BCR kinase phosphorylates 14-3-3 Tau on residue 233

Clokie, S. J., Cheung, K. Y., Mackie, S., Marquez, R., Peden, A. H. and Aitken, A. (2005) BCR kinase phosphorylates 14-3-3 Tau on residue 233. FEBS Journal, 272(15), pp. 3767-3776. (doi: 10.1111/j.1742-4658.2005.04765.x)

Abstract

The breakpoint cluster region protein, BCR, has protein kinase activity that can auto- and trans-phosphorylate serine, threonine and tyrosine residues. BCR has been implicated in chronic myelogenous leukaemia as well as important signalling pathways, and as such its interaction with 14-3-3 is of major interest. 14-3-3τ and ζ isoforms have been shown previously to be phosphorylated in vitro and in vivo by BCR kinase on serine and threonine residue(s) but site(s) were not determined. Phosphorylation of 14-3-3 isoforms at distinct sites is an important mode of regulation that negatively affects interaction with Raf kinase and Bax, and potentially influences the dimerization of 14-3-3. In this study we have further characterized the BCR−14-3-3 interaction and have identified the site phosphorylated by BCR. We show here that BCR interacts with at least five isoforms of 14-3-3 in vivo and phosphorylates 14-3-3τ on Ser233 and to a lesser extent 14-3-3ζ on Thr233. We have previously shown that these two isoforms are also phosphorylated at this site by casein kinase 1, which, in contrast to BCR, preferentially phosphorylates 14-3-3ζ.

• Item Type: Articles
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Marquez, Dr Rudi
• Authors: Clokie, S. J., Cheung, K. Y., Mackie, S., Marquez, R., Peden, A. H., and Aitken, A.
• College/School: College of Science and Engineering > School of Chemistry
• Journal Name: FEBS Journal
• Publisher: Wiley-Blackwell Publishing Ltd.
• ISSN: 1742-464X
• ISSN (Online): 1742-4658
• Published Online: 07 July 2005