The fully linked HTML version of this article has now been published.
JCS ePress
online publication date 10 Jun 2003
doi: 10.1242/jcs.00618
Research Article
DYRK1A accumulates in splicing speckles through a novel targeting signal and induces speckle disassembly
Mónica Álvarez,
Xavier Estivill,
and
Susana de la Luna*
* Author for correspondence (e-mail: susana.luna{at}crg.es)
The protein kinase DYRK1A is distributed throughout the nucleoplasm, accumulating in speckle-like regions. We have found that this punctuated nuclear distribution is determined by the contribution of several elements. Although the nuclear import is mediated by two distinct nuclear localization signals, one at the N-terminus and the other located in the linker region, between subdomains X and XI of the catalytic domain, the accumulation in speckles that are SC35 positive depends on a sequence motif that is located C-terminal to the kinase domain and comprises a histidine tail. A similar sequence is also responsible for the targeting of cyclin T1. Therefore the histidine-rich region represents a novel splicing speckle targeting signal. Moreover, overexpression of DYRK1A induces speckle disassembly. Such disassembly is DYRK1A activity specific, since the overexpression of a DYRK1A kinase inactive mutant, the paralogous DYRK1B or a chimeric protein DYRK1B that has been directed to the speckles via the DYRK1A targeting signal, leaves the SC35 speckle pattern untouched. Thus DYRK1A protein kinase may play a role in regulating the biogenesis of the splicing speckle compartment.
This article has been cited by other articles:
|
|
|
|
 
J. Shi, T. Zhang, C. Zhou, M. O. Chohan, X. Gu, J. Wegiel, J. Zhou, Y.-W. Hwang, K. Iqbal, I. Grundke-Iqbal, et al.
Increased Dosage of Dyrk1A Alters Alternative Splicing Factor (ASF)-regulated Alternative Splicing of Tau in Down Syndrome
J. Biol. Chem.,
October 17, 2008;
283(42):
28660 - 28669.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
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]
|
|
|
|
|
|
|
J.-i. Yomoda, M. Muraki, N. Kataoka, T. Hosoya, M. Suzuki, M. Hagiwara, and H. Kimura
Combination of Clk family kinase and SRp75 modulates alternative splicing of Adenovirus E1A.
Genes Cells,
March 1, 2008;
13(3):
233 - 244.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
E. G. Cline and W. J. Nelson
Characterization of Mammalian Par 6 as a Dual-Location Protein
Mol. Cell. Biol.,
June 15, 2007;
27(12):
4431 - 4443.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
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]
|
|
|
|
|
|
|
Z. Fu, M. J. Schroeder, J. Shabanowitz, P. Kaldis, K. Togawa, A. K. Rustgi, D. F. Hunt, and T. W. Sturgill
Activation of a Nuclear Cdc2-Related Kinase within a Mitogen-Activated Protein Kinase-Like TDY Motif by Autophosphorylation and Cyclin-Dependent Protein Kinase-Activating Kinase
Mol. Cell. Biol.,
July 15, 2005;
25(14):
6047 - 6064.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J. H. Sitz, M. Tigges, K. Baumgartel, L. G. Khaspekov, and B. Lutz
Dyrk1A Potentiates Steroid Hormone-Induced Transcription via the Chromatin Remodeling Factor Arip4
Mol. Cell. Biol.,
July 1, 2004;
24(13):
5821 - 5834.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. de Graaf, P. Hekerman, O. Spelten, A. Herrmann, L. C. Packman, K. Bussow, G. Muller-Newen, and W. Becker
Characterization of Cyclin L2, a Novel Cyclin with an Arginine/Serine-rich Domain: PHOSPHORYLATION BY DYRK1A AND COLOCALIZATION WITH SPLICING FACTORS
J. Biol. Chem.,
February 6, 2004;
279(6):
4612 - 4624.
[Abstract]
[Full Text]
[PDF]
|
|
|
© The Company of Biologists Ltd 2003
