Germinal Center Kinase Is Required for Optimal Jun N-Terminal Kinase Activation by Toll-Like Receptor Agonists and Is Regulated by the Ubiquitin Proteasome System and Agonist-Induced, TRAF6-Dependent Stabilization
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| Published in | Molecular and Cellular Biology Vol. 24; no. 20; pp. 9165 - 9175 |
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| Format | Journal Article |
| Language | English |
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United States
American Society for Microbiology
01.10.2004
Taylor & Francis |
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| ISSN | 0270-7306 1098-5549 1067-8824 1098-5549 |
| DOI | 10.1128/MCB.24.20.9165-9175.2004 |
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Germinal center kinase (GCK), a member of the Ste20 family, selectively activates the Jun N-terminal kinase (JNK) group of mitogen-activated protein kinases. Here, we show that endogenous GCK is activated by polyinosine-polycytidine [poly(IC)] and lipopolysaccharides (LPS), lipid A, interleukin-1 (IL-1), and engagement of CD40, all agonists that require TRAF6 for JNK activation. RNA interference experiments indicate that GCK is required for the maximal activation of JNK by LPS, lipid A, poly(IC), and, to a lesser extent, IL-1 and engagement of CD40. GCK is ubiquitinated in situ and stabilized by inhibitors of the proteasome, indicating that GCK is subject to proteasomal turnover. GCK is constitutively active, and the kinase activity of GCK is required for GCK ubiquitination. Agonist activation of GCK involves the TRAF6-dependent transient stabilization of the GCK polypeptide rather than an increase in intrinsic kinase activity. Our results identify a physiologic function and unexpected mode of regulation for GCK. Germinal center kinase (GCK), a member of the Ste20 family, selectively activates the Jun N-terminal kinase (JNK) group of mitogen-activated protein kinases. Here, we show that endogenous GCK is activated by polyinosine-polycytidine [poly(IC)] and lipopolysaccharides (LPS), lipid A, interleukin-1 (IL-1), and engagement of CD40, all agonists that require TRAF6 for JNK activation. RNA interference experiments indicate that GCK is required for the maximal activation of JNK by LPS, lipid A, poly(IC), and, to a lesser extent, IL-1 and engagement of CD40. GCK is ubiquitinated in situ and stabilized by inhibitors of the proteasome, indicating that GCK is subject to proteasomal turnover. GCK is constitutively active, and the kinase activity of GCK is required for GCK ubiquitination. Agonist activation of GCK involves the TRAF6-dependent transient stabilization of the GCK polypeptide rather than an increase in intrinsic kinase activity. Our results identify a physiologic function and unexpected mode of regulation for GCK.Germinal center kinase (GCK), a member of the Ste20 family, selectively activates the Jun N-terminal kinase (JNK) group of mitogen-activated protein kinases. Here, we show that endogenous GCK is activated by polyinosine-polycytidine [poly(IC)] and lipopolysaccharides (LPS), lipid A, interleukin-1 (IL-1), and engagement of CD40, all agonists that require TRAF6 for JNK activation. RNA interference experiments indicate that GCK is required for the maximal activation of JNK by LPS, lipid A, poly(IC), and, to a lesser extent, IL-1 and engagement of CD40. GCK is ubiquitinated in situ and stabilized by inhibitors of the proteasome, indicating that GCK is subject to proteasomal turnover. GCK is constitutively active, and the kinase activity of GCK is required for GCK ubiquitination. Agonist activation of GCK involves the TRAF6-dependent transient stabilization of the GCK polypeptide rather than an increase in intrinsic kinase activity. Our results identify a physiologic function and unexpected mode of regulation for GCK. |
| Author | Jian Zhong John M. Kyriakis |
| AuthorAffiliation | Molecular Cardiology Research Institute and Department of Medicine, Tufts-New England Medical Center, and Department of Medicine, Tufts University School of Medicine, Boston, Massachusetts |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/15456887$$D View this record in MEDLINE/PubMed |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Corresponding author. Mailing address: Molecular Cardiology Research Institute Tufts-New England Medical Center, 750 Washington St., Box 8486, Boston, MA 02111. Phone: (617) 636-5190. Fax: (617) 636-5204. E-mail: jkyriakis@tufts-nemc.org. |
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Mendeley... Germinal center kinase (GCK), a member of the Ste20 family, selectively activates the Jun N-terminal kinase (JNK) group of mitogen-activated protein kinases.... |
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| SubjectTerms | Animals CD40 Antigens - metabolism Cell Growth and Development Cell Line Enzyme Activation Humans Interferon Inducers - metabolism Interleukin-1 - metabolism JNK Mitogen-Activated Protein Kinases - metabolism Lipid A - metabolism Lipopolysaccharides - metabolism MAP Kinase Kinase Kinase 1 - metabolism Membrane Glycoproteins - agonists Membrane Glycoproteins - metabolism Poly I-C - metabolism Proteasome Endopeptidase Complex - metabolism Proteasome Inhibitors Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism Receptors, Cell Surface - agonists Receptors, Cell Surface - metabolism RNA Interference Signal Transduction - physiology TNF Receptor-Associated Factor 6 - metabolism Toll-Like Receptors Ubiquitin - metabolism |
| Title | Germinal Center Kinase Is Required for Optimal Jun N-Terminal Kinase Activation by Toll-Like Receptor Agonists and Is Regulated by the Ubiquitin Proteasome System and Agonist-Induced, TRAF6-Dependent Stabilization |
| URI | http://mcb.asm.org/content/24/20/9165.abstract https://www.tandfonline.com/doi/abs/10.1128/MCB.24.20.9165-9175.2004 https://www.ncbi.nlm.nih.gov/pubmed/15456887 https://www.proquest.com/docview/19721683 https://www.proquest.com/docview/66925827 https://pubmed.ncbi.nlm.nih.gov/PMC517887 http://doi.org/10.1128/MCB.24.20.9165-9175.2004 |
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