Interrogating PP1 activity in the MAPK pathway with optimized PP1-disrupting peptides
Protein phosphatase-1 (PP1)-disrupting peptides (PDPs) are selective chemical modulators of PP1 that liberate the active PP1 catalytic subunit from regulatory proteins; thus allowing the dephosphorylation of nearby substrates. We have optimized the original cell-active PDP3 for enhanced stability, a...
Gespeichert in:
| Hauptverfasser: | , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
2019
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| In: |
ChemBioChem
Year: 2018, Jahrgang: 20, Heft: 1, Pages: 66-71 |
| ISSN: | 1439-7633 |
| DOI: | 10.1002/cbic.201800541 |
| Online-Zugang: | Verlag, Volltext: http://dx.doi.org/10.1002/cbic.201800541
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| Verfasserangaben: | Yansong Wang, Bernhard Hoermann, Karolina Pavic, Malgorzata Trebacz, Pablo Rios, Maja Köhn |
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| 245 | 1 | 0 | |a Interrogating PP1 activity in the MAPK pathway with optimized PP1-disrupting peptides |c Yansong Wang, Bernhard Hoermann, Karolina Pavic, Malgorzata Trebacz, Pablo Rios, Maja Köhn |
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| 520 | |a Protein phosphatase-1 (PP1)-disrupting peptides (PDPs) are selective chemical modulators of PP1 that liberate the active PP1 catalytic subunit from regulatory proteins; thus allowing the dephosphorylation of nearby substrates. We have optimized the original cell-active PDP3 for enhanced stability, and obtained insights into the chemical requirements for stabilizing this 23-mer peptide for cellular applications. The optimized PDP-Nal was used to dissect the involvement of PP1 in the MAPK signaling cascade. Specifically, we have demonstrated that, in human osteosarcoma (U2OS) cells, phosphoMEK1/2 is a direct substrate of PP1, whereas dephosphorylation of phosphoERK1/2 is indirect and likely mediated through enhanced tyrosine phosphatase activity after PDP-mediated PP1 activation. Thus, as liberators of PP1 activity, PDPs represent a valuable tool for identifying the substrates of PP1 and understanding its role in diverse signaling cascades. | ||
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