Structure-destabilizing mutations unleash an intrinsic perforation activity of antiapoptotic Bcl-2 in the mitochondrial membrane enabling apoptotic cell death

[1]  A. García-Sáez,et al.  Visualization of BOK pores independent of BAX and BAK reveals a similar mechanism with differing regulation , 2022, Cell Death & Differentiation.

[2]  E. Thompson,et al.  Acquired mutations in BAX confer resistance to BH3-mimetic therapy in acute myeloid leukemia , 2022, Blood.

[3]  J. Seymour,et al.  Clinical experiences with venetoclax and other pro-apoptotic agents in lymphoid malignancies: lessons from monotherapy and chemotherapy combination , 2022, Journal of Hematology & Oncology.

[4]  Haige Ye,et al.  Progress in understanding the mechanisms of resistance to BCL-2 inhibitors , 2022, Experimental Hematology & Oncology.

[5]  T. Moldoveanu,et al.  Protein-protein and protein-lipid interactions of pore-forming BCL-2 family proteins in apoptosis initiation. , 2022, Biochemical Society transactions.

[6]  A. Villunger,et al.  BCL‐2‐family protein tBID can act as a BAX‐like effector of apoptosis , 2021, The EMBO journal.

[7]  E. Thompson,et al.  Clonal hematopoiesis, myeloid disorders and BAX-mutated myelopoiesis in patients receiving venetoclax for CLL , 2021, Blood.

[8]  D. Andrews,et al.  An amphipathic Bax core dimer forms part of the apoptotic pore wall in the mitochondrial␣membrane , 2021, The EMBO journal.

[9]  E. Thompson,et al.  Multiple BCL2 mutations co-occurring with Gly101Val emerge in chronic lymphocytic leukemia progression on venetoclax. , 2020, Blood.

[10]  E. Thompson,et al.  Characterization of a novel venetoclax resistance mutation (BCL2 Phe104Ile) observed in follicular lymphoma , 2019, British journal of haematology.

[11]  P. Colman,et al.  Structures of BCL-2 in complex with venetoclax reveal the molecular basis of resistance mutations , 2019, Nature Communications.

[12]  J. Sandow,et al.  BAX Activation: Mutations Near Its Proposed Non-canonical BH3 Binding Site Reveal Allosteric Changes Controlling Mitochondrial Association. , 2019, Cell reports.

[13]  D. Andrews,et al.  The carboxyl-terminal sequence of bim enables bax activation and killing of unprimed cells , 2019, bioRxiv.

[14]  E. Thompson,et al.  Acquisition of the Recurrent Gly101Val Mutation in BCL2 Confers Resistance to Venetoclax in Patients with Progressive Chronic Lymphocytic Leukemia. , 2018, Cancer discovery.

[15]  A. Strasser,et al.  BH3-Mimetic Drugs: Blazing the Trail for New Cancer Medicines. , 2018, Cancer cell.

[16]  Taosheng Chen,et al.  Intrinsic Instability of BOK Enables Membrane Permeabilization in Apoptosis , 2018, Cell reports.

[17]  Scott A. Brown,et al.  BOK Is a Non-canonical BCL-2 Family Effector of Apoptosis Regulated by ER-Associated Degradation , 2016, Cell.

[18]  D. Andrews,et al.  BH3‐in‐groove dimerization initiates and helix 9 dimerization expands Bax pore assembly in membranes , 2016, The EMBO journal.

[19]  G. Jeschke,et al.  Structural model of active Bax at the membrane. , 2014, Molecular cell.

[20]  J. Martinez-Climent,et al.  Acquired mutations in BCL2 family proteins conferring resistance to the BH3 mimetic ABT-199 in lymphoma. , 2014, Blood.

[21]  Peter E. Czabotar,et al.  Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy , 2013, Nature Reviews Molecular Cell Biology.

[22]  G. Dewson,et al.  Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis , 2013, Cell Death and Differentiation.

[23]  A. García-Sáez,et al.  Proapoptotic Bax and Bak Proteins Form Stable Protein-permeable Pores of Tunable Size , 2013, The Journal of Biological Chemistry.

[24]  D. Andrews,et al.  Mechanisms of action of Bcl-2 family proteins. , 2013, Cold Spring Harbor perspectives in biology.

[25]  S. Tait,et al.  Multiple functions of BCL-2 family proteins. , 2013, Cold Spring Harbor perspectives in biology.

[26]  Erinna F. Lee,et al.  Bax Crystal Structures Reveal How BH3 Domains Activate Bax and Nucleate Its Oligomerization to Induce Apoptosis , 2013, Cell.

[27]  L. Lam,et al.  ABT-199, a potent and selective BCL-2 inhibitor, achieves antitumor activity while sparing platelets , 2013, Nature Medicine.

[28]  C. Combet,et al.  Evolution of Bcl-2 homology motifs: homology versus homoplasy , 2012, Trends in Cell Biology.

[29]  Biyun Ni,et al.  Natural Diterpenoid Compound Elevates Expression of Bim Protein, Which Interacts with Antiapoptotic Protein Bcl-2, Converting It to Proapoptotic Bax-like Molecule* , 2011, The Journal of Biological Chemistry.

[30]  D. Hanahan,et al.  Hallmarks of Cancer: The Next Generation , 2011, Cell.

[31]  M. Zoratti,et al.  Single-point mutations of a lysine residue change function of Bax and Bcl-xL expressed in Bax- and Bak-less mouse embryonic fibroblasts: novel insights into the molecular mechanisms of Bax-induced apoptosis , 2011, Cell Death and Differentiation.

[32]  L. Walensky,et al.  BH3-triggered structural reorganization drives the activation of proapoptotic BAX. , 2010, Molecular cell.

[33]  D. Andrews,et al.  Still embedded together binding to membranes regulates Bcl-2 protein interactions , 2010, Oncogene.

[34]  Arthur E. Johnson,et al.  Bax Forms an Oligomer via Separate, Yet Interdependent, Surfaces* , 2010, The Journal of Biological Chemistry.

[35]  H. Steinhoff,et al.  Molecular Details of Bax Activation, Oligomerization, and Membrane Insertion* , 2009, The Journal of Biological Chemistry.

[36]  Osamu Takeuchi,et al.  Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis. , 2009, Molecular cell.

[37]  B. Baggenstoss,et al.  Oligomerization of membrane-bound Bcl-2 is involved in its pore formation induced by tBid , 2009, Apoptosis.

[38]  Joel Quispe,et al.  Mitochondrial outer membrane proteins assist Bid in Bax-mediated lipidic pore formation. , 2009, Molecular biology of the cell.

[39]  D. Andrews,et al.  Membrane Binding by tBid Initiates an Ordered Series of Events Culminating in Membrane Permeabilization by Bax , 2008, Cell.

[40]  John Calvin Reed,et al.  Bcl-2 family proteins and cancer , 2008, Oncogene.

[41]  John Calvin Reed,et al.  A short Nur77-derived peptide converts Bcl-2 from a protector to a killer. , 2008, Cancer cell.

[42]  A. Letai,et al.  Diagnosing and exploiting cancer's addiction to blocks in apoptosis , 2008, Nature Reviews Cancer.

[43]  David W. Andrews,et al.  Embedded together: The life and death consequences of interaction of the Bcl-2 family with membranes , 2007, Apoptosis.

[44]  A. Tocilj,et al.  The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site. , 2006, Molecular cell.

[45]  D. Andrews,et al.  tBid Elicits a Conformational Alteration in Membrane-bound Bcl-2 Such That It Inhibits Bax Pore Formation* , 2006, Journal of Biological Chemistry.

[46]  W. Zong,et al.  Gossypol induces Bax/Bak‐independent activation of apoptosis and cytochrome c release via a conformational change in Bcl‐2 , 2006, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[47]  D. Andrews,et al.  Bcl‐2 changes conformation to inhibit Bax oligomerization , 2006, The EMBO journal.

[48]  David W Andrews,et al.  Auto-activation of the Apoptosis Protein Bax Increases Mitochondrial Membrane Permeability and Is Inhibited by Bcl-2* , 2006, Journal of Biological Chemistry.

[49]  T. Kuwana,et al.  The multidomain proapoptotic molecules Bax and Bak are directly activated by heat. , 2005, Proceedings of the National Academy of Sciences of the United States of America.

[50]  M. Miura,et al.  Bax‐like protein Drob‐1 protects neurons from expanded polyglutamine‐induced toxicity in Drosophila , 2005, The EMBO journal.

[51]  D. Andrews,et al.  Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis , 2005, The EMBO journal.

[52]  D. Andrews,et al.  Bcl-2 Homodimerization Involves Two Distinct Binding Surfaces, a Topographic Arrangement That Provides an Effective Mechanism for Bcl-2 to Capture Activated Bax* , 2004, Journal of Biological Chemistry.

[53]  D. Andrews,et al.  During apoptosis bcl-2 changes membrane topology at both the endoplasmic reticulum and mitochondria. , 2004, Molecular cell.

[54]  John Calvin Reed,et al.  Conversion of Bcl-2 from Protector to Killer by Interaction with Nuclear Orphan Receptor Nur77/TR3 , 2004, Cell.

[55]  C. Tian,et al.  Essential role of the voltage-dependent anion channel (VDAC) in mitochondrial permeability transition pore opening and cytochrome c release induced by arsenic trioxide , 2004, Oncogene.

[56]  Suzanne Cory,et al.  The Bcl-2 family: roles in cell survival and oncogenesis , 2003, Oncogene.

[57]  Mason R. Mackey,et al.  Bid, Bax, and Lipids Cooperate to Form Supramolecular Openings in the Outer Mitochondrial Membrane , 2002, Cell.

[58]  J J Hill,et al.  Biophysical characterization of recombinant human Bcl-2 and its interactions with an inhibitory ligand, antimycin A. , 2001, Biochemistry.

[59]  A. Petros,et al.  Solution structure of the antiapoptotic protein bcl-2 , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[60]  Nico Tjandra,et al.  Structure of Bax Coregulation of Dimer Formation and Intracellular Localization , 2000, Cell.

[61]  Sharad Kumar,et al.  Debcl, a Proapoptotic Bcl-2 Homologue, Is a Component of the Drosophila melanogaster Cell Death Machinery , 2000, The Journal of cell biology.

[62]  H. Okano,et al.  Drob-1, a Drosophila member of the Bcl-2/CED-9 family that promotes cell death. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[63]  S. Korsmeyer,et al.  Solution Structure of the Proapoptotic Molecule BID A Structural Basis for Apoptotic Agonists and Antagonists , 1999, Cell.

[64]  Junying Yuan,et al.  Solution Structure of BID, an Intracellular Amplifier of Apoptotic Signaling , 1999, Cell.

[65]  Junying Yuan,et al.  Cleavage of BID by Caspase 8 Mediates the Mitochondrial Damage in the Fas Pathway of Apoptosis , 1998, Cell.

[66]  Xiaodong Wang,et al.  Bid, a Bcl2 Interacting Protein, Mediates Cytochrome c Release from Mitochondria in Response to Activation of Cell Surface Death Receptors , 1998, Cell.

[67]  E. Cheng,et al.  Conversion of Bcl-2 to a Bax-like death effector by caspases. , 1997, Science.

[68]  H. Horvitz,et al.  Caenorhabditis elegans CED-9 protein is a bifunctional cell-death inhibitor , 1997, Nature.

[69]  R. Stroud,et al.  Crystal structure of colicin Ia , 1997, Nature.

[70]  R. Meadows,et al.  X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death , 1996, Nature.

[71]  Z. Oltvai,et al.  BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax , 1994, Nature.

[72]  H. Horvitz,et al.  Activation of C. elegans cell death protein CED-9 by an ammo-acid substitution in a domain conserved in Bcl-2 , 1994, Nature.

[73]  Katherine A. Kantardjieff,et al.  The crystal structure of diphtheria toxin , 1992, Nature.