Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis

Overview

Journal Int J Mol Sci

Publisher MDPI

Specialties Biochemistry
Chemistry
Molecular Biology

Date 2010 May 19

PMID 20480043

Citations 34

Authors

Gilles J P Rautureau

Catherine L Day

Mark G Hinds

Affiliations

Soon will be listed here.

Abstract

Intrinsic cell death is mediated by interaction between pro-apoptotic and pro-survival proteins of the B-cell lymphoma-2 (Bcl-2) family. Members of this family are either intrinsically disordered or contain intrinsically disordered regions/domains that are critical to their function. Alternate splicing and post-translational modifications can determine the extent of these disordered regions and are critical for regulating Bcl-2 proteins. Conformational plasticity and structural transitions characterize the interactions within the Bcl-2 family, with conserved sequence motifs on both binding partners required for their molecular recognition.

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References

Klumpp S, Selke D, Krieglstein J . Protein phosphatase type 2C dephosphorylates BAD. Neurochem Int. 2003; 42(7):555-60. DOI: 10.1016/s0197-0186(02)00174-2. View

Willis S, Adams J . Life in the balance: how BH3-only proteins induce apoptosis. Curr Opin Cell Biol. 2005; 17(6):617-25. PMC: 2930980. DOI: 10.1016/j.ceb.2005.10.001. View

Chen L, Willis S, Wei A, Smith B, Fletcher J, Hinds M . Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function. Mol Cell. 2005; 17(3):393-403. DOI: 10.1016/j.molcel.2004.12.030. View

Hsu Y, Wolter K, Youle R . Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis. Proc Natl Acad Sci U S A. 1997; 94(8):3668-72. PMC: 20498. DOI: 10.1073/pnas.94.8.3668. View

Liu X, Dai S, Zhu Y, Marrack P, Kappler J . The structure of a Bcl-xL/Bim fragment complex: implications for Bim function. Immunity. 2003; 19(3):341-52. DOI: 10.1016/s1074-7613(03)00234-6. View

Wilson-Annan J, OReilly L, Crawford S, Hausmann G, Beaumont J, Parma L . Proapoptotic BH3-only proteins trigger membrane integration of prosurvival Bcl-w and neutralize its activity. J Cell Biol. 2003; 162(5):877-87. PMC: 2172834. DOI: 10.1083/jcb.200302144. View

Renshaw S, Dempsey C, Barnes F, Bagstaff S, Dower S, Bingle C . Three novel Bid proteins generated by alternative splicing of the human Bid gene. J Biol Chem. 2003; 279(4):2846-55. DOI: 10.1074/jbc.M309769200. View

Morales A, Olsson A, Celsing F, Osterborg A, Jondal M, Osorio L . Expression and transcriptional regulation of functionally distinct Bmf isoforms in B-chronic lymphocytic leukemia cells. Leukemia. 2003; 18(1):41-7. DOI: 10.1038/sj.leu.2403183. View

Donovan N, Becker E, Konishi Y, Bonni A . JNK phosphorylation and activation of BAD couples the stress-activated signaling pathway to the cell death machinery. J Biol Chem. 2002; 277(43):40944-9. DOI: 10.1074/jbc.M206113200. View

10.

Desagher S, Osen-Sand A, Montessuit S, Magnenat E, Vilbois F, HOCHMANN A . Phosphorylation of bid by casein kinases I and II regulates its cleavage by caspase 8. Mol Cell. 2001; 8(3):601-11. DOI: 10.1016/s1097-2765(01)00335-5. View

11.

Wei M, Zong W, Cheng E, LINDSTEN T, Panoutsakopoulou V, Ross A . Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science. 2001; 292(5517):727-30. PMC: 3049805. DOI: 10.1126/science.1059108. View

12.

Chou J, Li H, Salvesen G, Yuan J, Wagner G . Solution structure of BID, an intracellular amplifier of apoptotic signaling. Cell. 1999; 96(5):615-24. DOI: 10.1016/s0092-8674(00)80572-3. View

13.

Chang B, Minn A, Muchmore S, Fesik S, Thompson C . Identification of a novel regulatory domain in Bcl-X(L) and Bcl-2. EMBO J. 1997; 16(5):968-77. PMC: 1169697. DOI: 10.1093/emboj/16.5.968. View

14.

Ley R, Balmanno K, Hadfield K, Weston C, Cook S . Activation of the ERK1/2 signaling pathway promotes phosphorylation and proteasome-dependent degradation of the BH3-only protein, Bim. J Biol Chem. 2003; 278(21):18811-6. DOI: 10.1074/jbc.M301010200. View

15.

Blagosklonny M, Alvarez M, Fojo A, Neckers L . bcl-2 protein downregulation is not required for differentiation of multidrug resistant HL60 leukemia cells. Leuk Res. 1996; 20(2):101-7. DOI: 10.1016/0145-2126(95)00103-4. View

16.

Deng X, Kornblau S, Ruvolo P, May Jr W . Regulation of Bcl2 phosphorylation and potential significance for leukemic cell chemoresistance. J Natl Cancer Inst Monogr. 2001; (28):30-7. DOI: 10.1093/oxfordjournals.jncimonographs.a024254. View

17.

Aouacheria A, Brunet F, Gouy M . Phylogenomics of life-or-death switches in multicellular animals: Bcl-2, BH3-Only, and BNip families of apoptotic regulators. Mol Biol Evol. 2005; 22(12):2395-416. DOI: 10.1093/molbev/msi234. View

18.

Schinzel A, Kaufmann T, Borner C . Bcl-2 family members: integrators of survival and death signals in physiology and pathology [corrected]. Biochim Biophys Acta. 2004; 1644(2-3):95-105. DOI: 10.1016/j.bbamcr.2003.09.006. View

19.

Day C, Puthalakath H, Skea G, Strasser A, Barsukov I, Lian L . Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands. Biochem J. 2003; 377(Pt 3):597-605. PMC: 1223895. DOI: 10.1042/BJ20031251. View

20.

Willis S, Chen L, Dewson G, Wei A, Naik E, Fletcher J . Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. Genes Dev. 2005; 19(11):1294-305. PMC: 1142553. DOI: 10.1101/gad.1304105. View