pubmed-article:10557308 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10557308 | lifeskim:mentions | umls-concept:C0034678 | lld:lifeskim |
pubmed-article:10557308 | lifeskim:mentions | umls-concept:C1364684 | lld:lifeskim |
pubmed-article:10557308 | lifeskim:mentions | umls-concept:C1704803 | lld:lifeskim |
pubmed-article:10557308 | lifeskim:mentions | umls-concept:C1704804 | lld:lifeskim |
pubmed-article:10557308 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
pubmed-article:10557308 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
pubmed-article:10557308 | lifeskim:mentions | umls-concept:C1332768 | lld:lifeskim |
pubmed-article:10557308 | lifeskim:mentions | umls-concept:C1413549 | lld:lifeskim |
pubmed-article:10557308 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
pubmed-article:10557308 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:10557308 | pubmed:issue | 23 | lld:pubmed |
pubmed-article:10557308 | pubmed:dateCreated | 1999-12-13 | lld:pubmed |
pubmed-article:10557308 | pubmed:abstractText | Connector enhancer of KSR (CNK) is a multidomain protein required for RAS signaling. Its C-terminal portion (CNK(C-term)) directly binds to RAF. Herein, we show that the N-terminal portion of CNK (CNK(N-term)) strongly cooperates with RAS, whereas CNK(C-term) efficiently blocks RAS- and RAF-dependent signaling when overexpressed in the Drosophila eye. Two effector loop mutants of RAS(V12), S35 and C40, which selectively activate the mitogen-activated protein kinase (MAPK) and phosphatidylinositol-3-kinase pathways, respectively, do not cooperate with CNK. However, a strong cooperation is observed between CNK and RAS(V12G37), an effector loop mutant known in mammals to activate specifically the RAL pathway. We have identified two domains in CNK(N-term) that are critical for cooperation with RAS. Our results suggest that CNK functions in more than one pathway downstream of RAS. CNK(c-term) seems to regulate RAF, a component of the MAPK pathway, whereas CNK(N-term) seems to be involved in a MAPK-independent pathway. | lld:pubmed |
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pubmed-article:10557308 | pubmed:language | eng | lld:pubmed |
pubmed-article:10557308 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10557308 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10557308 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10557308 | pubmed:month | Nov | lld:pubmed |
pubmed-article:10557308 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:10557308 | pubmed:author | pubmed-author:RubinG MGM | lld:pubmed |
pubmed-article:10557308 | pubmed:author | pubmed-author:KwakJJ | lld:pubmed |
pubmed-article:10557308 | pubmed:author | pubmed-author:WongA MAM | lld:pubmed |
pubmed-article:10557308 | pubmed:author | pubmed-author:TherrienMM | lld:pubmed |
pubmed-article:10557308 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10557308 | pubmed:day | 9 | lld:pubmed |
pubmed-article:10557308 | pubmed:volume | 96 | lld:pubmed |
pubmed-article:10557308 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10557308 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10557308 | pubmed:pagination | 13259-63 | lld:pubmed |
pubmed-article:10557308 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:10557308 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10557308 | pubmed:articleTitle | Functional analysis of CNK in RAS signaling. | lld:pubmed |
pubmed-article:10557308 | pubmed:affiliation | Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3200, USA. | lld:pubmed |
pubmed-article:10557308 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10557308 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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