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Adaptation of the bound intrinsically disordered protein YAP to mutations at the YAP:TEAD interface.

Mesrouze Y, Bokhovchuk F, Izaac A, Meyerhofer M, Zimmermann C, Fontana P, Schmelzle T, Erdmann D, Furet P, Kallen J, Chène P
Protein Sci 27 1810-1820 (2018)
Related entries: 6ge3, 6ge5, 6ge6, 6gec, 6gee, 6geg, 6gei, 6gek

Cited: 15 times
EuropePMC logo PMID: 30058229

Abstract

Many interactions between proteins are mediated by intrinsically disordered regions (IDRs). Intrinsically disordered proteins (IDPs) do not adopt a stable three-dimensional structure in their unbound form, but they become more structured upon binding to their partners. In this communication, we study how a bound IDR adapts to mutations, preventing the formation of hydrogen bonds at the binding interface that needs a precise positioning of the interacting residues to be formed. We use as a model the YAP:TEAD interface, where one YAP (IDP) and two TEAD residues form hydrogen bonds via their side chain. Our study shows that the conformational flexibility of bound YAP and the reorganization of water molecules at the interface help to reduce the energetic constraints created by the loss of H-bonds at the interface. The residual flexibility/dynamic of bound IDRs and water might, therefore, be a key for the adaptation of IDPs to different interface landscapes and to mutations occurring at binding interfaces.

Articles - 6ge4 mentioned but not cited (1)

  1. Adaptation of the bound intrinsically disordered protein YAP to mutations at the YAP:TEAD interface. Mesrouze Y, Bokhovchuk F, Izaac A, Meyerhofer M, Zimmermann C, Fontana P, Schmelzle T, Erdmann D, Furet P, Kallen J, Chène P. Protein Sci 27 1810-1820 (2018)


Reviews citing this publication (5)

  1. Templated folding of intrinsically disordered proteins. Toto A, Malagrinò F, Visconti L, Troilo F, Pagano L, Brunori M, Jemth P, Gianni S. J Biol Chem 295 6586-6593 (2020)
  2. Matrin3: Disorder and ALS Pathogenesis. Salem A, Wilson CJ, Rutledge BS, Dilliott A, Farhan S, Choy WY, Duennwald ML. Front Mol Biosci 8 794646 (2021)
  3. Targeting the Hippo/YAP/TAZ signalling pathway: Novel opportunities for therapeutic interventions into skin cancers. Howard A, Bojko J, Flynn B, Bowen S, Jungwirth U, Walko G. Exp Dermatol 31 1477-1499 (2022)
  4. Leveraging Hot Spots of TEAD-Coregulator Interactions in the Design of Direct Small Molecule Protein-Protein Interaction Disruptors Targeting Hippo Pathway Signaling. Zhao B, Pobbati AV, Rubin BP, Stauffer S. Pharmaceuticals (Basel) 16 583 (2023)
  5. Assays Used for Discovering Small Molecule Inhibitors of YAP Activity in Cancers. Maity S, Gridnev A, Misra JR. Cancers (Basel) 14 1029 (2022)

Articles citing this publication (9)

  1. YAP-dependent necrosis occurs in early stages of Alzheimer's disease and regulates mouse model pathology. Tanaka H, Homma H, Fujita K, Kondo K, Yamada S, Jin X, Waragai M, Ohtomo G, Iwata A, Tagawa K, Atsuta N, Katsuno M, Tomita N, Furukawa K, Saito Y, Saito T, Ichise A, Shibata S, Arai H, Saido T, Sudol M, Muramatsu SI, Okano H, Mufson EJ, Sobue G, Murayama S, Okazawa H. Nat Commun 11 507 (2020)
  2. Identification of FAM181A and FAM181B as new interactors with the TEAD transcription factors. Bokhovchuk F, Mesrouze Y, Delaunay C, Martin T, Villard F, Meyerhofer M, Fontana P, Zimmermann C, Erdmann D, Furet P, Scheufler C, Schmelzle T, Chène P. Protein Sci 29 509-520 (2020)
  3. A new perspective on the interaction between the Vg/VGLL1-3 proteins and the TEAD transcription factors. Mesrouze Y, Aguilar G, Bokhovchuk F, Martin T, Delaunay C, Villard F, Meyerhofer M, Zimmermann C, Fontana P, Wille R, Vorherr T, Erdmann D, Furet P, Scheufler C, Schmelzle T, Affolter M, Chène P. Sci Rep 10 17442 (2020)
  4. Fluorescence polarization assay for the identification and evaluation of inhibitors at YAP-TEAD protein-protein interface 3. Zhou W, Li Y, Song J, Li C. Anal Biochem 586 113413 (2019)
  5. Hot Spot Analysis of YAP-TEAD Protein-Protein Interaction Using the Fragment Molecular Orbital Method and Its Application for Inhibitor Discovery. Kim J, Lim H, Moon S, Cho SY, Kim M, Park JH, Park HW, No KT. Cancers (Basel) 13 4246 (2021)
  6. N-terminal β-strand in YAP is critical for stronger binding to scalloped relative to TEAD transcription factor. Bokhovchuk F, Mesrouze Y, Meyerhofer M, Fontana P, Zimmermann C, Villard F, Erdmann D, Kallen J, Scheufler C, Velez-Vega C, Chène P. Protein Sci 32 e4545 (2023)
  7. Study of the TEAD-binding domain of the YAP protein from animal species. Mesrouze Y, Bokhovchuk F, Meyerhofer M, Zimmermann C, Fontana P, Erdmann D, Chène P. Protein Sci 30 339-349 (2021)
  8. PERCC1, a new member of the Yap/TAZ/FAM181 transcriptional co-regulator family. Sanchez-Pulido L, Jia S, Hansen CG, Ponting CP. Bioinform Adv 2 vbac008 (2022)
  9. The role of lysine palmitoylation/myristoylation in the function of the TEAD transcription factors. Mesrouze Y, Aguilar G, Meyerhofer M, Bokhovchuk F, Zimmermann C, Fontana P, Vissières A, Voshol H, Erdmann D, Affolter M, Chène P. Sci Rep 12 4984 (2022)


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