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).
Mukhopadhyay, S, Wen, X, Ratti, N, Loktev, A, Rangell, L, Scales, SJ, Jackson, PK
Sassone-Corsi, P
Mukhopadhyay, S, Wen, X, Chih, B, Nelson, CD, Lane, WS, Scales, SJ, Jackson, PK
Mukhopadhyay, S, Rohatgi, R
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