A dynamic charge-charge interaction modulates PP2A:B56 substrate recruitment
Open accessAbstract
The recruitment of substrates by the ser/thr protein phosphatase 2A (PP2A) is poorly understood, limiting our understanding of PP2A-regulated signaling. Recently, the first PP2A:B56 consensus binding motif, LxxIxE, was identified. However, most validated LxxIxE motifs bind PP2A:B56 with micromolar affinities, suggesting that additional motifs exist to enhance PP2A:B56 binding. Here, we report the requirement of a positively charged motif in a subset of PP2A:B56 interactors, including KIF4A, to facilitate B56 binding via dynamic, electrostatic interactions. Using molecular and cellular experiments, we show that a conserved, negatively charged groove on B56 mediates dynamic binding. We also discovered that this positively charged motif, in addition to facilitating KIF4A dephosphorylation, is essential for condensin I binding, a function distinct and exclusive from PP2A-B56 binding. Together, these results reveal how dynamic, charge-charge interactions fine-tune the interactions mediated by specific motifs, providing a new framework for understanding how PP2A regulation drives cellular signaling.
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An acidic patch between B56α amino acids E301-E341 is an additional determinant for high-affinity binding of LxxIxE substrates to B56α.
“the recently identified additional determinant for high affinity binding of LxxIxE substrates to B56α, an acidic patch between B56α amino acids E301-E34142”
From Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A (2023) · cites this paper as [42]
The Results section identifies an acidic patch adjacent to the LxxIxE-binding pocket and shows that it enhances binding for a subset of B56 interactors. Figure 3 identifies B56α E301, E335 and D338 as acidic-patch residues, but our copy does not establish E341 as a boundary. The claim also omits the paper’s qualification that this mechanism applies to a subset of substrates. (LLM, conf=0.83)
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Emerging Roles of B56 Phosphorylation and Binding Motif in PP2A-B56 Holoenzyme Biological Function
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Specificity determinants of phosphoprotein phosphatases controlling kinetochore functions
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An Aurora kinase A-BOD1L1-PP2A B56 axis promotes chromosome segregation fidelity
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Self-citationMRBLE-pep Measurements Reveal Accurate Binding Affinities for B56, a PP2A Regulatory Subunit
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Deep learning molecular interaction motifs from receptor structures alone
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Structural and biochemical studies of human PP2A(B55) holoenzyme and ENSA protein complexPreprint
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A busy BOD1-y: the diverse functions of an intracellular signaling regulatory protein family
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- Authors
- Wang, X., Garvanska, D. H., Nasa, I., Ueki, Y., Zhang, G., Kettenbach, A. N., Peti, W., Nilsson, J., & Page, R.
- Affiliations
- University of Arizona (US)
- University of Copenhagen (DK)
- Dartmouth College (US)
- Corresponding author
- Nilsson, Jakob
- Page, Rebecca
- ORCID
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2020-03-20
- Volume
- 9
- ISSN
- 2050-084X (ISSN-L)
- PMC
- PMC7108865
- OpenAlex
- W3012005750
- Cited by
- 53
- References
- 60
- Citations by year
- 2026: 2 · 2025: 11 · 2024: 9 · 2023: 7 · 2022: 7 · 2021: 14 · 2020: 3
- FWCI
- 2.51
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- eLife (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, cc-by)
- UA Campus Repository (The University of Arizona) (acceptedVersion, cc-by)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Apollo (University of Cambridge) (submittedVersion, cc-by)
- Apollo (cc-by)
- Funders
- National Institute of General Medical Sciences (R35GM119455, P20GM113132, R01GM098482, R01GM134683)
- National Institute of Neurological Disorders and Stroke (R01NS091336)
- Novo Nordisk (NNF14CC0001)
- Independent Research Fund Denmark (DFF-7016-00086)
- 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 › Molecular Biology › Signaling Pathways in Disease
- Keywords
- PP2A-B56, protein phosphatase 2A, substrate recruitment, charge-charge interactions, electrostatic interactions, KIF4A, condensin I, protein dephosphorylation, protein-protein binding
- MeSH terms
- Amino Acid Sequence, Cloning, Molecular, Gene Expression Regulation, HeLa Cells, Humans, Models, Molecular, Mutation, Protein Conformation, Substrate Specificity, Kinesins, RNA Interference, Protein Phosphatase 2
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