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TitleCryo-EM structures reveal the PP2A-B55α and Eya3 interaction that can be disrupted by a peptide inhibitor.
Journal, issue, pagesJ Biol Chem, Vol. 301, Issue 7, Page 110287, Year 2025
Publish dateMay 23, 2025
AuthorsShasha Shi / Xueni Li / Christopher Alderman / Lars Wick / Wei Huang / North Foulon / Lingdi Zhang / John Rossi / Wenxin Hu / Shouqing Cui / Hongjin Zheng / Derek J Taylor / Heide L Ford / Rui Zhao /
PubMed AbstractWe have previously shown that Eya3 recruits PP2A-B55α to dephosphorylate pT58 on Myc, increasing Myc stability and enhancing primary tumor growth of triple-negative breast cancer (TNBC). However, ...We have previously shown that Eya3 recruits PP2A-B55α to dephosphorylate pT58 on Myc, increasing Myc stability and enhancing primary tumor growth of triple-negative breast cancer (TNBC). However, the molecular details of how Eya3 recruits PP2A-B55α remain unclear. Here, we determined the cryo-EM structures of PP2A-B55α bound with Eya3, with an inhibitory peptide B55i, and in its unbound state. These studies demonstrate that Eya3 binds B55α through an extended peptide in the N-terminal domain of Eya3. The Eya3 peptide, PP2A-B55α substrates, and protein-peptide inhibitors including B55i bind to a similar area on the B55α surface, but the molecular details of the binding differ. We further demonstrated that the B55i peptide inhibits the B55α and Eya3 interaction in vitro. The B55i peptide expressed on a plasmid increases Myc pT58 and decreases Myc protein levels in TNBC cells, suggesting the potential of B55i or similar peptides as therapies for TNBC.
External linksJ Biol Chem / PubMed:40414499 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 3.71 Å
Structure data

48798

9n0y

EMDB-48798, PDB-9n0y:
PP2A-B55 Holoenzyme with Eya3
Method: EM (single particle) / Resolution: 3.71 Å

48799

9n0z

EMDB-48799, PDB-9n0z:
PP2A-B55 Holoenzyme with B55i
Method: EM (single particle) / Resolution: 3.5 Å

Source
  • homo sapiens (human)
KeywordsONCOPROTEIN / Ser/Thr phosphatase / complex / Myc stabilization / ONCOPROTEIN/INHIBITOR / Phosphatase / EYA family / peptide inhibitor / ONCOPROTEIN-INHIBITOR complex

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