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Appears in Networks 2

In-Edges 2

act(p(HGNC:PPP2R1A)) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A)) View Subject | View Object

First, conformational flexibility of the scaffold subunit is required for binding to the catalytic subunit and possibly other interacting proteins such as the regulatory subunits. PubMed:19277525

p(HGNC:PPP2R1A, pmod(Ph, Ser), pmod(Ph, Thr)) decreases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A)) View Subject | View Object

A recent report also indicates the existence of regulated phosphorylation of the scaffolding A subunit on Ser/Thr residues, which affects its binding to the catalytic subunit and PP2A signaling in the heart (Kotlo et al.,2014). PubMed:24653673

Out-Edges 4

complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A)) decreases p(HGNC:MAPT, pmod(Ph)) View Subject | View Object

The specificity in this in vitro system is quite robust, as evidenced by the observation that the PP2A core enzyme exhibited a lower activity to dephosphorylate the Tau protein than the PP2A holoenzyme involving the B subunit, but a higher activity than the holoenzyme involving the B′ subunit PubMed:19277525

complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A)) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55")) View Subject | View Object

In fact, competition experiments using recombinant proteins suggested that, compared to the unmethylated form, the methylated PP2A core enzyme exhibited a higher binding affinity for the B subunit PubMed:19277525


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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.