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@ARTICLE{MiasLucquin:867581,
      author       = {Mias-Lucquin, Dominique and Dos Santos Morais, Raphael and
                      Chéron, Angélique and Lagarrigue, Mélanie and Winder,
                      Steve J. and Chenuel, Thomas and Pérez, Javier and Appavou,
                      Marie-Sousai and Martel, Anne and Alviset, Guillaume and Le
                      Rumeur, Elisabeth and Combet, Sophie and Hubert,
                      Jean-François and Delalande, Olivier},
      title        = {{H}ow the central domain of dystrophin acts to bridge
                      {F}-actin to sarcolemmal lipids},
      journal      = {Journal of structural biology},
      volume       = {209},
      issn         = {1047-8477},
      address      = {San Diego, Calif.},
      publisher    = {Elsevier},
      reportid     = {FZJ-2019-06204},
      pages        = {107411 -},
      year         = {2020},
      abstract     = {Dystrophin is a large intracellular protein that prevents
                      sarcolemmal ruptures by providing a mechanical link between
                      the intracellular actin cytoskeleton and the transmembrane
                      dystroglycan complex. Dystrophin deficiency leads to the
                      severe muscle wasting disease Duchenne Muscular Dystrophy
                      and the milder allelic variant, Becker Muscular Dystrophy
                      (DMD and BMD). Previous work has shown that concomitant
                      interaction of the actin binding domain 2 (ABD2) comprising
                      spectrin like repeats 11 to 15 (R11-15) of the central
                      domain of dystrophin, with both actin and membrane lipids,
                      can greatly increase membrane stiffness. Based on a
                      combination of SAXS and SANS measurements, mass spectrometry
                      analysis of cross-linked complexes and interactive
                      low-resolution simulations, we explored in vitro the
                      molecular properties of dystrophin that allow the formation
                      of ABD2-F-actin and ABD2-membrane model complexes. In
                      dystrophin we identified two subdomains interacting with
                      F-actin, one located in R11 and a neighbouring region in R12
                      and another one in R15, while a single lipid binding domain
                      was identified at the C-terminal end of R12. Relative
                      orientations of the dystrophin central domain with F-actin
                      and a membrane model were obtained from docking simulation
                      under experimental constraints. SAXS-based models were then
                      built for an extended central subdomain from R4 to R19,
                      including ABD2. Overall results are compatible with a
                      potential F-actin/dystrophin/membrane lipids ternary
                      complex. Our description of this selected part of the
                      dystrophin associated complex bridging muscle cell membrane
                      and cytoskeleton opens the way to a better understanding of
                      how cell muscle scaffolding is maintained through this
                      essential protein.},
      cin          = {JCNS-FRM-II / JCNS-1 / MLZ},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-588b)4597118-3},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6G15 - FRM II / MLZ (POF3-6G15)},
      pid          = {G:(DE-HGF)POF3-6G4 / G:(DE-HGF)POF3-6G15},
      experiment   = {EXP:(DE-MLZ)KWS1-20140101 / EXP:(DE-MLZ)KWS2-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31689503},
      UT           = {WOS:000507695200016},
      doi          = {10.1016/j.jsb.2019.107411},
      url          = {https://juser.fz-juelich.de/record/867581},
}