Centre for Biological Signalling Studies

Dr. Frank Edlich

Dr. Frank Edlich

Institute for Biochemistry and Molecular Biology
University of Freiburg

+49 761 203 97482


We are exploring the molecular mechanism of apoptosis focusing on members of the Bcl-2 protein family. The complex interplay of Bcl-2 proteins regulates intrinsic apoptosis signaling converging at the mitochondrial outer membrane permeabilization (MOMP). MOMP results in cytochrome c (cyt c) release from the inner membrane space and subsequent caspase activation that dooms a cell to death. Despite extensive research on the regulatory step committing a cell to apoptosis - the activation of the Bcl-2 member Bax - the true nature of active Bax and the regulatory interplay of Bcl-2 proteins remain mysteries. We have found that inactive Bax migrates from the cytosol to the mitochondria, undergoes a conformational change and retrotranslocates back into the cytoplasm in healthy cells. Bax retrotranslocation depends on pro-survival Bcl-2 activities and is the mechanism that prevents Bax accumulation on the mitochondria in non-apoptotic cells. The molecular processes underlying the retrotranslocation of Bcl-2 proteins and the activation of mitochondrial Bax are now under investigation, concentrating on the influence of conformational changes in the regulation of Bcl-2 proteins.


10 selected publications

  • Mito-priming as a method to engineer Bcl-2 addiction.
    Lopez J, Bessou M, Riley JS, Giampazolias E, Todt F, Rochegüe T, Oberst A, Green DR, Edlich F, Ichim G, Tait SW.
    Nat Commun. 2016 Feb 2;7:10538.
  • Platelets induce apoptosis via membrane-bound FasL.
    Schleicher RI, Reichenbach F, Kraft P, Kumar A, Lescan M, Todt F, Göbel K, Hilgendorf I, Geisler T, Bauer A, Olbrich M, Schaller M, Wesselborg S, O'Reilly L, Meuth SG, Schulze-Osthoff K, Gawaz M, Li X, Kleinschnitz C, Edlich F, Langer HF.
    Blood. 2015 Sep 17;126(12):1483-93.
  • Differential retrotranslocation of mitochondrial Bax and Bak.
    Todt F, Cakir Z, Reichenbach F, Emschermann F, Lauterwasser J, Kaiser A, Ichim G, Tait SW, Frank S, Langer HF, Edlich F.
    EMBO J. 2015 Jan 2;34(1):67-80.
  • The C-terminal helix of Bcl-x(L) mediates Bax retrotranslocation from the mitochondria.
    Todt F, Cakir Z, Reichenbach F, Youle RJ, Edlich F.
    Cell Death Differ. 2013 Feb;20(2):333-42.
  • Structural mechanism of Bax inhibition by cytomegalovirus protein vMIA.
    Ma J, Edlich F, Bermejo GA, Norris KL, Youle RJ, Tjandra N.
    Proc Natl Acad Sci U S A. 2012 Dec 18;109(51):20901-6.
  • Bcl-x(L) retrotranslocates Bax from the mitochondria into the cytosol.
    Edlich F, Banerjee S, Suzuki M, Cleland MM, Arnoult D, Wang C, Neutzner A, Tjandra N, Youle RJ (2011).
    Cell 145, 104-16.
  • The soluble form of Bax regulates mitochondrial fusion via MFN2 homotypic complexes.
    Hoppins S, Edlich F, Cleland MM, Banerjee S, McCaffery JM, Youle RJ, Nunnari J (2011).
    Mol Cell 41, 150-60.
  • FKBP36 is an inherent multifunctional glyceraldehyde-3-phosphate dehydrogenase inhibitor.
    Jarczowski F, Jahreis G, Erdmann F, Schierhorn A, Fischer G, Edlich F  (2009).
    J Biol Chem 284, 766-73.
  • FKBP36 forms complexes with clathrin and Hsp72 in spermatocytes.
    Jarczowski F, Fischer G, Edlich F (2008).
    Biochemistry 47, 6946-6952.
  • A novel calmodulin-Ca2+ target recognition activates the Bcl-2 regulator FKBP38.
    Edlich F, Maestre-Martinez M, Jarczowski F, Weiwad M, Moutty MC, Malesevic M, Jahreis G, Fischer G, Lücke C (2007).
    J Biol Chem 282, 36496-36504.