Chapter 23 Dissection of the BCL-2 Family Signaling Network with Stabilized α-Helices of BCL-2 Domains

Methods in Enzymology

Volumn 446, Issue , 2008, Pages 387-408

  Pitter, Kenneth ^a   Bernal, Federico ^a   LaBelle, James ^a   Walensky, Loren D ^a  

^a DANA FARBER CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BH3 PROTEIN; BUFFER; CYTOCHROME C; DEATH RECEPTOR; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; STABILIZED ALPHA HELICES OF BCL 2 DOMAINS; UNCLASSIFIED DRUG; DEXTRAN; DRUG DERIVATIVE; FLUORESCEIN ISOTHIOCYANATE; FLUORESCEIN ISOTHIOCYANATE DEXTRAN; LIPOCORTIN 5; LIPOSOME; PROTEIN BID;

ALPHA HELIX; ANIMAL CELL; ANIMAL TISSUE; APOPTOSIS; CELL ISOLATION; CELL MEMBRANE PERMEABILITY; ENZYME REGULATION; ENZYME RELEASE; FLUORESCENCE POLARIZATION IMMUNOASSAY; IN VITRO STUDY; MITOCHONDRION; MOUSE; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN INTERACTION; REVIEW; SIGNAL TRANSDUCTION; ANIMAL; ARTICLE; DRUG EFFECT; FLUORESCENCE POLARIZATION; HUMAN; METABOLISM; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; SECRETION;

ANIMALS; ANNEXIN A5; APOPTOSIS; BCL-2-ASSOCIATED X PROTEIN; BH3 INTERACTING DOMAIN DEATH AGONIST PROTEIN; CYTOCHROMES C; DEXTRANS; FLUORESCEIN-5-ISOTHIOCYANATE; FLUORESCENCE POLARIZATION; HUMANS; LIPOSOMES; MICE; MITOCHONDRIA; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-BCL-2; SIGNAL TRANSDUCTION;

EID: 50349092358     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(08)01623-6     Document Type: Review

References (43)

1. Annis M.G., Soucie E.L., Dlugosz P.J., Cruz-Aguado J.A., Penn L.Z., Leber B., and Andrews D.W. Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis. Embo J. 24 (2005) 2096-2103
2. Antonsson B., Montessuit S., Lauper S., Eskes R., and Martinou J.C. Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria. Biochem. J. 345 Pt 2 (2000) 271-278
3. Ardail D., Privat J.P., Egret-Charlier M., Levrat C., Lerme F., and Louisot P. Mitochondrial contact sites. Lipid composition and dynamics. J. Biol. Chem. 265 (1990) 18797-18802
4. Bakhshi A., Jensen J.P., Goldman P., Wright J.J., McBride O.W., Epstein A.L., and Korsmeyer S.J. Cloning the chromosomal breakpoint of t(14;18) human lymphomas: Clustering around JH on chromosome 14 and near a transcriptional unit on 18. Cell 41 (1985) 899-906
5. Bird G.H., Bernal F., Pitter K., and Walensky L.D. Synthesis and Biophysical Characterization of Stabilized Alpha-Helices of BCL-2 Domains. Methods Enzymol. 446 (2008) 387-408
6. Böttcher C.J.F., van Gent C.M., and Pries C. A rapid and sensitive sub-micro phosphorus determination. Anal. Chim. Acta 24 (1961) 203-204
7. Certo M., Del Gaizo Moore V., Nishino M., Wei G., Korsmeyer S., Armstrong S.A., and Letai A. Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members. Cancer Cell 9 (2006) 351-365
8. Cheng E.H., Wei M.C., Weiler S., Flavell R.A., Mak T.W., Lindsten T., and Korsmeyer S.J. BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. Mol. Cell 8 (2001) 705-711
9. Cleary M.L., and Sklar J. Nucleotide sequence of a t(14;18) chromosomal breakpoint in follicular lymphoma and demonstration of a breakpoint-cluster region near a transcriptionally active locus on chromosome 18. Proc. Natl. Acad. Sci. USA 82 (1985) 7439-7443
10. Copeland R.A. Enzymes: A practical introduction to structure, mechanism, and data analysis. 2nd ed (2000), Wiley-VCH, New York
11. Danial N.N., and Korsmeyer S.J. Cell death: Critical control points. Cell 116 (2004) 205-219
12. Danial N.N., et al. Dual role of proapoptotic BAD in insulin secretion and beta cell survival. Nat. Med. 14 (2008) 144-153
13. Ellerby H.M., Martin S.J., Ellerby L.M., Naiem S.S., Rabizadeh S., Salvesen G.S., Casiano C.A., Cashman N.R., Green D.R., and Bredesen D.E. Establishment of a cell-free system of neuronal apoptosis: Comparison of premitochondrial, mitochondrial, and postmitochondrial phases. J. Neurosci. 17 (1997) 6165-6178
14. Eskes R., Desagher S., Antonsson B., and Martinou J.C. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol. Cell. Biol. 20 (2000) 929-935
15. Goping I.S., Gross A., Lavoie J.N., Nguyen M., Jemmerson R., Roth K., Korsmeyer S.J., and Shore G.C. Regulated targeting of BAX to mitochondria. J. Cell. Biol. 143 (1998) 207-215
16. Gross A., Jockel J., Wei M.C., and Korsmeyer S.J. Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis. Embo. J. 17 (1998) 3878-3885
17. Hockenbery D., Nunez G., Milliman C., Schreiber R.D., and Korsmeyer S.J. Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature 348 (1990) 334-336
18. Karbowski M., Norris K.L., Cleland M.M., Jeong S.Y., and Youle R.J. Role of Bax and Bak in mitochondrial morphogenesis. Nature 443 (2006) 658-662
19. Kim H., Rafiuddin-Shah M., Tu H.C., Jeffers J.R., Zambetti G.P., Hsieh J.J., and Cheng E.H. Hierarchical regulation of mitochondrion-dependent apoptosis by BCL-2 subfamilies. Nat. Cell. Biol. 8 (2006) 1348-1358
20. Kuwana T., Mackey M.R., Perkins G., Ellisman M.H., Latterich M., Schneiter R., Green D.R., and Newmeyer D.D. Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell 111 (2002) 331-342
21. Kuwana T., Bouchier-Hayes L., Chipuk J.E., Bonzon C., Sullivan B.A., Green D.R., and Newmeyer D.D. BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. Mol. Cell 17 (2005) 525-535
22. Letai A., Bassik M.C., Walensky L.D., Sorcinelli M.D., Weiler S., and Korsmeyer S.J. Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cell 2 (2002) 183-192
23. Luo X., Budihardjo I., Zou H., Slaughter C., and Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 94 (1998) 481-490
24. Lutter M., Fang M., Luo X., Nishijima M., Xie X., and Wang X. Cardiolipin provides specificity for targeting of tBid to mitochondria. Nat. Cell. Biol. 2 (2000) 754-761
25. McDonnell T.J., Deane N., Platt F.M., Nunez G., Jaeger U., McKearn J.P., and Korsmeyer S.J. bcl-2-immunoglobulin transgenic mice demonstrate extended B cell survival and follicular lymphoproliferation. Cell 57 (1989) 79-88
26. Nunez G., London L., Hockenbery D., Alexander M., McKearn J.P., and Korsmeyer S.J. Deregulated Bcl-2 gene expression selectively prolongs survival of growth factor-deprived hemopoietic cell lines. J. Immunol. 144 (1990) 3602-3610
27. Oh K.J., Barbuto S., Pitter K., Morash J., Walensky L.D., and Korsmeyer S.J. A membrane-targeted BID BCL-2 homology 3 peptide is sufficient for high potency activation of BAX in vitro. J. Biol. Chem. 281 (2006) 36999-37008
28. Sattler M., et al. Structure of Bcl-xL-Bak peptide complex: Recognition between regulators of apoptosis. Science 275 (1997) 983-986
29. Scorrano L., Ashiya M., Buttle K., Weiler S., Oakes S.A., Mannella C.A., and Korsmeyer S.J. A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis. Dev. Cell 2 (2002) 55-67
30. Seto M., Jaeger U., Hockett R.D., Graninger W., Bennett S., Goldman P., and Korsmeyer S.J. Alternative promoters and exons, somatic mutation and deregulation of the Bcl-2-Ig fusion gene in lymphoma. Embo J. 7 (1988) 123-131
31. Suzuki M., Youle R.J., and Tjandra N. Structure of Bax: Coregulation of dimer formation and intracellular localization. Cell 103 (2000) 645-654
32. Terrones O., Antonsson B., Yamaguchi H., Wang H.G., Liu J., Lee R.M., Herrmann A., and Basanez G. Lipidic pore formation by the concerted action of proapoptotic BAX and tBID. J. Biol. Chem. 279 (2004) 30081-30091
33. Terrones O., Etxebarria A., Landajuela A., Landeta O., Antonsson B., and Basanez G. Bim and tbid are not mechanistically equivalent when assisting Bax to permeabilize bilayer membranes. J. Biol. Chem. 283 (2008) 7790-7803
34. Tsujimoto Y., Gorham J., Cossman J., Jaffe E., and Croce C.M. The t(14;18) chromosome translocations involved in B-cell neoplasms result from mistakes in VDJ joining. Science 229 (1985) 1390-1393
35. Uren R.T., Dewson G., Chen L., Coyne S.C., Huang D.C., Adams J.M., and Kluck R.M. Mitochondrial permeabilization relies on BH3 ligands engaging multiple prosurvival Bcl-2 relatives, not Bak. J. Cell. Biol. 177 (2007) 277-287
36. Vaux D.L., Cory S., and Adams J.M. Bcl-2 gene promotes haemopoietic cell survival and cooperates with c- myc to immortalize pre-B cells. Nature 335 (1988) 440-442
37. Walensky L.D., Pitter K., Morash J., Oh K.J., Barbuto S., Fisher J., Smith E., Verdine G.L., and Korsmeyer S.J. A stapled BID BH3 helix directly binds and activates BAX. Mol. Cell 24 (2006) 199-210
38. Walensky L.D., Kung A.L., Escher I., Malia T.J., Barbuto S., Wright R.D., Wagner G., Verdine G.L., and Korsmeyer S.J. Activation of apoptosis in vivo by a hydrocarbon-stapled BH3 helix. Science 305 (2004) 1466-1470
39. Wei M.C., Lindsten T., Mootha V.K., Weiler S., Gross A., Ashiya M., Thompson C.B., and Korsmeyer S.J. tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c. Genes. Dev. 14 (2000) 2060-2071
40. Willis S.N., et al. Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak. Science 315 (2007) 856-859
41. Yethon J.A., Epand R.F., Leber B., Epand R.M., and Andrews D.W. Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis. J. Biol. Chem. 278 (2003) 48935-48941
42. Youle R.J., and Strasser A. The BCL-2 protein family: Opposing activities that mediate cell death. Nat. Rev. Mol. Cell Biol. 9 (2008) 47-59
43. Zha H., Aime-Sempe C., Sato T., and Reed J.C. Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2. J. Biol. Chem. 271 (1996) 7440-7444