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dc.contributor.authorStordal, Britta
dc.contributor.authorDavey, Ross
dc.date.accessioned2009-11-11T03:55:14Z
dc.date.available2009-11-11T03:55:14Z
dc.date.issued2008-02-19
dc.identifier.citationStordal B, Davey R. A 39 kDa fragment of endogenous ASK1 suggests specific cleavage not degradation by the proteasome. IUBMB Life. 2008 Mar;60(3):180-4.en
dc.identifier.urihttp://hdl.handle.net/2123/5684
dc.description.abstractTransfected human ASK1 produces a 150kDa protein. However, we have detected endogenous ASK1 predominantly as 39kDa and 50kDa C-terminal and 75kDa and 110kDa N-terminal fragments in a panel of non-transfected cancer cell lines and HUVEC endothelial cells. This suggests that in non-apoptotic 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 39kDa C-terminal ASK1 fragment 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.en
dc.language.isoenen
dc.publisherTaylor & Francisen
dc.rightsThe University of Sydney claims copyright ownership of all information stored on this site, unless expressly stated otherwise.en
dc.subjectapoptosisen
dc.titleA 39 kDa fragment of endogenous ASK1 suggests specific cleavage not degradation by the proteasomeen
dc.typeArticleen
dc.contributor.departmentBill Walsh Cancer Research Laboratoriesen
dc.identifier.doihttp://dx.doi.org/10.1002/iub.24


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