| pubmed-article:15758184 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15758184 | lifeskim:mentions | umls-concept:C0027882 | lld:lifeskim |
| pubmed-article:15758184 | lifeskim:mentions | umls-concept:C0521119 | lld:lifeskim |
| pubmed-article:15758184 | lifeskim:mentions | umls-concept:C0530778 | lld:lifeskim |
| pubmed-article:15758184 | lifeskim:mentions | umls-concept:C1179132 | lld:lifeskim |
| pubmed-article:15758184 | lifeskim:mentions | umls-concept:C1858131 | lld:lifeskim |
| pubmed-article:15758184 | lifeskim:mentions | umls-concept:C1155502 | lld:lifeskim |
| pubmed-article:15758184 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
| pubmed-article:15758184 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
| pubmed-article:15758184 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
| pubmed-article:15758184 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:15758184 | pubmed:dateCreated | 2005-3-10 | lld:pubmed |
| pubmed-article:15758184 | pubmed:abstractText | Group I metabotropic glutamate receptors (mGluRs) increase cellular levels of inositol-1,4,5-triphosphate (IP3) and thereby trigger intracellular Ca2+ release. Also, group I mGluRs are organized with members of Homer scaffold proteins into multiprotein complexes involved in postreceptor signaling. In this study, we investigated the relative importance of the IP3/Ca2+ signaling and novel Homer proteins in group I mGluR-mediated activation of extracellular signal-regulated protein kinases 1 and 2 (ERK1/2) in cultured rat striatal neurons. We found that selective activation of mGluR5, but not mGluR1, increased ERK1/2 phosphorylation. Whereas the IP3/Ca2+ cascade transmits a small portion of signals from mGluR5 to ERK1/2, the member of Homer family Homer1b/c forms a central signaling pathway linking mGluR5 to ERK1/2 in a Ca2+-independent manner. This was demonstrated by the findings that the mGluR5-mediated ERK1/2 phosphorylation was mostly reduced by a cell-permeable Tat-fusion peptide that selectively disrupted the interaction of mGluR5 with the Homer1b/c and by small interfering RNAs that selectively knocked down cellular levels of Homer1b/c proteins. Furthermore, ERK1/2, when only coactivated by both IP3/Ca2+- and Homer1b/c-dependent pathways, showed the ability to phosphorylate two transcription factors, Elk-1 and cAMP response element-binding protein, and thereby facilitated c-Fos expression. Together, we have identified two coordinated signaling pathways (a conventional IP3/Ca2+ vs a novel Homer pathway) that differentially mediate the mGluR5-ERK coupling in neurons. Both the Ca2+-dependent and -independent pathways are corequired to activate ERK1/2 to a level sufficient to achieve the mGluR5-dependent synapse-to-nucleus communication imperative for the transcriptional regulation. | lld:pubmed |
| pubmed-article:15758184 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15758184 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15758184 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15758184 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15758184 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15758184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15758184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15758184 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15758184 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:15758184 | pubmed:issn | 1529-2401 | lld:pubmed |
| pubmed-article:15758184 | pubmed:author | pubmed-author:WangJohn QJQ | lld:pubmed |
| pubmed-article:15758184 | pubmed:author | pubmed-author:MaoLiminL | lld:pubmed |
| pubmed-article:15758184 | pubmed:author | pubmed-author:ZANARR | lld:pubmed |
| pubmed-article:15758184 | pubmed:author | pubmed-author:ZhangGuochiG | lld:pubmed |
| pubmed-article:15758184 | pubmed:author | pubmed-author:TangQingsongQ | lld:pubmed |
| pubmed-article:15758184 | pubmed:author | pubmed-author:SamdaniShazia... | lld:pubmed |
| pubmed-article:15758184 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:15758184 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:15758184 | pubmed:volume | 25 | lld:pubmed |
| pubmed-article:15758184 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15758184 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15758184 | pubmed:pagination | 2741-52 | lld:pubmed |
| pubmed-article:15758184 | pubmed:dateRevised | 2010-1-13 | lld:pubmed |
| pubmed-article:15758184 | pubmed:meshHeading | pubmed-meshheading:15758184... | lld:pubmed |
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| pubmed-article:15758184 | pubmed:meshHeading | pubmed-meshheading:15758184... | lld:pubmed |
| pubmed-article:15758184 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15758184 | pubmed:articleTitle | The scaffold protein Homer1b/c links metabotropic glutamate receptor 5 to extracellular signal-regulated protein kinase cascades in neurons. | lld:pubmed |
| pubmed-article:15758184 | pubmed:affiliation | Department of Basic Medical Science, University of Missouri-Kansas City, School of Medicine, Kansas City, Missouri 64108, USA. | lld:pubmed |
| pubmed-article:15758184 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15758184 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15758184 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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