TAILIEUCHUNG - Báo cáo khoa học: BCR kinase phosphorylates 14-3-3 Tau on residue 233

The breakpoint cluster region protein, BCR, has protein kinase activity that can auto- and trans-phosphorylate serine, threonine and tyrosine resi-dues. 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. 14-3-3sandfisoforms have been shown previously to be phosphorylatedin vitro andin vivo by BCR kinase on serine and threonine residue(s) but site(s) were not determined. | ềFEBS Journal BCR kinase phosphorylates 14-3-3 Tau on residue 233 Samuel J. Clokie1 Kin Y. Cheung1 Shaun Mackie1 Rodolfo Marquez2 Alex H. Peden1 t and Alastair Aitken1 1 Schoolof Biomedicaland ClinicalLaboratory Sciences University of Edinburgh UK 2 Schoolof Life Sciences University of Dundee UK Keywords 14-3-3 isoforms phosphorylation BCR kinase protein interactions Correspondence A. Aitken Schoolof Biomedicaland Clinical Laboratory Sciences Darwin Building University of Edinburgh King s Buildings Mayfield Road Edinburgh EH8 9XD UK Fax Tel 44 131 650 5357 E-mail Present addresses Psychiatric Genetics Section Molecular Medicine Centre University of Edinburgh UK tThe NationalCreutzfeldt-Jakob Disease Surveillance Unit Western General Hospital Edinburgh UK 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. 14-3-3s and f 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 14-3-3s on Ser233 and to a lesser extent 14-3-3f 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 14-3-3f. Received 21 February 2005 revised 4 May 2005 accepted 13 May 2005 doi .

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