scholarly journals Monitoring Agonist-induced Phospholipase C Activation in Live Cells by Fluorescence Resonance Energy Transfer

2001 ◽  
Vol 276 (18) ◽  
pp. 15337-15344 ◽  
Author(s):  
Jose van der Wal ◽  
Ron Habets ◽  
Péter Várnai ◽  
Tamas Balla ◽  
Kees Jalink
Keyword(s):  
Energy Transfer ◽  
Phospholipase C ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Live Cells ◽  
Fluorescence Resonance

scholarly journals Spectral wide-field microscopic fluorescence resonance energy transfer imaging in live cells

2015 ◽  
Vol 20 (8) ◽  
pp. 086011 ◽  
Author(s):  
Lili Zhang ◽  
Guiqi Qin ◽  
Liuying Chai ◽  
Jiang Zhang ◽  
Fangfang Yang ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Live Cells ◽  
Wide Field ◽  
Fluorescence Resonance

Analisis of A-Kinase Anchoring Protein Interactions With PKA Using Fluorescence Resonance Energy Transfer

2000 ◽  
Vol 6 (S2) ◽  
pp. 828-829
Author(s):  
M. L. Ruehr ◽  
D. S. Damron ◽  
M. Bond
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Regulatory Subunit ◽  
Live Cells ◽  
Human Thyroid ◽  
Local Concentration ◽  
Fluorescence Resonance

The clustering of components of a signaling pathway at a specific subcellular location raises the local concentration of the appropriate messengers and serves to amplify the signal. The cAMP dependent-protein kinase (PKA) pathway is regulated by compartmentalization of its components. A-kinase anchoring proteins (AKAPs) tether PKA to specific subcellular sites, thus presumably increasing substrate specificity. Phosphorylation of the type II regulatory subunit of PKA (RII) increases its affinity for AKAPs in vitro (1). The purpose of this study was to investigate whether altering the phosphorylation state of RII in live cells changes its affinity for an AKAP. Specifically, we investigated the binding kinetics between Ht31, a peptide containing the PKA binding portion of an AKAP from human thyroid (2), and RII, in response to PKA activators or inhibitors.Fluorescence resonance energy transfer (FRET) was used to monitor binding events between RII and the catalytic subunit (C) of PKA, Ht31, or Ht31P, a mutated form of Ht31 which does not bind RII.

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