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- W2626382019 abstract "ARPP-16, ARPP-19, and ENSA are inhibitors of protein phosphatase PP2A. ARPP-19 and ENSA phosphorylated by Greatwall kinase inhibit PP2A during mitosis. ARPP-16 is expressed in striatal neurons where basal phosphorylation by MAST3 kinase inhibits PP2A and regulates key components of striatal signaling. The ARPP-16/19 proteins were discovered as substrates for PKA, but the function of PKA phosphorylation is unknown. We find that phosphorylation by PKA or MAST3 mutually suppresses the ability of the other kinase to act on ARPP-16. Phosphorylation by PKA also acts to prevent inhibition of PP2A by ARPP-16 phosphorylated by MAST3. Moreover, PKA phosphorylates MAST3 at multiple sites resulting in its inhibition. Mathematical modeling highlights the role of these three regulatory interactions to create a switch-like response to cAMP. Together, the results suggest a complex antagonistic interplay between the control of ARPP-16 by MAST3 and PKA that creates a mechanism whereby cAMP mediates PP2A disinhibition." @default.
- W2626382019 created "2017-06-23" @default.
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- W2626382019 date "2017-06-14" @default.
- W2626382019 modified "2023-10-17" @default.
- W2626382019 title "Reciprocal regulation of ARPP-16 by PKA and MAST3 kinases provides a cAMP-regulated switch in protein phosphatase 2A inhibition" @default.
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- W2626382019 doi "https://doi.org/10.7554/elife.24998" @default.
- W2626382019 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5515580" @default.
- W2626382019 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28613156" @default.
- W2626382019 hasPublicationYear "2017" @default.
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