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BCR kinase phosphorylates 14‐3‐3 Tau on residue 233
Author(s) -
Clokie Samuel J.,
Cheung Kin Y.,
Mackie Shaun,
Marquez Rodolfo,
Peden Alex H.,
Aitken Alastair
Publication year - 2005
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2005.04765.x
Subject(s) - breakpoint cluster region , phosphorylation , casein kinase 2 , casein kinase 2, alpha 1 , threonine , serine , kinase , chemistry , map2k7 , tyrosine kinase , gene isoform , protein kinase a , biology , biochemistry , mitogen activated protein kinase kinase , signal transduction , cyclin dependent kinase 2 , receptor , gene
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.