Source:http://linkedlifedata.com/resource/pubmed/id/11342545
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
28
|
pubmed:dateCreated |
2001-7-9
|
pubmed:abstractText |
Endothelin-1 (ET-1) is a vasoconstrictor peptide known to be a potent mitogen for glomerular mesangial cells (GMC). In the current study, it is demonstrated that ET-1 treatment of GMC results in serine phosphorylation of the 66-kDa isoform of the adapter protein Shc (p66(Shc)). ET-1-induced serine phosphorylation of p66(Shc) requires activation of the mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase (ERK) signaling module and is efficiently inhibited by both a MAPK/ERK kinase (MEK)-selective inhibitor and adenovirus-mediated transfer of a dominant interfering MEK1 mutant. Furthermore, adenovirus-mediated transfer of a constitutively active MEK1 mutant was found to markedly increase p66(Shc) serine phosphorylation. Adenoviruses encoding constitutively active mutants of MAPK kinases 3 and 6 (upstream kinases of p38(MAPK)) and 7 (upstream kinase of c-Jun NH(2)-terminal kinase) failed to induce serine phosphorylation of this adaptor protein. Serine phosphorylation of p66(Shc) resulted in its association with the serine binding motif-containing protein 14-3-3. ET-1-induced phosphorylation of a serine encompassed in the 14-3-3 binding motif of p66(Shc) was confirmed in experiments employing anti-phospho-14-3-3 binding motif antibodies. These studies are the first to demonstrate that G protein-coupled receptors stimulate serine phosphorylation of p66(Shc) and the first to report the formation of a signaling complex between p66(Shc) and 14-3-3.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/14-3-3 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/Endothelin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SHC1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Shc Signaling Adaptor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Shc1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine 3-Monooxygenase
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
13
|
pubmed:volume |
276
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
26640-7
|
pubmed:dateRevised |
2008-11-21
|
pubmed:meshHeading |
pubmed-meshheading:11342545-14-3-3 Proteins,
pubmed-meshheading:11342545-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:11342545-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:11342545-Animals,
pubmed-meshheading:11342545-Cells, Cultured,
pubmed-meshheading:11342545-Endothelin-1,
pubmed-meshheading:11342545-Glomerular Mesangium,
pubmed-meshheading:11342545-Humans,
pubmed-meshheading:11342545-Phosphorylation,
pubmed-meshheading:11342545-Proteins,
pubmed-meshheading:11342545-Rats,
pubmed-meshheading:11342545-Rats, Sprague-Dawley,
pubmed-meshheading:11342545-Serine,
pubmed-meshheading:11342545-Shc Signaling Adaptor Proteins,
pubmed-meshheading:11342545-Signal Transduction,
pubmed-meshheading:11342545-Tyrosine 3-Monooxygenase
|
pubmed:year |
2001
|
pubmed:articleTitle |
Endothelin-1 induces serine phosphorylation of the adaptor protein p66Shc and its association with 14-3-3 protein in glomerular mesangial cells.
|
pubmed:affiliation |
Department of Internal Medicine, University of Florence, v. le Morgagni 85, Florence 50141, Italy. m.foschi@dfc.unifi.it
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|