| pubmed-article:18708665 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18708665 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:18708665 | lifeskim:mentions | umls-concept:C0070876 | lld:lifeskim |
| pubmed-article:18708665 | lifeskim:mentions | umls-concept:C0442805 | lld:lifeskim |
| pubmed-article:18708665 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:18708665 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:18708665 | lifeskim:mentions | umls-concept:C0220905 | lld:lifeskim |
| pubmed-article:18708665 | pubmed:issue | 43 | lld:pubmed |
| pubmed-article:18708665 | pubmed:dateCreated | 2008-10-20 | lld:pubmed |
| pubmed-article:18708665 | pubmed:abstractText | To investigate the effect of phosphorylation on the interactions of phospholamban (PLB) with itself and its regulatory target, SERCA, we measured FRET from CFP-SERCA or CFP-PLB to YFP-PLB in live AAV-293 cells. Phosphorylation of PLB was mimicked by mutations S16E (PKA site) or S16E/T17E (PKA+CaMKII sites). FRET increased with protein concentration up to a maximum (FRET(max)) that was taken to represent the intrinsic FRET of the bound complex. The concentration dependence of FRET yielded dissociation constants (K(D)) for the PLB-PLB and PLB-SERCA interactions. PLB-PLB FRET data suggest pseudo-phosphorylation of PLB increased oligomerization of PLB but did not alter PLB pentamer quaternary structure. PLB-SERCA FRET experiments showed an apparent decrease in binding of PLB to SERCA and an increase in the apparent PLB-SERCA binding cooperativity. It is likely that these changes are secondary effects of increased oligomerization of PLB; a change in the inherent affinity of monomeric PLB for SERCA was not detected. In addition, PLB-SERCA complex FRET(max) was reduced by phosphomimetic mutations, suggesting the conformation of the regulatory complex is significantly altered by PLB phosphorylation. | lld:pubmed |
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| pubmed-article:18708665 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18708665 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18708665 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18708665 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18708665 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:18708665 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:18708665 | pubmed:author | pubmed-author:RobiaSeth LSL | lld:pubmed |
| pubmed-article:18708665 | pubmed:author | pubmed-author:HouZhanjiaZ | lld:pubmed |
| pubmed-article:18708665 | pubmed:author | pubmed-author:KellyEileen... | lld:pubmed |
| pubmed-article:18708665 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18708665 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:18708665 | pubmed:volume | 283 | lld:pubmed |
| pubmed-article:18708665 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18708665 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18708665 | pubmed:pagination | 28996-9003 | lld:pubmed |
| pubmed-article:18708665 | pubmed:dateRevised | 2011-5-2 | lld:pubmed |
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| pubmed-article:18708665 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18708665 | pubmed:articleTitle | Phosphomimetic mutations increase phospholamban oligomerization and alter the structure of its regulatory complex. | lld:pubmed |
| pubmed-article:18708665 | pubmed:affiliation | Department of Physiology, Loyola University Chicago, Maywood, Illinois 60153, USA. | lld:pubmed |
| pubmed-article:18708665 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18708665 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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