pubmed-article:14581471 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:14581471 | lifeskim:mentions | umls-concept:C1708800 | lld:lifeskim |
pubmed-article:14581471 | lifeskim:mentions | umls-concept:C1367675 | lld:lifeskim |
pubmed-article:14581471 | lifeskim:mentions | umls-concept:C1150423 | lld:lifeskim |
pubmed-article:14581471 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
pubmed-article:14581471 | lifeskim:mentions | umls-concept:C1150582 | lld:lifeskim |
pubmed-article:14581471 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:14581471 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:14581471 | pubmed:dateCreated | 2004-1-12 | lld:pubmed |
pubmed-article:14581471 | pubmed:abstractText | MEKK1 is a mitogen-activated protein kinase kinase kinase (MAP3K) that can regulate the c-Jun amino-terminal kinase (JNK) MAP kinase cascade. MEKK1 is comprised of a kinase domain and a long amino-terminal regulatory domain. This amino-terminal domain has a scaffold function in that it can assemble modules of the JNK and ERK MAP kinase cascades. Recently, we have demonstrated that MEKK1 binds to p115 Rho GTPase-activating protein, which has GTPase-activating protein activity toward RhoA. Thus, we tested whether Rho GTPases interact with the regulatory domain of MEKK1. RhoA, but not Rac or Cdc42, binds to a site in the aminoterminal one-third of MEKK1, which includes its PHD domain. The interaction is prevented by mutation of the essential cysteine in the MEKK1 PHD domain. Rho-GTP stimulates the kinase activity of full-length MEKK1 as much as 10-fold toward MEK4 but does not appear to be ubiquitinated by MEKK1 under conditions that result in modification of ERK2. In summary, we have characterized a novel point at which Rho GTPases impinge upon the regulation and function of MEKK1. | lld:pubmed |
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pubmed-article:14581471 | pubmed:language | eng | lld:pubmed |
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pubmed-article:14581471 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:14581471 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:14581471 | pubmed:month | Jan | lld:pubmed |
pubmed-article:14581471 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:14581471 | pubmed:author | pubmed-author:GutowskiSteph... | lld:pubmed |
pubmed-article:14581471 | pubmed:author | pubmed-author:SternweisPaul... | lld:pubmed |
pubmed-article:14581471 | pubmed:author | pubmed-author:CobbMelanie... | lld:pubmed |
pubmed-article:14581471 | pubmed:author | pubmed-author:GallagherEwen... | lld:pubmed |
pubmed-article:14581471 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:14581471 | pubmed:day | 16 | lld:pubmed |
pubmed-article:14581471 | pubmed:volume | 279 | lld:pubmed |
pubmed-article:14581471 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:14581471 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:14581471 | pubmed:pagination | 1872-7 | lld:pubmed |
pubmed-article:14581471 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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pubmed-article:14581471 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:14581471 | pubmed:articleTitle | RhoA binds to the amino terminus of MEKK1 and regulates its kinase activity. | lld:pubmed |
pubmed-article:14581471 | pubmed:affiliation | Department of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9041, USA. | lld:pubmed |
pubmed-article:14581471 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:14581471 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:14581471 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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