| pubmed-article:11427728 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11427728 | lifeskim:mentions | umls-concept:C1706586 | lld:lifeskim |
| pubmed-article:11427728 | lifeskim:mentions | umls-concept:C0007620 | lld:lifeskim |
| pubmed-article:11427728 | lifeskim:mentions | umls-concept:C0532128 | lld:lifeskim |
| pubmed-article:11427728 | lifeskim:mentions | umls-concept:C0085862 | lld:lifeskim |
| pubmed-article:11427728 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:11427728 | lifeskim:mentions | umls-concept:C1299583 | lld:lifeskim |
| pubmed-article:11427728 | lifeskim:mentions | umls-concept:C0812215 | lld:lifeskim |
| pubmed-article:11427728 | lifeskim:mentions | umls-concept:C2746015 | lld:lifeskim |
| pubmed-article:11427728 | lifeskim:mentions | umls-concept:C1608386 | lld:lifeskim |
| pubmed-article:11427728 | lifeskim:mentions | umls-concept:C1549571 | lld:lifeskim |
| pubmed-article:11427728 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:11427728 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:11427728 | pubmed:dateCreated | 2001-7-4 | lld:pubmed |
| pubmed-article:11427728 | pubmed:abstractText | The Ser/Thr kinase Raf-1 is a protooncogene product that is a central component in many signaling pathways involved in normal cell growth and oncogenic transformation. Upon activation, Raf-1 phosphorylates mitogen-activated protein kinase kinase (MEK), which in turn activates mitogen-activated protein kinase/extracellular signal-regulated kinases (MAPK/ERKs), leading to the propagation of signals. Depending on specific stimuli and cellular environment, the Raf-1--MEK--ERK cascade regulates diverse cellular processes such as proliferation, differentiation, and apoptosis. Here, we describe a MEK--ERK-independent prosurvival function of Raf-1. We found that Raf-1 interacts with the proapoptotic, stress-activated protein kinase ASK1 (apoptosis signal-regulating kinase 1) in vitro and in vivo. Deletion analysis localized the Raf-1 binding site to the N-terminal regulatory fragment of ASK1. This interaction allows Raf-1 to act independently of the MEK--ERK pathway to inhibit apoptosis. Furthermore, catalytically inactive forms of Raf-1 can mimic the wild-type effect, raising the possibility of a kinase-independent function of Raf-1. Thus, Raf-1 may promote cell survival through its protein-protein interactions in addition to its established MEK kinase function. | lld:pubmed |
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| pubmed-article:11427728 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11427728 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11427728 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11427728 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11427728 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11427728 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:11427728 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:11427728 | pubmed:author | pubmed-author:FujiiKK | lld:pubmed |
| pubmed-article:11427728 | pubmed:author | pubmed-author:ChenJJ | lld:pubmed |
| pubmed-article:11427728 | pubmed:author | pubmed-author:RobertsTT | lld:pubmed |
| pubmed-article:11427728 | pubmed:author | pubmed-author:ZhangLL | lld:pubmed |
| pubmed-article:11427728 | pubmed:author | pubmed-author:GIEE | lld:pubmed |
| pubmed-article:11427728 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11427728 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:11427728 | pubmed:volume | 98 | lld:pubmed |
| pubmed-article:11427728 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11427728 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11427728 | pubmed:pagination | 7783-8 | lld:pubmed |
| pubmed-article:11427728 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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| pubmed-article:11427728 | pubmed:meshHeading | pubmed-meshheading:11427728... | lld:pubmed |
| pubmed-article:11427728 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11427728 | pubmed:articleTitle | Raf-1 promotes cell survival by antagonizing apoptosis signal-regulating kinase 1 through a MEK-ERK independent mechanism. | lld:pubmed |
| pubmed-article:11427728 | pubmed:affiliation | Department of Pharmacology, Emory University School of Medicine, Atlanta, GA 30322, USA. | lld:pubmed |
| pubmed-article:11427728 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11427728 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11427728 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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