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TitleCryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19.
Journal, issue, pagesNature, Vol. 625, Issue 7993, Page 195-203, Year 2024
Publish dateDec 20, 2023
AuthorsSathish K R Padi / Margaret R Vos / Rachel J Godek / James R Fuller / Thomas Kruse / Jamin B Hein / Jakob Nilsson / Matthew S Kelker / Rebecca Page / Wolfgang Peti /
PubMed AbstractProgression through the cell cycle is controlled by regulated and abrupt changes in phosphorylation. Mitotic entry is initiated by increased phosphorylation of mitotic proteins, a process driven by ...Progression through the cell cycle is controlled by regulated and abrupt changes in phosphorylation. Mitotic entry is initiated by increased phosphorylation of mitotic proteins, a process driven by kinases, whereas mitotic exit is achieved by counteracting dephosphorylation, a process driven by phosphatases, especially PP2A:B55. Although the role of kinases in mitotic entry is well established, recent data have shown that mitosis is only successfully initiated when the counterbalancing phosphatases are also inhibited. Inhibition of PP2A:B55 is achieved by the intrinsically disordered proteins ARPP19 and FAM122A. Despite their critical roles in mitosis, the mechanisms by which they achieve PP2A:B55 inhibition is unknown. Here, we report the single-particle cryo-electron microscopy structures of PP2A:B55 bound to phosphorylated ARPP19 and FAM122A. Consistent with our complementary NMR spectroscopy studies, both intrinsically disordered proteins bind PP2A:B55, but do so in highly distinct manners, leveraging multiple distinct binding sites on B55. Our extensive structural, biophysical and biochemical data explain how substrates and inhibitors are recruited to PP2A:B55 and provide a molecular roadmap for the development of therapeutic interventions for PP2A:B55-related diseases.
External linksNature / PubMed:38123684 / PubMed Central
MethodsEM (single particle)
Resolution2.55 - 2.79961 Å
Structure data

40644

8so0

EMDB-40644, PDB-8so0:
Cryo-EM structure of the PP2A:B55-FAM122A complex
Method: EM (single particle) / Resolution: 2.79961 Å

41604

8ttb

EMDB-41604, PDB-8ttb:
Cryo-EM structure of the PP2A:B55-ARPP19 complex
Method: EM (single particle) / Resolution: 2.77 Å

41667

8twe

EMDB-41667, PDB-8twe:
Cryo-EM structure of the PP2A:B55-FAM122A complex, B55 body
Method: EM (single particle) / Resolution: 2.55 Å

41668

8twi

EMDB-41668, PDB-8twi:
Cryo-EM structure of the PP2A:B55-FAM122A complex, PP2Ac body
Method: EM (single particle) / Resolution: 2.69 Å

Chemicals

ChemComp-FE:
Unknown entry

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / Protein Phosphatase 2A:B55 holoenzyme FAM122A inhibitor substrate binding cell cycle regulation / HYDROLASE / Protein Phosphatase 2A:B55 holoenzyme / ARPP19 inhibitor / cell cycle regulation

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