cAMP is a known regulator of PKA activity and works by binding to the regulatory subunits and promoting dissociation of the tetramer, freeing the active catalytic subunits (reviewed in Sassone-Corsi, 2012). In the Hh pathway in the absence of ligand, cAMP levels increase in response to the recruitment of GPR161 to the ciliary base by TULP3 and the IFT-A retrograde complex (Mukhopadhyay et al, 2010; Mukhopadhyay et al, 2013). Activated PKA then initiates the phosphorylation cascade that regulates processing and/or degradation of the GLI proteins (reviewed in Briscoe and Therond, 2013; Mukhopadhyay and Rohatgi, 2014).
Sassone-Corsi, P
Scales, SJ, Wen, X, Rangell, L, Jackson, PK, Loktev, A, Mukhopadhyay, S, Ratti, N
Lane, WS, Scales, SJ, Wen, X, Chih, B, Jackson, PK, Nelson, CD, Mukhopadhyay, S
Rohatgi, R, Mukhopadhyay, S
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