of the 20S proteasome.
History
Publication status
- Published
Journal
Archives of Biochemistry and BiophysicsISSN
0003-9861Publisher
ElsevierExternal DOI
Issue
2Volume
466Page range
186-193Pages
8.0Department affiliated with
- Biochemistry Publications
Full text available
- No
Peer reviewed?
- Yes
Legacy Posted Date
2012-02-06Usage metrics
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