Autor: |
Jason S. Wasserman, Felicity Feiser, Seren Palacio, Kishan Patel, Joy Gonzalez, Holly Fowle, Xavier Graña |
Jazyk: |
angličtina |
Rok vydání: |
2023 |
Předmět: |
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Zdroj: |
STAR Protocols, Vol 4, Iss 2, Pp 102148- (2023) |
Druh dokumentu: |
article |
ISSN: |
2666-1667 |
DOI: |
10.1016/j.xpro.2023.102148 |
Popis: |
Summary: Serine/threonine protein phosphatase 2 (PP2A) forms heterotrimeric holoenzymes, where a scaffold subunit bridges the PP2A catalytic subunit to a B regulatory subunit, e.g., B55α. The PP2A/B55α holoenzyme plays key roles in signaling and cell-cycle control targeting multiple substrates. Here, we describe semiquantitative approaches to determine PP2A/B55α substrate specificity. Parts I and II detail approaches to assess PP2A/B55α-mediated dephosphorylation of immobilized substrate peptide variants. Parts III and IV detail methods to assess PP2A/B55α-substrate-binding specificity. These approaches are adaptable to other serine/threonine phosphatases.For complete details on the use and execution of this protocol, please refer to Fowle et al..1 : Publisher’s note: Undertaking any experimental protocol requires adherence to local institutional guidelines for laboratory safety and ethics. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
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