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Structural Mechanism of Demethylation and Inactivation of Protein Phosphatase 2A
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Protein phosphatase 2A (PP2A) is an important serine/threonine phosphatase that plays a role in many biological processes. Reversible carboxyl methylation of the PP2A catalytic subunit is an essential regulatory mechanism for its function. Demethylation and negative regulation of PP2A is mediated by a PP2A-specific methylesterase PME-1, which is conserved from yeast to humans. However, the underlying mechanism of PME-1 function remains enigmatic. Here we report the crystal structures of PME-1 by itself and in complex with a PP2A heterodimeric core enzyme. The structures reveal that PME-1 directly binds to the active site of PP2A and that this interaction results in the activation of PME-1 by rearranging the catalytic triad into an active conformation. Strikingly, these interactions also lead to inactivation of PP2A by evicting the manganese ions that are required for the phosphatase activity of PP2A. These observations identify a dual role of PME-1 that regulates PP2A activation, methylation, and holoenzyme assembly in cells.
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“Carboxymethylation on L309 is reversibly controlled by two PP2A-specific enzymes, leucine carboxy methyltransferase (LCMT-1) and PP2A-specific methylesterase 1 (PME-1) (Stanevich et al., 2011; Xing et al., 2008).”
From PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer (2019) · cites this paper as Xing et al., 2008
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Metadata
- Authors
- Xing, Y., Li, Z., Chen, Y., Stock, J. B., Jeffrey, P. D., & Shi, Y.
- Affiliations
- Princeton University (US)
- Corresponding author
- Shi, Yigong
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2008-04
- Volume
- 133
- Issue
- 1
- Pages
- 154-163
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2012819402
- Cited by
- 206
- References
- 52
- Citations by year
- 2026: 8 · 2025: 10 · 2024: 9 · 2023: 9 · 2022: 11 · 2021: 14 · 2020: 8 · 2019: 12 · 2018: 15 · 2017: 4 · 2016: 17 · 2015: 9 · 2014: 12 · 2013: 9 · 2012: 19
- FWCI
- 5.34
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (K01CA124856, R01CA123155)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- protein phosphatase 2A, PME-1, carboxyl methylation, demethylation, PP2A catalytic subunit, catalytic triad, enzyme activation, enzyme inactivation, holoenzyme assembly, crystal structure
- MeSH terms
- Amino Acid Sequence, Animals, Carboxylic Ester Hydrolases, Humans, Methylation, Models, Molecular, Molecular Sequence Data, Sequence Alignment, Crystallography, X-Ray, Protein Phosphatase 2
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