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@ARTICLE{Landeta:126963,
      author       = {O. Landeta and A. Landajuela and A. Garcia-Saez$^*$ and G.
                      Basañez},
      title        = {{M}inimalist {M}odel {S}ystems {R}eveal {S}imilarities and
                      {D}ifferences between {M}embrane {I}nteraction {M}odes of
                      {MCL}1 and {BAK}.},
      journal      = {The journal of biological chemistry},
      volume       = {290},
      number       = {27},
      issn         = {1083-351X},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {DKFZ-2017-02989},
      pages        = {17004 - 17019},
      year         = {2015},
      abstract     = {Proteins belonging to the BCL2 family are key modulators of
                      apoptosis that establish a complex network of interactions
                      among themselves and with other cellular factors to regulate
                      cell fate. It is well established that mitochondrial
                      membranes are the main locus of action of all BCL2 family
                      proteins, but it is difficult to obtain a precise view of
                      how BCL2 family members operate at the native mitochondrial
                      membrane environment during apoptosis. Here, we used
                      minimalist model systems and multiple fluorescence-based
                      techniques to examine selected membrane activities of MCL1
                      and BAK under apoptotic-like conditions. We show that three
                      distinct apoptosis-related factors (i.e. the BCL2 homology 3
                      ligand cBID, the mitochondrion-specific lipid cardiolipin,
                      and membrane geometrical curvature) all promote membrane
                      association of BCL2-like structural folds belonging to both
                      MCL1 and BAK. However, at the same time, the two proteins
                      exhibited distinguishing features in their membrane
                      association modes under apoptotic-like conditions. In
                      addition, scanning fluorescence cross-correlation
                      spectroscopy and FRET measurements revealed that the
                      BCL2-like structural fold of MCL1, but not that of BAK,
                      forms stable heterodimeric complexes with cBID in a manner
                      adjustable by membrane cardiolipin content and curvature
                      degree. Our results add significantly to a growing body of
                      evidence indicating that the mitochondrial membrane
                      environment plays a complex and active role in the mode of
                      action of BCL2 family proteins.},
      keywords     = {BH3 Interacting Domain Death Agonist Protein (NLM
                      Chemicals) / Bak1 protein, mouse (NLM Chemicals) / Mcl1
                      protein, mouse (NLM Chemicals) / Myeloid Cell Leukemia
                      Sequence 1 Protein (NLM Chemicals) / bcl-2 Homologous
                      Antagonist-Killer Protein (NLM Chemicals)},
      cin          = {B160},
      ddc          = {570},
      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:25987560},
      pmc          = {pmc:PMC4505444},
      doi          = {10.1074/jbc.M114.602193},
      url          = {https://inrepo02.dkfz.de/record/126963},
}