Cell cycle-dependent caspase-like activity that cleaves p27KIP1 is the ß1 subunit of the 20S proteasome

Tambyrajah, Winston S., Bowler, Lucas D., Medina-Palazon, Cahora and Sinclair, Alison J. (2007) Cell cycle-dependent caspase-like activity that cleaves p27KIP1 is the ß1 subunit of the 20S proteasome. Archives of Biochemistry and Biophysics, 466 (2). pp. 186-193. ISSN 0003-9861

Full text not available from this repository.

Abstract

We 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.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Depositing User: Lucas Bowler
Date Deposited: 06 Feb 2012 20:59
Last Modified: 30 Mar 2012 14:28
URI: http://sro.sussex.ac.uk/id/eprint/28978
📧 Request an update