| pubmed-article:19917606 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19917606 | lifeskim:mentions | umls-concept:C1333166 | lld:lifeskim |
| pubmed-article:19917606 | lifeskim:mentions | umls-concept:C1705705 | lld:lifeskim |
| pubmed-article:19917606 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:19917606 | lifeskim:mentions | umls-concept:C0010531 | lld:lifeskim |
| pubmed-article:19917606 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:19917606 | lifeskim:mentions | umls-concept:C1332813 | lld:lifeskim |
| pubmed-article:19917606 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:19917606 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:19917606 | pubmed:dateCreated | 2010-2-8 | lld:pubmed |
| pubmed-article:19917606 | pubmed:abstractText | Expression of the VACM-1/cul5 gene in endothelial and in cancer cell lines in vitro inhibits cellular proliferation and decreases phosphorylation of MAPK. Structure-function analysis of the VACM-1 protein sequence identified consensus sites specific for phosphorylation by protein kinases A and C (PKA and PKC) and a Nedd8 protein modification site. Mutations at the PKA-specific site in VACM-1/Cul5 ((S730A)VACM-1) sequence resulted in increased cellular growth and the appearance of a Nedd8-modified VACM-1/Cul5. The aim of this study was to examine if PKA-dependent phosphorylation of VACM-1/Cul5 controls its neddylation status, phosphorylation by PKC, and ultimately growth. Our results indicate that in vitro transfection of rat adrenal medullary endothelial cells with anti-VACM-1-specific small interfering RNA oligonucleotides decreases endogenous VACM-1 protein concentration and increases cell growth. Western blot analysis of cell lysates immunoprecipitated with an antibody directed against a PKA-specific phosphorylation site and probed with anti-VACM-1-specific antibody showed that PKA-dependent phosphorylation of VACM-1 protein was decreased in cells transfected with (S730A)VACM-1 cDNA when compared with the cytomegalovirus-transfected cells. This change was associated with increased modification of VACM-1 protein by Nedd8. Induction of PKA activity with forskolin reduced modification of VACM-1 protein by Nedd8. Finally, rat adrenal medullary endothelial cells transfected with (S730A)VACM-1/cul5 cDNA and treated with phorbol 12-myristate 13-acetate (10 and 100 nm) to induce PKC activity grew significantly faster than the control cells. These results suggest that the antiproliferative effect of VACM-1/Cul5 is dependent on its posttranslational modifications and will help in the design of new anticancer therapeutics that target the Nedd8 pathway. | lld:pubmed |
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| pubmed-article:19917606 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19917606 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19917606 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19917606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19917606 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19917606 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:19917606 | pubmed:issn | 1083-351X | lld:pubmed |
| pubmed-article:19917606 | pubmed:author | pubmed-author:JohnsonAlyssa... | lld:pubmed |
| pubmed-article:19917606 | pubmed:author | pubmed-author:LeIsabelle... | lld:pubmed |
| pubmed-article:19917606 | pubmed:author | pubmed-author:BradleyShirle... | lld:pubmed |
| pubmed-article:19917606 | pubmed:author | pubmed-author:OosterhouseEl... | lld:pubmed |
| pubmed-article:19917606 | pubmed:author | pubmed-author:HledinMichael... | lld:pubmed |
| pubmed-article:19917606 | pubmed:author | pubmed-author:MarquezGabrie... | lld:pubmed |
| pubmed-article:19917606 | pubmed:author | pubmed-author:Burnatowska-H... | lld:pubmed |
| pubmed-article:19917606 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19917606 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:19917606 | pubmed:volume | 285 | lld:pubmed |
| pubmed-article:19917606 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19917606 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19917606 | pubmed:pagination | 4883-95 | lld:pubmed |
| pubmed-article:19917606 | pubmed:dateRevised | 2011-7-25 | lld:pubmed |
| pubmed-article:19917606 | pubmed:meshHeading | pubmed-meshheading:19917606... | lld:pubmed |
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| pubmed-article:19917606 | pubmed:meshHeading | pubmed-meshheading:19917606... | lld:pubmed |
| pubmed-article:19917606 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:19917606 | pubmed:articleTitle | Phosphorylation of VACM-1/Cul5 by protein kinase A regulates its neddylation and antiproliferative effect. | lld:pubmed |
