BAIT

PPP1R3C

PTG, Ppp1r5
protein phosphatase 1, regulatory (inhibitor) subunit 3C
GO Process (3)
GO Function (3)
GO Component (4)
Mus musculus
PREY

PRKAA2

2310008I11Rik, A830082D05, AMPKalpha2, RP23-431F3.2
protein kinase, AMP-activated, alpha 2 catalytic subunit
Mus musculus

Affinity Capture-Western

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Publication

AMP-activated protein kinase phosphorylates R5/PTG, the glycogen targeting subunit of the R5/PTG-protein phosphatase 1 holoenzyme, and accelerates its down-regulation by the laforin-malin complex.

Vernia S, Solaz-Fuster MC, Gimeno-Alcaniz JV, Rubio T, Garcia-Haro L, Foretz M, de Cordoba SR, Sanz P

R5/PTG is one of the glycogen targeting subunits of type 1 protein phosphatase, a master regulator of glycogen synthesis. R5/PTG recruits the phosphatase to the places where glycogen synthesis occurs, allowing the activation of glycogen synthase and the inactivation of glycogen phosphorylase, thus increasing glycogen synthesis and decreasing its degradation. In this report, we show that the activity of R5/PTG ... [more]

J. Biol. Chem. Mar. 27, 2009; 284(13);8247-55 [Pubmed: 19171932]

Throughput

  • Low Throughput

Curated By

  • BioGRID