This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Myers, A. P.
Right arrow Articles by Baker, J. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Myers, A. P.
Right arrow Articles by Baker, J. C.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, May 2004, p. 4255-4266, Vol. 24, No. 10
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.10.4255-4266.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Characterization of Mouse Rsk4 as an Inhibitor of Fibroblast Growth Factor-RAS-Extracellular Signal-Regulated Kinase Signaling

Andrea Pomrehn Myers,1 Laura B. Corson,2 Janet Rossant,2,3 and Julie C. Baker1*

Department of Genetics, Stanford Medical School, Stanford, California,1 Samuel Lunenfeld Research Institute, Mount Sinai Hospital,2 Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario, Canada3

Received 28 October 2003/ Returned for modification 5 December 2003/ Accepted 2 February 2004

Receptor tyrosine kinase (RTK) signals regulate the specification of a varied array of tissue types by utilizing distinct modules of proteins to elicit diverse effects. The RSK proteins are part of the RTK signal transduction pathway and are thought to relay these signals by acting downstream of extracellular signal-regulated kinase (ERK). In this study we report the identification of ribosomal S6 kinase 4 (Rsk4) as an inhibitor of RTK signals. Among the RSK proteins, RTK inhibition is specific to RSK4 and, in accordance, is dependent upon a region of the RSK4 protein that is divergent from other RSK family members. We demonstrate that Rsk4 inhibits the transcriptional activation of specific targets of RTK signaling as well as the activation of ERK. Developmentally, Rsk4 is expressed in extraembryonic tissue, where RTK signals are known to have critical roles. Further examination of Rsk4 expression in the extraembryonic tissues demonstrates that its expression is inversely correlated with the presence of activated ERK 1/2. These studies demonstrate a new and divergent function for RSK4 and support a role for RSK proteins in the specification of RTK signals during early mouse development.

* Corresponding author. Mailing address: Stanford University, Genetics Department, Alway Room 337, 300 Pasteur Dr., Stanford, CA 94305. Phone: (650) 723-1082. Fax: (650) 725-1534. E-mail: jbaker{at}stanford.edu.

Molecular and Cellular Biology, May 2004, p. 4255-4266, Vol. 24, No. 10
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.10.4255-4266.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Gao, X., Patel, T. B. (2009). Regulation of Protein Kinase A Activity by p90 Ribosomal S6 Kinase 1. J. Biol. Chem. 284: 33070-33078 [Abstract] [Full Text]  
  • Lopez-Vicente, L., Armengol, G., Pons, B., Coch, L., Argelaguet, E., Lleonart, M., Hernandez-Losa, J., de Torres, I., Ramon y Cajal, S. (2009). Regulation of Replicative and Stress-Induced Senescence by RSK4, which is Down-regulated in Human Tumors. Clin. Cancer Res. 15: 4546-4553 [Abstract] [Full Text]  
  • Arur, S., Ohmachi, M., Nayak, S., Hayes, M., Miranda, A., Hay, A., Golden, A., Schedl, T. (2009). Multiple ERK substrates execute single biological processes in Caenorhabditis elegans germ-line development. Proc. Natl. Acad. Sci. USA 106: 4776-4781 [Abstract] [Full Text]  
  • Thakur, A., Sun, Y., Bollig, A., Wu, J., Biliran, H., Banerjee, S., Sarkar, F. H., Liao, D. J. (2008). Anti-invasive and Antimetastatic Activities of Ribosomal Protein S6 Kinase 4 in Breast Cancer Cells. Clin. Cancer Res. 14: 4427-4436 [Abstract] [Full Text]  
  • Thakur, A., Rahman, K. W., Wu, J., Bollig, A., Biliran, H., Lin, X., Nassar, H., Grignon, D. J., Sarkar, F. H., Liao, J. D. (2007). Aberrant Expression of X-Linked Genes RbAp46, Rsk4, and Cldn2 in Breast Cancer. Mol Cancer Res 5: 171-181 [Abstract] [Full Text]  
  • Fletcher, R. B., Baker, J. C., Harland, R. M. (2006). FGF8 spliceforms mediate early mesoderm and posterior neural tissue formation in Xenopus. Development 133: 1703-1714 [Abstract] [Full Text]  
  • Dumont, J., Umbhauer, M., Rassinier, P., Hanauer, A., Verlhac, M.-H. (2005). p90Rsk is not involved in cytostatic factor arrest in mouse oocytes. JCB 169: 227-231 [Abstract] [Full Text]  
  • Clark, D.E., Errington, T.M., Smith, J.A., Frierson, H.F. Jr., Weber, M.J., Lannigan, D.A. (2005). The Serine/Threonine Protein Kinase, p90 Ribosomal S6 Kinase, Is an Important Regulator of Prostate Cancer Cell Proliferation. Cancer Res. 65: 3108-3116 [Abstract] [Full Text]  
  • Dummler, B. A., Hauge, C., Silber, J., Yntema, H. G., Kruse, L. S., Kofoed, B., Hemmings, B. A., Alessi, D. R., Frodin, M. (2005). Functional Characterization of Human RSK4, a New 90-kDa Ribosomal S6 Kinase, Reveals Constitutive Activation in Most Cell Types. J. Biol. Chem. 280: 13304-13314 [Abstract] [Full Text]  
  • Chiao, E., Leonard, J., Dickinson, K., Baker, J. C. (2005). High-throughput functional screen of mouse gastrula cDNA libraries reveals new components of endoderm and mesoderm specification. Genome Res 15: 44-53 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»