phosphatase-1 (PP1)
Jump to navigation
Jump to search
Function
- protein phosphatase 1 (PP1) is essential for cell division, & participates in the regulation of glycogen metabolism, muscle contractility & protein synthesis
- involved in regulation of ionic conductances & long-term synaptic plasticity
- may play a role in dephosphorylating substrates such as the postsynaptic density-associated CaM kinase 2
- exhibits broad specificity, partly overlapping with protein phosphatase 2A
Inhibition:
- inhibited by calyculin A[3] & akadaic acid
phosphoprotein + H2O = a protein + phosphate Struture:
- PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 & glycogen synthetase kinase 3, & then complexed to one or several targeting or regulatory subunits
- PPP1R12A, PPP1R12B & PPP1R12C mediate binding to myosin
- PPP1R3A, PPP1R3B, PPP1R3C & PPP1R3D mediate binding to glycogen
- PPP1R15A & PPP1R15B mediate binding to EIF2S1
Compartment
- cytoplasm, nucleus, nucleoplasm, nucleolus
- primarily nuclear & largely excluded from the nucleolus
- highly mobile in cells & can be relocalized through interaction with targeting subunits
Notes
- related complexes
More general terms
More specific terms
Additional terms
References
- ↑ UniProt http://www.uniprot.org/uniprot/P62136.html
- ↑ Armstrong DL Calcium channel regulation by calcineurin, a Ca2+-activated phosphatase in mammalian brain. TINS 12(3):117 1989 PMID: https://www.ncbi.nlm.nih.gov/pubmed/2469218
- ↑ 3.0 3.1 Denton RM. Insulin signalling: search for the missing links. Nature. 1990 Nov 22;348(6299):286-7. PMID: https://www.ncbi.nlm.nih.gov/pubmed/2250701
- ↑ Kosik KS, Shimura H. Phosphorylated tau and the neurodegenerative foldopathies. Biochim Biophys Acta. 2005 Jan 3;1739(2-3):298-310. Epub 2004 Nov 26. Review. PMID: https://www.ncbi.nlm.nih.gov/pubmed/15615647