Structural basis of protein phosphatase 2A stable latency
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The catalytic subunit of protein phosphatase 2A (PP2Ac) is stabilized in a latent form by α4, a regulatory protein essential for cell survival and biogenesis of all PP2A complexes. Here we report the structure of α4 bound to the N-terminal fragment of PP2Ac. This structure suggests that α4 binding to the full-length PP2Ac requires local unfolding near the active site, which perturbs the scaffold subunit binding site at the opposite surface via allosteric relay. These changes stabilize an inactive conformation of PP2Ac and convert oligomeric PP2A complexes to the α4 complex upon perturbation of the active site. The PP2Ac–α4 interface is essential for cell survival and sterically hinders a PP2A ubiquitination site, important for the stability of cellular PP2Ac. Our results show that α4 is a scavenger chaperone that binds to and stabilizes partially folded PP2Ac for stable latency, and reveal a mechanism by which α4 regulates cell survival, and biogenesis and surveillance of PP2A holoenzymes. The protein α4 is essential for the formation, stability and activity of protein phosphatase 2A (PP2A) complexes. Here the authors solve the crystal structure of a truncated PP2A bound to α4 and show that α4 binds to a partially folded form of the protein, stabilizing the enzyme in an inactive state.
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α4 binds partially folded PP2A/C, stabilizing it in a latent state and preventing its ubiquitination and degradation by MID1.
“It has been shown that partially folded PP2A/C is stabilized for latency by the binding of α4, which in part prevents its ubiquitination and subsequent degradation by Midline 1 (MID1) (Jiang et al., 2013; Liu et al., 2001; Short et al., 2002).”
From PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer (2019) · cites this paper as Jiang et al., 2013
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- Authors
- Jiang, L., Stanevich, V., Satyshur, K. A., Kong, M., Watkins, G. R., Wadzinski, B. E., Sengupta, R., & Xing, Y.
- Affiliations
- University of Wisconsin–Madison (US)
- City Of Hope National Medical Center (US)
- Vanderbilt University (US)
- Corresponding author
- Xing, Yongna
- Venue
- Nature Communications
- Published
- 2013-04-16
- Volume
- 4
- Issue
- 1
- Pages
- 1699-1699
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC3644067
- OpenAlex
- W1993512412
- Cited by
- 68
- References
- 43
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 6 · 2023: 3 · 2022: 9 · 2021: 6 · 2020: 2 · 2019: 5 · 2018: 5 · 2017: 7 · 2016: 7 · 2015: 4 · 2014: 9 · 2013: 1
- FWCI
- 3.13
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Nature Communications (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- University of Wisconsin-Madison
- National Institutes of Health (GM051366)
- National Cancer Institute (K01CA124856)
- National Institute of General Medical Sciences (R01GM051366, R01GM096060)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- protein phosphatase 2A, PP2A catalytic subunit, allosteric regulation, ubiquitination sites, molecular chaperones, cell survival, protein stability
- MeSH terms
- Crystallization, Enzyme Stability, Models, Molecular, Protein Conformation, Catalytic Domain, Protein Phosphatase 2, Ubiquitination
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