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@ARTICLE{Bleicken:125273,
      author       = {S. Bleicken$^*$ and A. Hantusch and K. K. Das and T.
                      Frickey and A. J. Garcia-Saez$^*$},
      title        = {{Q}uantitative interactome of a membrane {B}cl-2 network
                      identifies a hierarchy of complexes for apoptosis
                      regulation.},
      journal      = {Nature Communications},
      volume       = {8},
      number       = {1},
      issn         = {2041-1723},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {DKFZ-2017-01412},
      pages        = {73},
      year         = {2017},
      abstract     = {The Bcl-2 proteins form a complex interaction network that
                      controls mitochondrial permeabilization and apoptosis. The
                      relative importance of different Bcl-2 complexes and their
                      spatio-temporal regulation is debated. Using fluorescence
                      cross-correlation spectroscopy to quantify the interactions
                      within a minimal Bcl-2 network, comprised by cBid, Bax, and
                      Bcl-xL, we show that membrane insertion drastically alters
                      the pattern of Bcl-2 complexes, and that the C-terminal
                      helix of Bcl-xL determines its binding preferences. At
                      physiological temperature, Bax can spontaneously activate in
                      a self-amplifying process. Strikingly, Bax also recruits
                      Bcl-xL to membranes, which is sufficient to retrotranslocate
                      Bax back into solution to secure membrane integrity. Our
                      study disentangles the hierarchy of Bcl-2 complex formation
                      in relation to their environment: Bcl-xL association with
                      cBid occurs in solution and in membranes, where the complex
                      is stabilized, whereas Bcl-xL binding to Bax occurs only in
                      membranes and with lower affinity than to cBid, leading
                      instead to Bax retrotranslocation.The permeabilization of
                      the mitochondrial outer membrane to induce apoptosis is
                      regulated by complex interactions between Bcl-2 family
                      members. Here the authors develop a quantitative interactome
                      of a membrane Bcl-2 network and identify a hierarchy of
                      protein complexes in apoptosis induction.},
      cin          = {B160},
      ddc          = {500},
      cid          = {I:(DE-He78)B160-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28706229},
      pmc          = {pmc:PMC5509671},
      doi          = {10.1038/s41467-017-00086-6},
      url          = {https://inrepo02.dkfz.de/record/125273},
}