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The kinase DYRK1A phosphorylates the transcription factor FKHR at Ser329 in vitro, a novel in vivo phosphorylation site

April 24, 2001

Synopsis:
Two papers from Woods and colleagues describe novel roles for members of the dual specificity tyrosine phosphorylated and regulated kinase (DYRK) family. In one, DYRK1A is shown to phosphorylate a novel site in the transcription factor FKHR (a forkhead protein) regulating its nuclear presence and transcriptional activity. In the second paper, it is shown that both DYRK1A and DYRK2 can phosphorylate sites on eIF2BE and Tau that are required for priming phosphorylation by GSK-3. These observations have implications not only with respect to mapping insulin, and related growth factor control pathways, but also in providing a basis for understanding genetics aberrations associated with the DYRK1A region of chromosome 21.

Published online: 24 April 2001

Published in Biochemical Journal: 1 May 2001

Information
 Biochemical Journal

The kinase DYRK1A phosphorylates the transcription factor FKHR at Ser329 in vitro, a novel in vivo phosphorylation site
Yvonne L. WOODS, Graham RENA, Nick MORRICE, Andreas BARTHEL, Walter BECKER, Shaodong GUO, Terry G. UNTERMAN and Philip COHEN
Vol. 355, part 3 (1 May 2001) pp 597-607

The kinase DYRK phosphorylates protein-synthesis initiation factor eIFB2Be at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase
Vol. 355, part 3 (1 May 2001) pp 609-615
Yvonne L. WOODS, Philip COHEN, Walter BECKER, Ross JAKES, Michel GOEDERT, Xuemin WANG and Christopher G. PROUD

http://www.biochemj.org

Full text of papers is available online to institutional subscribers. In case of difficulty contact support@portlandpress.com

Professor Sir Philp Cohen
MRC Protein Phosphorylation Unit
School of Life Sciences
University of Dundee
Dundee
DD1 5EH
E-mail: p.cohen@dundee.ac.uk

 Biochemical Journal Online
http://www.biochemistry.org

Scott Partnership Ltd, The

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