JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on August 4, 2000
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
275/32/24421    most recent
M003148200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email 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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sun, W.
Right arrow Articles by Johnson, G. L
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sun, W.
Right arrow Articles by Johnson, G. L
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print May 18, 2000
J. Biol. Chem, 10.1074/jbc.M003148200
Submitted on April 12, 2000
Revised on May 17, 2000
Accepted on May 18, 2000

MEK kinase 2 binds and activates protein kinase C-related kinase 2: bifurcation of kinase regulatory pathways at the level of a MAPK kinase Kinase

Weiyong Sun, Sylvie Vincent, Jeffrey Settleman, and Gary L Johnson

Department of Pharmacology, University of Colorado Health Sciences Center, Denver, CO 80262

Corresponding Author: Gary.Johnson{at}uchsc.edu

MEK kinase 2 (MEKK2) is a 70 kDa protein serine/threonine kinase that has been shown to function as a mitogen activated protein kinase (MAPK) kinase kinase. MEKK2 has its kinase domain in the COOH-terminal moiety of the protein. The NH2-terminal moiety of MEKK2 has no signature motif that would suggest a defined regulatory function. Yeast two-hybrid screening was performed to identify proteins that bind MEKK2. Protein kinase C-related kinase 2 (PRK2) was found to bind MEKK2, PRK2 has been previously shown to bind RhoA and the SH3 domain of Nck. PRK2 did not bind MEKK3, which closely related to MEKK2. The MEKK2 binding site maps to amino acids 637-660 in PRK2 that is distinct from the binding sites for RhoA and Nck. This sequence is divergent in the closely related kinase PRK1 (PKN) that did not bind MEKK2. In cells, MEKK2 and PRK2 are co-immunoprecipitated and PRK2 is activated by MEKK2. Similarly, purified recombinant MEKK2 activated PRK2 in vitro. MEKK2 activation of PRK2 is independent of MEKK2 regulation of the c-Jun NH2-terminal kinase (JNK) pathway. MEKK2 activation of PRK2 results in a bifurcation of signaling for the dual control of MAPK pathways and PRK2 regulated responses.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 GeneticsHome page
M. Betson and J. Settleman
A Rho-Binding Protein Kinase C-Like Activity Is Required for the Function of Protein Kinase N in Drosophila Development
Genetics, August 1, 2007; 176(4): 2201 - 2212.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
M. Blonska, Y. You, R. Geleziunas, and X. Lin
Restoration of NF-{kappa}B Activation by Tumor Necrosis Factor Alpha Receptor Complex-Targeted MEKK3 in Receptor-Interacting Protein-Deficient Cells
Mol. Cell. Biol., December 15, 2004; 24(24): 10757 - 10765.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S.-J. Kim, J.-H. Kim, Y.-G. Kim, H.-S. Lim, and J.-W. Oh
Protein Kinase C-related Kinase 2 Regulates Hepatitis C Virus RNA Polymerase Function by Phosphorylation
J. Biol. Chem., November 26, 2004; 279(48): 50031 - 50041.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. McDonald, P. O. Vacratsis, J. B. Bliska, and J. E. Dixon
The Yersinia Virulence Factor YopM Forms a Novel Protein Complex with Two Cellular Kinases
J. Biol. Chem., May 9, 2003; 278(20): 18514 - 18523.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
W. Sun, X. Wei, K. Kesavan, T. P. Garrington, R. Fan, J. Mei, S. M. Anderson, E. W. Gelfand, and G. L. Johnson
MEK Kinase 2 and the Adaptor Protein Lad Regulate Extracellular Signal-Regulated Kinase 5 Activation by Epidermal Growth Factor via Src
Mol. Cell. Biol., April 1, 2003; 23(7): 2298 - 2308.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
H. Mukai
The Structure and Function of PKN, a Protein Kinase Having a Catalytic Domain Homologous to That of PKC
J. Biochem., January 1, 2003; 133(1): 17 - 27.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
W. Sun, K. Kesavan, B. C. Schaefer, T. P. Garrington, M. Ware, N. L. Johnson, E. W. Gelfand, and G. L. Johnson
MEKK2 Associates with the Adapter Protein Lad/RIBP and Regulates the MEK5-BMK1/ERK5 Pathway
J. Biol. Chem., February 9, 2001; 276(7): 5093 - 5100.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. S. T. Hii, N. Moghadammi, A. Dunbar, and A. Ferrante
Activation of the Phosphatidylinositol 3-Kinase-Akt/Protein Kinase B Signaling Pathway in Arachidonic Acid-stimulated Human Myeloid and Endothelial Cells. INVOLVEMENT OF THE ErbB RECEPTOR FAMILY
J. Biol. Chem., July 13, 2001; 276(29): 27246 - 27255.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.