5zt0

Structural highlights

Function

[PP1A_MOUSE] Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. 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. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. 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 CENPA (By similarity). Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1 complex, thereby inhibiting autophagy (By similarity).[UniProtKB:P62136]^{[1] [2] [3] [4]} [PPR3B_HUMAN] Acts as a glycogen-targeting subunit for phosphatase PP1. Facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. Suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by PYGL, resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in hepatocytes (By similarity).

References

1. ↑ Kim TH, Goodman J, Anderson KV, Niswander L. Phactr4 regulates neural tube and optic fissure closure by controlling PP1-, Rb-, and E2F1-regulated cell-cycle progression. Dev Cell. 2007 Jul;13(1):87-102. doi: 10.1016/j.devcel.2007.04.018. PMID:17609112 doi:http://dx.doi.org/10.1016/j.devcel.2007.04.018
2. ↑ Schmutz I, Wendt S, Schnell A, Kramer A, Mansuy IM, Albrecht U. Protein phosphatase 1 (PP1) is a post-translational regulator of the mammalian circadian clock. PLoS One. 2011;6(6):e21325. doi: 10.1371/journal.pone.0021325. Epub 2011 Jun 21. PMID:21712997 doi:http://dx.doi.org/10.1371/journal.pone.0021325
3. ↑ Lee HM, Chen R, Kim H, Etchegaray JP, Weaver DR, Lee C. The period of the circadian oscillator is primarily determined by the balance between casein kinase 1 and protein phosphatase 1. Proc Natl Acad Sci U S A. 2011 Sep 27;108(39):16451-6. doi:, 10.1073/pnas.1107178108. Epub 2011 Sep 19. PMID:21930935 doi:http://dx.doi.org/10.1073/pnas.1107178108
4. ↑ Zhang Y, Kim TH, Niswander L. Phactr4 regulates directional migration of enteric neural crest through PP1, integrin signaling, and cofilin activity. Genes Dev. 2012 Jan 1;26(1):69-81. doi: 10.1101/gad.179283.111. PMID:22215812 doi:http://dx.doi.org/10.1101/gad.179283.111
5. ↑ Yu J, Deng T, Xiang S. Structural basis for protein phosphatase 1 recruitment by glycogen-targeting subunits. FEBS J. 2018 Dec;285(24):4646-4659. doi: 10.1111/febs.14699. Epub 2018 Nov 28. PMID:30422398 doi:http://dx.doi.org/10.1111/febs.14699