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rdf:type
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Description
| - Phosducin (Pdc), a highly conserved phosphoprotein, plays an important role in the regulation of G protein signaling, transcriptional control, and modulation of blood pressure. Pdc is negatively regulated by phosphorylation followed by binding to the 14-3-3 protein, whose role is still unclear. To gain insight into the role of 14-3-3 in the regulation of Pdc function, we studied structural changes of Pdc induced by phosphorylation and 14-3-3 protein binding using time-resolved fluorescence spectroscopy. Our data show that the phosphorylation of the N-terminal domain of Pdc at Ser-54 and Ser-73 affects the structure of the whole Pdc molecule. Complex formation with 14-3-3 reduces the flexibility of both the N- and C-terminal domains of phosphorylated Pdc, as determined by time-resolved tryptophan and dansyl fluorescence
- Phosducin (Pdc), a highly conserved phosphoprotein, plays an important role in the regulation of G protein signaling, transcriptional control, and modulation of blood pressure. Pdc is negatively regulated by phosphorylation followed by binding to the 14-3-3 protein, whose role is still unclear. To gain insight into the role of 14-3-3 in the regulation of Pdc function, we studied structural changes of Pdc induced by phosphorylation and 14-3-3 protein binding using time-resolved fluorescence spectroscopy. Our data show that the phosphorylation of the N-terminal domain of Pdc at Ser-54 and Ser-73 affects the structure of the whole Pdc molecule. Complex formation with 14-3-3 reduces the flexibility of both the N- and C-terminal domains of phosphorylated Pdc, as determined by time-resolved tryptophan and dansyl fluorescence (en)
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Title
| - Structural Modulation of Phosducin by Phosphorylation and 14-3-3 Protein Binding
- Structural Modulation of Phosducin by Phosphorylation and 14-3-3 Protein Binding (en)
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skos:prefLabel
| - Structural Modulation of Phosducin by Phosphorylation and 14-3-3 Protein Binding
- Structural Modulation of Phosducin by Phosphorylation and 14-3-3 Protein Binding (en)
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skos:notation
| - RIV/00216208:11310/12:10124478!RIV13-GA0-11310___
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http://linked.open...avai/riv/aktivita
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http://linked.open...avai/riv/aktivity
| - I, P(GAP305/11/0708), S, Z(MSM0021620857)
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http://linked.open...iv/cisloPeriodika
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http://linked.open...vai/riv/dodaniDat
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http://linked.open...aciTvurceVysledku
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http://linked.open.../riv/druhVysledku
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http://linked.open...iv/duvernostUdaju
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http://linked.open...titaPredkladatele
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http://linked.open...dnocenehoVysledku
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http://linked.open...ai/riv/idVysledku
| - RIV/00216208:11310/12:10124478
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http://linked.open...riv/jazykVysledku
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http://linked.open.../riv/klicovaSlova
| - fluorescence; 14-3-3 protein; phosducin (en)
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http://linked.open.../riv/klicoveSlovo
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http://linked.open...odStatuVydavatele
| - US - Spojené státy americké
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http://linked.open...ontrolniKodProRIV
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http://linked.open...i/riv/nazevZdroje
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http://linked.open...in/vavai/riv/obor
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http://linked.open...ichTvurcuVysledku
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http://linked.open...cetTvurcuVysledku
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http://linked.open...vavai/riv/projekt
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http://linked.open...UplatneniVysledku
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http://linked.open...v/svazekPeriodika
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http://linked.open...iv/tvurceVysledku
| - Heřman, Petr
- Obšil, Tomáš
- Šulc, Miroslav
- Štěpánek, Miroslav
- Večeř, Jaroslav
- Obšilová, Veronika
- Řežábková, Lenka
- Kacířová, Miroslava
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http://linked.open...ain/vavai/riv/wos
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http://linked.open...n/vavai/riv/zamer
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issn
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number of pages
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http://bibframe.org/vocab/doi
| - 10.1016/j.bpj.2012.09.021
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http://localhost/t...ganizacniJednotka
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