%0 Journal Article
%T ¡°Shaping¡± of cell signaling via AKAP-tethered PDE4D: Probing with AKAR2-AKAP5 biosensor
%A Salih S Kocer
%A Hsien-yu Wang
%A Craig C Malbon
%J Journal of Molecular Signaling
%D 2012
%I Ubiquity Press
%R 10.1186/1750-2187-7-4
%X Using an AKAR2-AKAP5 fusion ¡°biosensor¡±, we investigated the spatial-temporal activation of AKAP5 undergoing phosphorylation by PKA in response to ¦Â-adrenergic stimulation. The pattern of PKA activation reported by AKAR2-AKAP5 is a more rapid and spatially distinct from those ¡°sensed¡± by AKAR2-AKAP12. Spatial-temporal restriction of activated PKA by AKAP5 was found to ¡°shape¡± the signaling response. Phosphatase PDE4D tethered to AKAP5 also later reverses within 60£¿s elevated intracellular cyclic AMP levels stimulated by ¦Â-adrenergic agonist. AKAP12, however, fails to attenuate the rise in cyclic AMP over this time. Fusion of the AKAP5 PDE4D-binding-domain to AKAP12 was found to accelerate a reversal of accumulation of intracellular cyclic AMP.AKAPs, which are scaffolds with tethered enzymes, can ¡°shape¡± the temporal and spatial aspects of cell signaling.
%K AKAP5
%K AKAP12
%K AKAR2
%K ¦Â-adrenergic receptor
%K PDE4D
%K Protein kinase A
%K Scaffold
%K Tethered
%U http://www.jmolecularsignaling.com/content/7/1/4/abstract