PkCa/q phosphorylate Rgs9-1:Gn5b:R9s9bp

Stable Identifier
R-BTA-74618
Type
Reaction [transition]
Species
Bos taurus
Compartment
Synonyms
PkCa/q phosphorylate Rgs9-1:Gn5b:R9s9bp to form p-475-Rgs9-1:Gn5b:R9s9bp
General
SVG |   | PPTX  | SBGN
PkCa/q phosphorylate Rgs9-1:Gn5b:R9s9bp

RGS9-1 is phosphorylated in darkness at Ser475 by protein kinase C (PRKC, specifically the isozymes PRKCalpha and PRKCtheta). Phosphorylation significantly decreases the affinity of RGS9 for RGS9-1 anchor protein (R9S9BP) thus representing a potential mechanism for feedback control of the kinetics of photoresponse recovery in both rods and cones (Sokal et al. 2003, Balasubramanian et al. 2001, Hu et al. 2001). Dephosphorylation is mediated by protein phosphatase 2A.

Literature References
PubMed ID Title Journal Year
12499365 Identification of protein kinase C isozymes responsible for the phosphorylation of photoreceptor-specific RGS9-1 at Ser475

Sokal, I, Hu, G, Liang, Y, Mao, M, Wensel, TG, Palczewski, K

J. Biol. Chem. 2003
11292825 Phosphorylation of RGS9-1 by an endogenous protein kinase in rod outer segments.

Hu, G, Jang, GF, Cowan, CW, Wensel, TG, Palczewski, K

J Biol Chem 2001
11601986 Phosphorylation of the regulator of G protein signaling RGS9-1 by protein kinase A is a potential mechanism of light- and Ca2+-mediated regulation of G protein function in photoreceptors.

Balasubramanian, N, Levay, K, Keren-Raifman, T, Faurobert, E, Slepak, VZ

Biochemistry 2001
Participants
Catalyst Activity

protein serine/threonine kinase activity of PrkCa/q [photoreceptor disc membrane]

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