Linked Life Data

16849316

Source:http://linkedlifedata.com/resource/pubmed/id/16849316

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pubmed-article:16849316pubmed:dateCreated2006-9-4lld:pubmed
pubmed-article:16849316pubmed:abstractTextThe p38alpha MAPK participates in a variety of biological processes. Activation of p38alpha is mediated by phosphorylation on specific regulatory tyrosine and threonine sites, and the three dual kinases, MAPK kinase 3 (MKK3), MKK4, and MKK6, are known to be the upstream activators of p38alpha. In addition to activation by upstream kinases, p38alpha can autoactivate when interacting with transforming growth factor-beta-activated protein kinase 1-binding protein 1 (TAB1). Here we used MKK3 and MKK6 double knock-out (MKK3/6 DKO) and MKK4/7 DKO mouse embryonic fibroblast (MEF) cells to examine activation mechanisms of p38alpha. We confirmed that the MKK3/6 pathway is a primary mechanism for p38alpha phosphorylation in MEF cells, and we also showed the presence of other p38alpha activation pathways. We show that TAB1-mediated p38alpha phosphorylation in MEF cells did not need MKK3/4/6, and it accounted for a small portion of the total p38alpha phosphorylation that was induced by hyperosmolarity and anisomycin. We observed that a portion of peroxynitrite-induced phospho-p38alpha is associated with an approximately 85-kDa disulfide complex in wild-type MEF cells. Peroxynitrite-induced phosphorylation of p38alpha in the approximately 85-kDa complex is independent from MKK3/6 because only phospho-p38alpha not associated with the disulfide complex was diminished in MKK3/6 DKO cells. In addition, our data suggest interference among different pathways because TAB1 had an inhibitory effect on p38alpha phosphorylation in the peroxynitrite-induced approximately 85-kDa complex. Mutagenesis analysis of the cysteines in p38alpha revealed that no disulfide bond forms between p38alpha and other proteins in the approximately 85-kDa complex, suggesting it is a p38alpha binding partner(s) that forms disulfide bonds, which enable it to bind to p38alpha. Therefore, multiple mechanisms of p38alpha activation exist that can influence each other, be simultaneously activated by a given stimulus, and/or be selectively used by different stimuli in a cell type-specific manner.lld:pubmed
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pubmed-article:16849316pubmed:authorpubmed-author:DavisRoger...lld:pubmed
pubmed-article:16849316pubmed:authorpubmed-author:HanJiahuaiJlld:pubmed
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pubmed-article:16849316pubmed:dateRevised2009-11-19lld:pubmed
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pubmed-article:16849316pubmed:year2006lld:pubmed
pubmed-article:16849316pubmed:articleTitleMultiple activation mechanisms of p38alpha mitogen-activated protein kinase.lld:pubmed
pubmed-article:16849316pubmed:affiliationDepartment of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA.lld:pubmed
pubmed-article:16849316pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:16849316pubmed:publicationTypeResearch Support, N.I.H., Extramurallld:pubmed
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