Ppp1Ca Gene is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
{{Infobox gene
| symbol = PPP1CA
| name = Protein Phosphatase 1 Catalytic Subunit Alpha
| chromosome = 11
| locus = 11q13.2
| geneID = 5499
| omim = 176875
| ensembl = ENSG00000172531
| uniprot = P62136
| uniprot_name = PPP1CA
| diseases = Alzheimer's Disease, Parkinson's Disease, Spinocerebellar Ataxia
| diseases_ref = Braithwaite et al., 2012, Nat Rev Neurosci
}}
Protein phosphatase 1 catalytic subunit alpha (PPP1CA) is one of three catalytic subunits of protein phosphatase 1 (PP1), a major serine/threonine phosphatase that regulates numerous cellular processes. The PPP1CA gene is located on chromosome 11q13.4 and encodes a protein of 330 amino acids. PPP1CA is ubiquitously expressed and plays critical roles in glycogen metabolism, muscle contraction, synaptic plasticity, and cell division. In neurons, PPP1CA regulates tau phosphorylation, dopamine signaling, and circadian rhythm through dephosphorylation of target proteins. Dysregulation of PPP1CA is implicated in Alzheimer's disease, Parkinson's disease, and spinocerebellar ataxia. The enzyme's activity is regulated by inhibitor proteins and targeting subunits that direct it to specific substrates.
Protein phosphatase 1 catalytic subunit alpha (PPP1CA) is one of three catalytic subunits of protein phosphatase 1 (PP1), a major serine/threonine phosphatase involved in the regulation of numerous cellular processes. PPP1CA is ubiquitously expressed and participates in diverse signaling pathways.
PPP1CA removes phosphate groups from serine and threonine residues:
In neurons, PPP1CA is crucial for:
PPP1CA dephosphorylates tau protein:
PPP1CA is dysregulated in AD:
PPP1CA contributes to PD through:
PPP1CA variants cause SCA:
PPP1CA is expressed in:
In neurons, PPP1CA is localized to:
The study of Ppp1Ca Gene has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
Banzhaf-Strathmann J et al.. "MicroRNA-125b induces tau hyperphosphorylation and cognitive deficits in Alzheimer's disease." The EMBO journal (2014) DOI:10.15252/embj.201387576
Bunik V et al.. "Thiamine-dependent regulation of mammalian brain pyridoxal kinase in vitro and in vivo." Journal of neurochemistry (2022) DOI:10.1111/jnc.15576
Wang P et al.. "PP1A-mediated dephosphorylation positively regulates YAP2 activity." PloS one (2011) DOI:10.1371/journal.pone.0024288
Benatti C et al.. "Modulation of neuroplasticity-related targets following stress-induced acute escape deficit." Behavioural brain research (2019) DOI:10.1016/j.bbr.2019.02.023
Shastry AH et al.. "Nuclear Protein Phosphatase 1 α (PP1A) Expression is Associated with Poor Prognosis in p53 Expressing Glioblastomas." Pathology oncology research : POR (2016) DOI:10.1007/s12253-015-9928-5
Kawano S et al.. "A cell-based screening for TAZ activators identifies ethacridine, a widely used antiseptic and abortifacient, as a compound that promotes dephosphorylation of TAZ and inhibits adipogenesis in C3H10T1/2 cells." Journal of biochemistry (2015) DOI:10.1093/jb/mvv051
Kakiya N et al.. "Cell surface expression of the major amyloid-β peptide (Aβ)-degrading enzyme, neprilysin, depends on phosphorylation by mitogen-activated protein kinase/extracellular signal-regulated kinase kinase (MEK) and dephosphorylation by protein phosphatase 1a." The Journal of biological chemistry (2012) DOI:10.1074/jbc.M112.340372