|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
43
|
|
pubmed:dateCreated |
2008-10-20
|
|
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.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-10233073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-10766848,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-10809745,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-10964438,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-10998362,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-11700069,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-12134142,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-12465028,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-12525698,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-12838339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-12962492,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-14507721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-15049694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-15215472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-15448204,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-15766259,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-15909986,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-16043693,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-16231289,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-16363815,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-16564056,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-16574147,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-17073452,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-17548345,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-17766390,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-17804809,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-17975108,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-18081313,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-18287099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-18338856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-235523,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-2544595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-6211626,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-6229539,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-7703259,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-9062126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-9182523,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-9188486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-9335549,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18708665-9790566
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0021-9258
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
24
|
|
pubmed:volume |
283
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
28996-9003
|
|
pubmed:dateRevised |
2011-5-2
|
|
pubmed:meshHeading |
pubmed-meshheading:18708665-Calcium-Binding Proteins,
pubmed-meshheading:18708665-Cell Adhesion,
pubmed-meshheading:18708665-Cell Line,
pubmed-meshheading:18708665-Fluorescence Resonance Energy Transfer,
pubmed-meshheading:18708665-Humans,
pubmed-meshheading:18708665-Kinetics,
pubmed-meshheading:18708665-Models, Biological,
pubmed-meshheading:18708665-Models, Molecular,
pubmed-meshheading:18708665-Models, Statistical,
pubmed-meshheading:18708665-Mutagenesis,
pubmed-meshheading:18708665-Mutation,
pubmed-meshheading:18708665-Phosphorylation,
pubmed-meshheading:18708665-Protein Structure, Quaternary,
pubmed-meshheading:18708665-Sarcoplasmic Reticulum Calcium-Transporting ATPases,
pubmed-meshheading:18708665-Static Electricity
|
|
pubmed:year |
2008
|
|
pubmed:articleTitle |
Phosphomimetic mutations increase phospholamban oligomerization and alter the structure of its regulatory complex.
|
|
pubmed:affiliation |
Department of Physiology, Loyola University Chicago, Maywood, Illinois 60153, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
|
