A 39 kDa fragment of endogenous ASK1 suggests specific cleavage not degradation by the proteasome

Stordal, Britta K. ORCID logoORCID: https://orcid.org/0000-0002-7892-951X and Davey, Ross (2008) A 39 kDa fragment of endogenous ASK1 suggests specific cleavage not degradation by the proteasome. IUBMB Life, 60 (3) . pp. 180-184. ISSN 1521-6543 [Article] (doi:10.1002/iub.24)

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Transfected human apoptosis signal-regulating kinase 1 (ASK1) produces a 150 kDa protein. However, we have detected endogenous ASK1 predominantly as 39 and 50 kDa C-terminal and 75 and 110 kDa N-terminal fragments in a panel of nontransfected cancer cell lines and HUVEC endothelial cells. This suggests that in nonapoptotic cells, endogenous ASK1 protein is normally cleaved at a number of specific sites, some of which are in the kinase domain. Transfected ASK1 protein is known to be degraded by the proteasome. In contrast, the cleavage of endogenous ASK1 is independent of the proteasome as treatment with the proteasome inhibitor, lactacystin did not inhibit cleavage. Cisplatin treatment decreased the amount of 39 kDa C-terminal ASK1 fragments in mutant p53 cell lines suggesting a decrease in cleavage associated with apoptosis. Transfected ASK1 may, therefore, not accurately reflect the role of endogenous ASK1.

Item Type: Article
Research Areas: A. > School of Science and Technology > Natural Sciences > Biomarkers for Cancer group
Item ID: 14438
Depositing User: Dr Britta Stordal
Date Deposited: 19 Mar 2015 10:04
Last Modified: 07 Jun 2022 05:04
URI: https://eprints.mdx.ac.uk/id/eprint/14438

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