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@ARTICLE{Goretzki:598500,
      author       = {Goretzki, Benedikt and Wiedemann, Christoph and McCray,
                      Brett A. and Schäfer, Stefan L. and Jansen, Jasmin and
                      Tebbe, Frederike and Mitrovic, Sarah-Ana and Nöth, Julia
                      and Cabezudo, Ainara Claveras and Donohue, Jack K. and
                      Jeffries, Cy and Steinchen, Wieland and Stengel, Florian and
                      Sumner, Charlotte J. and Hummer, Gerhard and Hellmich, Ute
                      A.},
      title        = {{C}rosstalk between regulatory elements in disordered
                      {TRPV}4 {N}-terminus modulates lipid-dependent channel
                      activity},
      journal      = {Nature Communications},
      volume       = {14},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {PUBDB-2023-06835},
      pages        = {4165},
      year         = {2023},
      abstract     = {Intrinsically disordered regions (IDRs) are essential for
                      membrane receptor regulation but often remain unresolved in
                      structural studies. TRPV4, a member of the TRP vanilloid
                      channel family involved in thermo- and osmosensation, has a
                      large N-terminal IDR of approximately 150 amino acids. With
                      an integrated structural biology approach, we analyze the
                      structural ensemble of the TRPV4 IDR and the network of
                      antagonistic regulatory elements it encodes. These modulate
                      channel activity in a hierarchical lipid-dependent manner
                      through transient long-range interactions. A highly
                      conserved autoinhibitory patch acts as a master regulator by
                      competing with PIP2 binding to attenuate channel activity.
                      Molecular dynamics simulations show that loss of the
                      interaction between the PIP2-binding site and the membrane
                      reduces the force exerted by the IDR on the structured core
                      of TRPV4. This work demonstrates that IDR structural
                      dynamics are coupled to TRPV4 activity and highlights the
                      importance of IDRs for TRP channel function and regulation.},
      cin          = {EMBL / EMBL-User / DOOR ; HAS-User},
      ddc          = {500},
      cid          = {I:(DE-H253)EMBL-20120731 / I:(DE-H253)EMBL-User-20120814 /
                      I:(DE-H253)HAS-User-20120731},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / DFG project 390713860 -
                      EXC 2051: Balance of the Microverse (390713860)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(GEPRIS)390713860},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {37443299},
      UT           = {WOS:001030405300023},
      doi          = {10.1038/s41467-023-39808-4},
      url          = {https://bib-pubdb1.desy.de/record/598500},
}