Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Definition:

Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective.

References:

[1]. Jeong-Heon Lee, et al. Identification and characterization of a novel human PP1 phosphatase complex. J Biol Chem. 2010 Aug 6;285(32):24466-76. [Content Brief]

[2]. Isabelle Schmutz, et al. Protein phosphatase 1 (PP1) is a post-translational regulator of the mammalian circadian clock. PLoS One. 2011;6(6):e21325. [Content Brief]

[3]. Hong Nie, et al. Phosphorylation of FOXP3 controls regulatory T cell function and is inhibited by TNF-α in rheumatoid arthritis. Nat Med. 2013 Mar;19(3):322-8. [Content Brief]

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