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TitleCoupling to short linear motifs creates versatile PME-1 activities in PP2A holoenzyme demethylation and inhibition.
Journal, issue, pagesElife, Vol. 11, Year 2022
Publish dateAug 4, 2022
AuthorsYitong Li / Vijaya Kumar Balakrishnan / Michael Rowse / Cheng-Guo Wu / Anastasia Phoebe Bravos / Vikash K Yadav / Ylva Ivarsson / Stefan Strack / Irina V Novikova / Yongna Xing /
PubMed AbstractProtein phosphatase 2A (PP2A) holoenzymes target broad substrates by recognizing short motifs via regulatory subunits. PP2A methylesterase 1 (PME-1) is a cancer-promoting enzyme and undergoes ...Protein phosphatase 2A (PP2A) holoenzymes target broad substrates by recognizing short motifs via regulatory subunits. PP2A methylesterase 1 (PME-1) is a cancer-promoting enzyme and undergoes methylesterase activation upon binding to the PP2A core enzyme. Here, we showed that PME-1 readily demethylates different families of PP2A holoenzymes and blocks substrate recognition in vitro. The high-resolution cryoelectron microscopy structure of a PP2A-B56 holoenzyme-PME-1 complex reveals that PME-1 disordered regions, including a substrate-mimicking motif, tether to the B56 regulatory subunit at remote sites. They occupy the holoenzyme substrate-binding groove and allow large structural shifts in both holoenzyme and PME-1 to enable multipartite contacts at structured cores to activate the methylesterase. B56 interface mutations selectively block PME-1 activity toward PP2A-B56 holoenzymes and affect the methylation of a fraction of total cellular PP2A. The B56 interface mutations allow us to uncover B56-specific PME-1 functions in p53 signaling. Our studies reveal multiple mechanisms of PME-1 in suppressing holoenzyme functions and versatile PME-1 activities derived from coupling substrate-mimicking motifs to dynamic structured cores.
External linksElife / PubMed:35924897 / PubMed Central
MethodsEM (single particle)
Resolution3.4 Å
Structure data

25363

7soy

EMDB-25363, PDB-7soy:
The structure of the PP2A-B56gamma1 holoenzyme-PME-1 complex
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • homo sapiens (human)
KeywordsRECOMBINATION / The structure of PP2A-B56gamma holoenzyme-PME-1 complex

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