Molecular Biology of the Cell track citations

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print May 25, 2005
Mol. Biol. Cell 10.1091/mbc.E04-12-1085

A more recent version of this article appeared on August 1, 2005
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E04-12-1085v1
16/8/3562    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kelly, P. A.
Right arrow Articles by Rahmani, Z.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kelly, P. A.
Right arrow Articles by Rahmani, Z.

Submitted on December 16, 2004
Revised on April 25, 2005
Accepted on May 13, 2005

DYRK1A Enhances the Mitogen-activated Protein Kinase Cascade in PC12 Cells by Forming a Complex with Ras, B-Raf, and MEK1

Paul A. Kelly and Zohra Rahmani*

INSERM U584, Faculté de Médecine Necker-Enfants Malades, 75730 Paris Cedex 15, France

Monitoring Editor: Gerard Evan

Dyrk1A (dual-specificity tyrosine-phosphorylated and regulated kinase 1A) is the human homologue of the Drosophila mnb (minibrain) gene. In Drosophila, mnb is involved in postembryonic neurogenesis. In human, DYRK1A maps within the Down syndrome critical region of chromosome 21 and is overexpressed in Down syndrome embryonic brain. Despite its potential involvement in the neurobiological alterations observed in Down syndrome patients, the biological functions of the serine/threonine kinase DYRK1A have not been identified yet. Here, we report that DYRK1A overexpression potentiates NGF-mediated PC12 neuronal differentiation by upregulating the Ras/MAP kinase signaling pathway independently of its kinase activity. Furthermore, we show that DYRK1A prolongs the kinetics of ERK activation by interacting with Ras, B-Raf, and MEK1 to facilitate the formation of a Ras/B-Raf/MEK1 multiprotein complex. These data indicate that DYRK1A may play a critical role in Ras-dependent transducing signals that are required for promoting or maintaining neuronal differentiation and suggest that overexpression of DYRK1A may contribute to the neurological abnormalities observed in Down syndrome patients.

*Present address: CNRS UMR 8542, Ecole Normale Supérieure, 46 Rue d’Ulm, 75230 Paris Cedex 05, France.

Address correspondence to: Zohra Rahmani (rahmani{at}biologie.ens.fr)




This article has been cited by other articles:


Home page
 Mol. Cell. Biol.Home page
S. Aranda, M. Alvarez, S. Turro, A. Laguna, and S. de la Luna
Sprouty2-Mediated Inhibition of Fibroblast Growth Factor Signaling Is Modulated by the Protein Kinase DYRK1A
Mol. Cell. Biol., October 1, 2008; 28(19): 5899 - 5911.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
M. Alvarez, X. Altafaj, S. Aranda, and S. de la Luna
DYRK1A Autophosphorylation on Serine Residue 520 Modulates Its Kinase Activity via 14-3-3 Binding
Mol. Biol. Cell, April 1, 2007; 18(4): 1167 - 1178.
[Abstract] [Full Text] [PDF]

Home page
 BioinformaticsHome page
M. Pellegrini-Calace and A. Tramontano
Identification of a novel putative mitogen-activated kinase cascade on human chromosome 21 by computational approaches
Bioinformatics, April 1, 2006; 22(7): 775 - 778.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2005 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.