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TitleMolecular mechanism of PP2A/B55α phosphatase inhibition by IER5.
Journal, issue, pagesCell Chem Biol, Vol. 32, Issue 4, Page 631-642.e7, Year 2025
Publish dateApr 17, 2025
AuthorsRuili Cao / Daniel T D Jones / Li Pan / Annie Yang / Shumei Wang / Sathish K R Padi / Shaun Rawson / Jon C Aster / Stephen C Blacklow /
PubMed AbstractPP2A serine/threonine phosphatases are heterotrimeric complexes that execute many essential physiologic functions. These activities are modulated by additional regulatory proteins, such as ARPP19, ...PP2A serine/threonine phosphatases are heterotrimeric complexes that execute many essential physiologic functions. These activities are modulated by additional regulatory proteins, such as ARPP19, FAM122A, and IER5. Here, we report the cryoelectron microscopy (cryo-EM) structure of a complex of PP2A/B55α with the N-terminal structured region of IER5 (IER5-N50), which occludes a surface on B55α used for substrate recruitment, and show that IER5-N50 inhibits PP2A/B55α catalyzed dephosphorylation of pTau in biochemical assays. Mutations of full-length IER5 that disrupt its PP2A/B55α interface interfere with co-immunoprecipitation of PP2A/B55α. IER5 antagonism of B55α in keratinocytes is required for expression of KRT1, a differentiation marker. Mini-IER5 composed of IER5-N50 and a nuclear localization sequence restores this activity in IER5 knockout cells. Using structural bioinformatics, we identify homology of IER5-N50 with SERTA (SEI-1, RBT-1, and TARA) domain containing proteins. These studies define the molecular basis of PP2A/B55α nuclear inhibition by IER5 and suggest a roadmap for selective pharmacologic modulation of PP2A/B55α complexes.
External linksCell Chem Biol / PubMed:40209703 / PubMed Central
MethodsEM (single particle)
Resolution3.27 Å
Structure data

42428

8uo5

EMDB-42428, PDB-8uo5:
Protein Phosphatase 2A B55 subunit in complex with IER5
Method: EM (single particle) / Resolution: 3.27 Å

Chemicals

ChemComp-FE:
Unknown entry

ChemComp-ZN:
Unknown entry

Source
  • Spodoptera frugiperda (fall armyworm)
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / Phosphatase / complex

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