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
Right arrow Citation Map
Services
Right arrow E-mail this article to a friend
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 Diaz-Meco, M. T.
Right arrow Articles by Moscat, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Diaz-Meco, M. T.
Right arrow Articles by Moscat, J.
Right arrowPubmed/NCBI databases
*Domain*Gene
*GEO Profiles*HomoloGene
*UniGene
*Substance via MeSH

 Previous Article  |  Next Article 

Molecular and Cellular Biology, February 2001, p. 1218-1227, Vol. 21, No. 4
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.4.1218-1227.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

MEK5, a New Target of the Atypical Protein Kinase C Isoforms in Mitogenic Signaling

María T. Diaz-Meco and Jorge Moscat*

Centro de Biología Molecular "Severo Ochoa," Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid, Universidad Autónoma, 28049 Madrid, Spain

Received 8 September 2000/Returned for modification 22 October 2000/Accepted 21 November 2000

The MEK5-extracellular signal-regulated kinase (ERK5) tandem is a novel mitogen-activated protein kinase cassette critically involved in mitogenic activation by the epidermal growth factor (EGF). The atypical protein kinase C isoforms (aPKCs) have been shown to be required for cell growth and proliferation and have been reported to interact with the adapter protein p62 through a short stretch of acidic amino acids termed the aPKC interaction domain. This region is also present in MEK5, suggesting that it may be an aPKC-binding partner. Here we demonstrate that the aPKCs interact in an EGF-inducible manner with MEK5 and that this interaction is required and sufficient for the activation of MEK5 in response to EGF. Consistent with the role of the aPKCs in the MEK5-ERK5 pathway, we show that zeta PKC and lambda /iota PKC activate the Jun promoter through the MEF2C element, a well-established target of ERK5. From all these results, we conclude that MEK5 is a critical target of the aPKCs during mitogenic signaling.

* Corresponding author. Mailing address: Centro de Biología Molecular "Severo Ochoa," (CSIC), Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain. Phone: 34-913978039. Fax: 34-629690055. E-mail: jmoscat{at}cbm.uam.es.

Molecular and Cellular Biology, February 2001, p. 1218-1227, Vol. 21, No. 4
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.4.1218-1227.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Guo, W., Wu, S., Wang, L., Wang, R.-y., Wei, X., Liu, J., Fang, B. (2009). Interruption of RNA processing machinery by a small compound, 1-[(4-chlorophenyl)methyl]-1H-indole-3-carboxaldehyde (oncrasin-1). Molecular Cancer Therapeutics 8: 441-448 [Abstract] [Full Text]  
  • Vasavada, R. C., Wang, L., Fujinaka, Y., Takane, K. K., Rosa, T. C., Mellado-Gil, J. M.D., Friedman, P. A., Garcia-Ocana, A. (2007). Protein Kinase C-{zeta} Activation Markedly Enhances {beta}-Cell Proliferation: An Essential Role in Growth Factor Mediated {beta}-Cell Mitogenesis. Diabetes 56: 2732-2743 [Abstract] [Full Text]  
  • Natrajan, R., Little, S. E., Reis-Filho, J. S., Hing, L., Messahel, B., Grundy, P. E., Dome, J. S., Schneider, T., Vujanic, G. M., Pritchard-Jones, K., Jones, C. (2006). Amplification and Overexpression of CACNA1E Correlates with Relapse in Favorable Histology Wilms' Tumors. Clin. Cancer Res. 12: 7284-7293 [Abstract] [Full Text]  
  • Kim, J. H., Kim, J. H., Ohba, M., Suh, P.-G., Ryu, S. H. (2005). Novel Functions of the Phospholipase D2-Phox Homology Domain in Protein Kinase C{zeta} Activation. Mol. Cell. Biol. 25: 3194-3208 [Abstract] [Full Text]  
  • Seibenhener, M. L., Babu, J. R., Geetha, T., Wong, H. C., Krishna, N. R., Wooten, M. W. (2004). Sequestosome 1/p62 Is a Polyubiquitin Chain Binding Protein Involved in Ubiquitin Proteasome Degradation. Mol. Cell. Biol. 24: 8055-8068 [Abstract] [Full Text]  
  • Sato, S., Fujita, N., Tsuruo, T. (2004). Involvement of 3-Phosphoinositide-dependent Protein Kinase-1 in the MEK/MAPK Signal Transduction Pathway. J. Biol. Chem. 279: 33759-33767 [Abstract] [Full Text]  
  • Xu, B.-e, Stippec, S., Lenertz, L., Lee, B.-H., Zhang, W., Lee, Y.-K., Cobb, M. H. (2004). WNK1 Activates ERK5 by an MEKK2/3-dependent Mechanism. J. Biol. Chem. 279: 7826-7831 [Abstract] [Full Text]  
  • Cameron, S. J., Abe, J.-i., Malik, S., Che, W., Yang, J. (2004). Differential Role of MEK5{alpha} and MEK5{beta} in BMK1/ERK5 Activation. J. Biol. Chem. 279: 1506-1512 [Abstract] [Full Text]  
  • Noda, Y., Kohjima, M., Izaki, T., Ota, K., Yoshinaga, S., Inagaki, F., Ito, T., Sumimoto, H. (2003). Molecular Recognition in Dimerization between PB1 Domains. J. Biol. Chem. 278: 43516-43524 [Abstract] [Full Text]  
  • Nakamura, K., Johnson, G. L. (2003). PB1 Domains of MEKK2 and MEKK3 Interact with the MEK5 PB1 Domain for Activation of the ERK5 Pathway. J. Biol. Chem. 278: 36989-36992 [Abstract] [Full Text]  
  • Lamark, T., Perander, M., Outzen, H., Kristiansen, K., Overvatn, A., Michaelsen, E., Bjorkoy, G., Johansen, T. (2003). Interaction Codes within the Family of Mammalian Phox and Bem1p Domain-containing Proteins. J. Biol. Chem. 278: 34568-34581 [Abstract] [Full Text]  
  • Geetha, T., Wooten, M. W. (2003). Association of the Atypical Protein Kinase C-interacting Protein p62/ZIP with Nerve Growth Factor Receptor TrkA Regulates Receptor Trafficking and Erk5 Signaling. J. Biol. Chem. 278: 4730-4739 [Abstract] [Full Text]  
  • Hirai, T., Chida, K. (2003). Protein Kinase C{zeta} (PKC{zeta}): Activation Mechanisms and Cellular Functions. J Biochem 133: 1-7 [Abstract] [Full Text]  
  • Suzuki, A., Akimoto, K., Ohno, S. (2003). Protein Kinase C {lambda}/{iota} (PKC{lambda}/{iota}): A PKC Isotype Essential for the Development of Multicellular Organisms. J Biochem 133: 9-16 [Abstract] [Full Text]  
  • Avila, A., Silverman, N., Diaz-Meco, M. T., Moscat, J. (2002). The Drosophila Atypical Protein Kinase C-Ref(2)P Complex Constitutes a Conserved Module for Signaling in the Toll Pathway. Mol. Cell. Biol. 22: 8787-8795 [Abstract] [Full Text]  
  • Pearson, G. W., Cobb, M. H. (2002). Cell Condition-dependent Regulation of ERK5 by cAMP. J. Biol. Chem. 277: 48094-48098 [Abstract] [Full Text]  
  • San-Antonio, B., Iniguez, M. A., Fresno, M. (2002). Protein Kinase Czeta Phosphorylates Nuclear Factor of Activated T Cells and Regulates Its Transactivating Activity. J. Biol. Chem. 277: 27073-27080 [Abstract] [Full Text]  


Copyright © 2010 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»