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@ARTICLE{Mastny:168215,
      author       = {Mastny, Markus and Heuck, Alexander and Kurzbauer, Robert
                      and Heiduk, Anja and Boisguerin, Prisca and Volkmer, Rudolf
                      and Ehrmann, Michael and Rodrigues, Christopher D. A. and
                      Rudner, David Z. and Clausen, Tim},
      title        = {{C}tp{B} {A}ssembles a {G}ated {P}rotease {T}unnel
                      {R}egulating {C}ell-{C}ell {S}ignaling during {S}pore
                      {F}ormation in {B}acillus subtilis},
      journal      = {Cell},
      volume       = {155},
      number       = {3},
      issn         = {0092-8674},
      address      = {[Cambridge, Mass.]},
      publisher    = {Cell Press},
      reportid     = {DESY-2014-02420},
      pages        = {647 - 658},
      year         = {2013},
      note         = {(c) Elsevier Inc.},
      abstract     = {Spore formation in Bacillus subtilis relies on a regulated
                      intramembrane proteolysis (RIP) pathway that synchronizes
                      mother-cell and forespore development. To address the
                      molecular basis of this SpoIV transmembrane signaling, we
                      carried out a structure-function analysis of the activating
                      protease CtpB. Crystal structures reflecting distinct
                      functional states show that CtpB constitutes a ring-like
                      protein scaffold penetrated by two narrow tunnels. Access to
                      the proteolytic sites sequestered within these tunnels is
                      controlled by PDZ domains that rearrange upon substrate
                      binding. Accordingly, CtpB resembles a minimal version of a
                      self-compartmentalizing protease regulated by a unique
                      allosteric mechanism. Moreover, biochemical analysis of the
                      PDZ-gated channel combined with sporulation assays reveal
                      that activation of the SpoIV RIP pathway is induced by the
                      concerted activity of CtpB and a second signaling protease,
                      SpoIVB. This proteolytic mechanism is of broad relevance for
                      cell-cell communication, illustrating how distinct signaling
                      pathways can be integrated into a single RIP module.},
      cin          = {EMBL-User},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {PETRA Beamline P14 (POF2-54G14)},
      pid          = {G:(DE-H253)POF2-P14-20130405},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000326571800018},
      pubmed       = {pmid:24243021},
      doi          = {10.1016/j.cell.2013.09.050},
      url          = {https://bib-pubdb1.desy.de/record/168215},
}