PRKCA/Q phosphorylate RGS9-1:GN5B:RGS9BP

Stable Identifier
Reaction [transition]
Homo sapiens
PRKCA/Q phosphorylate RGS9-1:GN5B:RGS9BP to form p-S478-RGS9-1:GN5B:RGS9BP
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In bovine experiments, phosphorylation of RGS9-1 (at Ser475, human site predicted to be at Ser478) by protein kinase C (PRKC, specifically the isozymes PRKCalpha and PRKCtheta) significantly decreased the affinity of RGS9-1 for its membrane anchor protein and GAP enhancer RGS9-1 anchor protein (R9S9BP). This represents a potential mechanism for feedback control of the photoresponse recovery in both rods and cones (Sokal et al. 2003, Balasubramanian et al. 2001, Hu et al. 2001).

Literature References
PubMed ID Title Journal Year
11292825 Phosphorylation of RGS9-1 by an endogenous protein kinase in rod outer segments.

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

J Biol Chem 2001
12499365 Identification of protein kinase C isozymes responsible for the phosphorylation of photoreceptor-specific RGS9-1 at Ser475

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

J. Biol. Chem. 2003
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.

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

Biochemistry 2001
Catalyst Activity

protein kinase C activity of PRKCA/Q [photoreceptor disc membrane]

Inferred From
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