The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs
Open accessAbstract
The PR65/A subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit, generating functionally diverse heterotrimers. Mutations of the beta isoform of PR65 are associated with lung and colon tumors. The crystal structure of the PR65/Aalpha subunit, at 2.3 A resolution, reveals the conformation of its 15 tandemly repeated HEAT sequences, degenerate motifs of approximately 39 amino acids present in a variety of proteins, including huntingtin and importin beta. Individual motifs are composed of a pair of antiparallel alpha helices that assemble in a mainly linear, repetitive fashion to form an elongated molecule characterized by a double layer of alpha helices. Left-handed rotations at three interrepeat interfaces generate a novel left-hand superhelical conformation. The protein interaction interface is formed from the intrarepeat turns that are aligned to form a continuous ridge.
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The PP2A scaffold has 15 tandem HEAT repeats, each made of two antiparallel α-helices, and these repeats form an elongated horseshoe-shaped structure.
“Structural analysis has revealed that the PP2A scaffold subunit contains 15 tandem HEAT (huntingtin-elongation-A subunit-TOR) repeats, each of which is made up of a pair of antiparallel α-helices (Fig. 1A). These HEAT repeats come together to form an elongated, horseshoe-shaped structure (Groves et al., 1999).”
From PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer (2019) · cites this paper as Groves et al., 1999
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References 64 · Cited by 442
- Authors
- Groves, M. R., Hanlon, N., Turowski, P., Hemmings, B. A., & Barford, D.
- Affiliations
- University of Oxford (GB)
- Friedrich Miescher Institute (CH)
- Corresponding author
- Barford, David
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1999-01
- Volume
- 96
- Issue
- 1
- Pages
- 99-110
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2125617798
- Cited by
- 442
- References
- 64
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 6 · 2023: 13 · 2022: 8 · 2021: 10 · 2020: 6 · 2019: 12 · 2018: 10 · 2017: 11 · 2016: 12 · 2015: 13 · 2014: 17 · 2013: 21 · 2012: 12
- FWCI
- 13.46
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Science and Technology Facilities Council (submittedVersion)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- protein phosphatase 2A, HEAT repeats, crystal structure, scaffold proteins, heterotrimers, protein-protein interfaces
- MeSH terms
- Adenocarcinoma, Amino Acid Sequence, Binding Sites, Humans, Molecular Sequence Data, Mutation, Phosphoprotein Phosphatases, Plant Proteins, Protein Conformation, Conserved Sequence, Tandem Repeat Sequences, Catalytic Domain, Protein Phosphatase 2
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