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RNA silencing identifies PDE4D5 as the functionally relevant cAMP phosphodiesterase interacting with beta arrestin to control the protein kinase A/AKAP79-mediated switching of the beta2-adrenergic receptor to activation of ERK in HEK293B2 cells.
Lynch MJ, Baillie GS, Mohamed A, Li X, Maisonneuve C, Klussmann E, van Heeke G, Houslay MD. Lynch MJ, et al. Among authors: li x. J Biol Chem. 2005 Sep 30;280(39):33178-89. doi: 10.1074/jbc.M414316200. Epub 2005 Jul 19. J Biol Chem. 2005. PMID: 16030021 Free article.
1H NMR structural and functional characterisation of a cAMP-specific phosphodiesterase-4D5 (PDE4D5) N-terminal region peptide that disrupts PDE4D5 interaction with the signalling scaffold proteins, beta-arrestin and RACK1.
Smith KJ, Baillie GS, Hyde EI, Li X, Houslay TM, McCahill A, Dunlop AJ, Bolger GB, Klussmann E, Adams DR, Houslay MD. Smith KJ, et al. Among authors: li x. Cell Signal. 2007 Dec;19(12):2612-24. doi: 10.1016/j.cellsig.2007.08.015. Epub 2007 Sep 1. Cell Signal. 2007. PMID: 17900862
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