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Peptides targeting the PDZ domain of PTPN4 are efficient inducers of glioblastoma cell death.

Babault N, Cordier F, Lafage M, Cockburn J, Haouz A, Prehaud C, Rey FA, Delepierre M, Buc H, Lafon M, Wolff N
Structure 19 1518-24 (2011)
Cited: 32 times
EuropePMC logo PMID: 22000519

Abstract

PTPN4, a human tyrosine phosphatase, protects cells against apoptosis. This protection could be abrogated by targeting the PDZ domain of this phosphatase with a peptide mimicking the C-terminal sequence of the G protein of an attenuated rabies virus strain. Here, we demonstrate that glioblastoma death is triggered upon intracellular delivery of peptides, either from viral origin or from known endogenous ligands of PTPN4-PDZ, such as the C terminus sequence of the glutamate receptor subunit GluN2A. The killing efficiency of peptides closely reflects their affinities for the PTPN4-PDZ. The crystal structures of two PTPN4-PDZ/peptide complexes allow us to pinpoint the main structural determinants of binding and to synthesize a peptide of high affinity for PTPN4-PDZ enhancing markedly its cell death capacity. These results allow us to propose a potential mechanism for the efficiency of peptides and provide a target and a robust framework for the design of new pro-death compounds.

Articles - 3nfl mentioned but not cited (1)

  1. Structural and functional characterization of the PDZ domain of the human phosphatase PTPN3 and its interaction with the human papillomavirus E6 oncoprotein. Genera M, Samson D, Raynal B, Haouz A, Baron B, Simenel C, Guerois R, Wolff N, Caillet-Saguy C. Sci Rep 9 7438 (2019)


Reviews citing this publication (8)

  1. Rabies. Fooks AR, Cliquet F, Finke S, Freuling C, Hemachudha T, Mani RS, Müller T, Nadin-Davis S, Picard-Meyer E, Wilde H, Banyard AC. Nat Rev Dis Primers 3 17091 (2017)
  2. The emerging contribution of sequence context to the specificity of protein interactions mediated by PDZ domains. Luck K, Charbonnier S, Travé G. FEBS Lett 586 2648-2661 (2012)
  3. Emerging Themes in PDZ Domain Signaling: Structure, Function, and Inhibition. Liu X, Fuentes EJ. Int Rev Cell Mol Biol 343 129-218 (2019)
  4. Proteinaceous Regulators and Inhibitors of Protein Tyrosine Phosphatases. Hendriks W, Bourgonje A, Leenders W, Pulido R. Molecules 23 E395 (2018)
  5. A Drosophila-centric view of protein tyrosine phosphatases. Hatzihristidis T, Desai N, Hutchins AP, Meng TC, Tremblay ML, Miranda-Saavedra D. FEBS Lett 589 951-966 (2015)
  6. Upsetting the Balance: When Viruses Manipulate Cell Polarity Control. Thomas M, Banks L. J Mol Biol 430 3481-3503 (2018)
  7. Targeting an oncogenic kinase/phosphatase signaling network for cancer therapy. Qi XM, Wang F, Mortensen M, Wertz R, Chen G. Acta Pharm Sin B 8 511-517 (2018)
  8. Leveraging machine learning models for peptide-protein interaction prediction. Yin S, Mi X, Shukla D. RSC Chem Biol 5 401-417 (2024)

Articles citing this publication (23)



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