Protein phosphatase 1 (PP1) is a crucial enzyme involved in cellular processes. It forms complexes with over 200 regulatory proteins, creating highly specific holoenzymes that dephosphorylate numerous biological targets. PP1 plays a critical role in various cellular functions, including cell division, regulation of glycogen metabolism, muscle contractility, and protein synthesis. It also participates in the regulation of ionic conductances and long-term synaptic plasticity. PP1 may contribute significantly to the dephosphorylation of substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. PP1 is a component of the PTW/PP1 phosphatase complex, which plays a vital role in controlling chromatin structure and cell cycle progression during the transition from mitosis to interphase. It regulates the function of NEK2, influencing its kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. PP1 acts as a regulator of neural tube and optic fissure closure, as well as enteric neural crest cell (ENCCs) migration during development. In balance with CSNK1D and CSNK1E, PP1 determines the circadian period length by regulating the speed and rhythmicity of PER1 and PER2 phosphorylation. PP1 may dephosphorylate CSNK1D and CSNK1E. It also dephosphorylates CENPA and the 'Ser-139' residue of ATG16L1, leading to the dissociation of the ATG12-ATG5-ATG16L1 complex and inhibition of autophagy.
Review: The differentially expressed proteins were validated by Western Blot. Compared with adjacent normal tissues, the protein expression of PTMA, PAK2, PPP1CA, HMGB2 were up-regulated.
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