Počet záznamů: 1  

Structural Modulation of Phosducin by Phosphorylation and 14-3-3 Protein Binding

  1. 1.
    0388343 - MBÚ 2013 RIV US eng J - Článek v odborném periodiku
    Řežábková, L. - Kacířová, M. - Šulc, Miroslav - Herman, P. - Večeř, J. - Štěpánek, M. - Obšilová, Veronika - Obšil, T.
    Structural Modulation of Phosducin by Phosphorylation and 14-3-3 Protein Binding.
    Biophysical Journal. Roč. 103, č. 9 (2012), s. 1960-1969. ISSN 0006-3495. E-ISSN 1542-0086
    Institucionální podpora: RVO:61388971 ; RVO:67985823
    Klíčová slova: phosducin * 14-3-3 protein * fluorescence
    Kód oboru RIV: CE - Biochemie
    Impakt faktor: 3.668, rok: 2012

    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
    Trvalý link: http://hdl.handle.net/11104/0217202

     
     
Počet záznamů: 1  

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