Completing the family portrait of the anti-apoptotic Bcl-2 proteins: Crystal structure of human Bfl-1 in complex with Bim

FEBS Letters

Volumn 582, Issue 25-26, 2008, Pages 3590-3594

  Herman, Maria Dolores ^a,b   Nyman, Tomas ^a   Welin, Martin ^a   Lehtiö, Lari ^a   Flodin, Susanne ^a   Trésaugues, Lionel ^a   Kotenyova, Tetyana ^a   Flores, Alex ^a   Nordlund, Pär ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b STOCKHOLM UNIVERSITY   (Sweden)

Author keywords

A1; Apoptosis; B cell lymphoma 2; Bfl 1; Cancer; Crystal structure

Indexed keywords

BCL2 RELATED PROTEIN A1; BIM PROTEIN; PROTEIN BCL 2; PROTEIN MCL 1;

ARTICLE; CRYSTAL STRUCTURE; HUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FAMILY; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; APOPTOSIS; APOPTOSIS REGULATORY PROTEINS; CRYSTALLOGRAPHY, X-RAY; HUMANS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-BCL-2;

EID: 54049102369     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.09.028     Document Type: Article

References (31)

1. Cory S., Huang D.C.S., and Adams J.M. The Bcl-2 family: roles in cell survival and oncogenesis. Oncogene 22 (2003) 8590-8607
2. Fesik S.W. Insights into programmed cell death through structural biology. Cell 103 (2000) 273-282
3. Petros A.M., Olejniczak E.T., and Fesik S.W. Structural biology of the Bcl-2 family of proteins. Biochim. Biophys. Acta (BBA) 1644 (2004) 83-94
4. Fesik S.W. Promoting apoptosis as a strategy for cancer drug discovery. Nat. Rev. Cancer 5 (2005) 876-885
5. Chen L., et al. Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function. Mol. Cell 17 (2005) 393-403
6. Certo M., Moore V.D.G., 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
7. 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
8. Hsu S.Y., Kaipia A., McGee E., Lomeli M., and Hsueh A.J.W. Bok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members. Proc. Nat. Acad. Sci. 94 (1997) 12401-12406
9. Petros A., et al. Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies. Protein Sci. 9 (2000) 2528-2534
10. Sattler M., et al. Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis. Science 275 (1997) 983-986
11. Liu X., Dai S., Zhu Y., Marrack P., and Kappler J.W. The structure of a Bcl-xL/Bim fragment complex: implications for Bim function. Immunity 19 (2003) 341-352
12. Denisov A.Y., Chen G., Sprules T., Moldoveanu T., Beauparlant P., and Gehring K. Structural model of the BCL-w-BID peptide complex and its interactions with phospholipid micelles. Biochemistry 45 (2006) 2250-2256
13. Czabotar P.E., et al. Structural insights into the degradation of Mcl-1 induced by BH3 domains. Proc. Nat. Acad. Sci. 104 (2007) 6217-6222
14. Cheng Q., Lee H., Li Y., Parks T.P., and Cheng G. Upregulation of Bcl-x and Bfl-1 as a potential mechanism of chemoresistance, where can be overcome by NF-KappaB inhibition. Oncogene 19 (2000) 4936-4940
15. Huang Q., Petros A.M., Virgin H.W., Fesik S.W., and Olejniczak E.T. Solution structure of the BHRF1 protein from epstein-barr virus, a homolog of human Bcl-2. J. Mol. Biol. 332 (2003) 1123-1130
16. Stenmark P., Ogg D., Flodin S., Flores A., Kotenyova T., Nyman T., Nordlund P., and Kursula P. The structure of human collapsin response mediator protein 2, a regulator of axonal growth. J. Neurochem. 101 (2007) 906-917
17. Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Cryst. 26 (1993) 795-800
18. Terwilliger T. Rapid automatic NCS identification using heavy-atom substructures. Acta Crystallogr. Sec. D 58 (2002) 2213-2215
19. Vagin A., and Teplyakov A. MolRep: an automated program for molecular replacement. J. Appl. Cryst. 30 (1997) 1022-1025
20. Perrakis A., Morris R., and Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6 (1999) 458-463
21. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sec. D 53 (1997) 240-255
22. Chandler D. Interfaces and the driving force of hydrophobic assembly. Nature 437 (2005) 640-647
23. Kucharczak J.F., Simmons M.J., Duckett C.S., and Gelinas C. Constitutive proteasome-mediated turnover of Bfl-1/A1 and its processing in response to TNF receptor activation in FL5.12 pro-B cells convert it into a prodeath factor. Cell Death Differ. 12 (2005) 1225-1239
24. Simmons M.J., Fan G., Zong W.X., Degenhardt K., White E., and Gelinas C. Bfl-1/A1 functions, similar to Mcl-1, as a selective tBid and Bak antagonist. Oncogene 27 (2008) 1421-1428
25. Ko J.-K., Choi K.-H., Pan Z., Lin P., Weisleder N., Kim C.-W., and Ma J. The tail-anchoring domain of Bfl1 and HCCS1 targets mitochondrial membrane permeability to induce apoptosis. J. Cell Sci. 120 (2007) 2912-2923
26. Herold M.J., Zeitz J., Pelzer C., Kraus C., Peters A., Wohlleben G., and Berberich I. The stability and anti-apoptotic function of A1 are controlled by its C terminus. J. Biol. Chem. 281 (2006) 13663-13671
27. Suzuki M., Youle R.J., and Tjandra N. Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 103 (2000) 645-654
28. Hinds M.G., Lackmann M., Skea G.L., Harrison P.J., Huang D.C., and Day C.L. The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity. EMBO J. 22 (2003) 1497-1507
29. Chen S., Dai Y., Harada H., Dent P., and Grant S. Mcl-1 down-regulation potentiates ABT-737 lethality by cooperatively inducing Bak activation and Bax translocation. Cancer Res. 67 (2007) 782-791
30. Lee E.F., Czabotar P.E., Smith B.J., Deshayes K., Zobel K., Colman P.M., and Fairlie W.D. Crystal structure of ABT-737 complexed with Bcl-xL: implications for selectivity of antagonists of the Bcl-2 family. Cell Death Differ. 14 (2007) 1711-1713
31. Gouet P., Robert X., and Courcelle E. ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucl. Acid Res. 31 (2003) 3320-3323