Caspase function in programmed cell death

Thornberry NA, Bull HG, Calaycay JR, Chapman KT, Howard AD, Kostura MJ et al. (1992) A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes. Nature 356: 768–774.

Cerretti DP, Kozlosky CJ, Mosley B, Nelson N, Van Ness K, Greenstreet TA et al. (1992) Molecular cloning of the interleukin-1 beta converting enzyme. Science 256: 97–100.

Yuan J, Shaham S, Ledoux S, Ellis HM, Horvitz HR (1993) The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme. Cell 75: 641–652.

Miura M, Zhu H, Rotello R, Hartwieg EA, Yuan J (1993) Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3. Cell 75: 653–660.

Kumar S, Tomooka Y, Noda M (1992) Identification of a set of genes with developmentally down-regulated expression in the mouse brain. Biochem Biophys Res Commun 185: 1155–1161.

Kumar S, Kinoshita M, Noda M, Copeland NG, Jenkins NA (1994) Induction of apoptosis by mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1β-converting enzyme. Genes Dev 8: 1613–1626.

Lamkanfi M, Declercq W, Kalai M, Saelens X, Vandenabeele P (2002) Alice in caspase land. A phylogenetic analysis of caspases from worm to man. Cell Death Differ 9: 358–361.

Fuentes-Prior P, Salvesen GS (2004) The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem J 384: 201–232.

Degterev A, Boyce M, Yuan J (2003) A decade of caspases. Oncogene 22: 8543–8567.

Ellis HM, Horvitz HR (1986) Genetic control of programmed cell death in the nematode C. elegans. Cell 44: 817–829.

Shaham S (1998) Identification of multiple Caenorhabditis elegans caspases and their potential roles in proteolytic cascades. J Biol Chem 273: 35109–35117.

Lettre G, Hengartner MO (2006) Developmental apoptosis in C. elegans: a complex CEDnario. Nat Rev Mol Cell Biol 7: 97–108.

Yan N, Chai J, Lee ES, Gu L, Liu Q, He J et al. (2005) Structure of the CED-4–CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans. Nature 437: 831–837.

Song Z, McCall K, Steller H (1997) DCP-1, a Drosophila cell death protease essential for development. Science 275: 536–540.

Chen P, Rodriguez A, Erskine R, Thach T, Abrams JM (1998) Dredd, a novel effector of the apoptosis activators reaper, grim and hid in Drosophila. Dev Biol 201: 202–216.

Fraser AG, Evan GI (1997) Identification of a Drosophila melanogaster ICE/CED-3-related protease, drICE. EMBO J 16: 2805–2813.

Dorstyn L, Colussi PA, Quinn LM, Richardson H, Kumar S (1999) DRONC, a novel ecdysone-inducible Drosophila caspase. Proc Natl Acad Sci USA 96: 4307–4312.

Dorstyn L, Read SH, Quinn LM, Richardson H, Kumar S (1999) DECAY, a novel Drosophila caspase related to mammalian caspase-3 and caspase-7. J Biol Chem 274: 30778–30783.

Harvey NL, Daish T, Mills K, Dorstyn L, Quinn LM, Read SH et al. (2001) Characterization of the Drosophila caspase, DAMM. J Biol Chem 276: 25342–25350.

Doumanis J, Quinn L, Richardson H, Kumar S (2001) STRICA, a novel Drosophila caspase with an unusual serine/threonine-rich prodomain, interacts with DIAP1 and DIAP2. Cell Death Diff 8: 387–394.

Kumar S, Doumanis J (2000) The fly caspases. Cell Death Diff 7: 1039–1044.

Leulier F, Rodriguez A, Khush RS, Abrams JM, Lemaitre B (2000) The Drosophila caspase Dredd is required to resist gram-negative bacterial infection. EMBO Rep 1: 353–358.

Hu S, Yang X (2000) dFADD, a novel death domain-containing adapter protein for the Drosophila caspase DREDD. J Biol Chem 275: 30761–30764.

Zhou R, Silverman N, Hong M, Liao DS, Chung Y, Chen ZJ et al. (2005) The role of ubiquitination in Drosophila innate immunity. J Biol Chem 280: 34048–34055.

Huh JR, Vernooy SY, Yu H, Yan N, Shi Y, Guo M et al. (2004) Multiple apoptotic caspase cascades are required in nonapoptotic roles for Drosophila spermatid individualization. PLoS Biol 2: E15.

Daish TJ, Mills K, Kumar S (2004) Drosophila caspase DRONC is required for specific developmental cell death pathways and stress-induced apoptosis. Dev Cell 7: 909–915.

Chew SK, Akdemir F, Chen P, Lu WJ, Mills K, Daish T et al. (2004) The apical caspase dronc governs programmed and unprogrammed cell death in Drosophila. Dev Cell 7: 897–907.

Xu D, Li Y, Arcaro M, Lackey M, Bergmann A (2005) The CARD-carrying caspase Dronc is essential for most, but not all, developmental cell death in Drosophila. Development 132: 2125–2134.

Waldhuber M, Emoto K, Petritsch C (2005) The Drosophila caspase DRONC is required for metamorphosis and cell death in response to irradiation and developmental signals. Mech Dev 122: 914–927.

Kondo S, Senoo-Matsuda N, Hiromi Y, Miura M (2006) DRONC coordinates cell death and compensatory proliferation. Mol Cell Biol 26: 7258–7268.

Mills K, Daish T, Kumar S (2005) The function of the Drosophila caspase DRONC in cell death and development. Cell Cycle 4: 744–746.

Kumar S (2004) Migrate, differentiate, proliferate, or die: pleiotropic functions of an apical ‘apoptotic caspase’. Sci STKE 2004: pe49.

Meier P, Silke J, Leevers SJ, Evan GI (2000) The Drosophila caspase DRONC is regulated by DIAP1. EMBO J 19: 598–611.

Quinn LM, Dorstyn L, Mills K, Colussi PA, Chen P, Coombe M et al. (2000) An essential role for the caspase Dronc in developmentally programmed cell death in Drosophila. J Biol Chem 275: 40416–40424.

Hawkins CJ, Yoo SJ, Peterson EP, Wang SL, Vernooy SY, Hay BA (2000) The Drosophila caspase Dronc cleaves following glutamate or aspartate and is regulated by Diap1, Hid and Grim. J Biol Chem 275: 27084–27093.

Leulier F, Ribeiro PS, Palmer E, Tenev T, Takahashi K, Robertson D et al. (2006) Systematic in vivo RNAi analysis of putative components of the Drosophila cell death machinery. Cell Death Differ 13: 1663–1674.

Cakouros D, Daish T, Martin D, Baehrecke EH, Kumar S (2002) Ecdysone-induced expression of the caspase DRONC during hormone dependent programmed cell death in Drosophila is regulated by Broad-Complex. J Cell Biol 157: 985–995.

Cakouros D, Daish TJ, Kumar S (2004) Ecdysone receptor directly binds the promoter of the Drosophila caspase dronc regulating its expression in specific tissues. J Cell Biol 165: 631–640.

Cakouros D, Daish TJ, Mills K, Kumar S (2004) An arginine-histone methyl transferase, CARMER, coordinates ecdysone-mediated apoptosis in Drosophila cells. J Biol Chem 279: 18467–18471.

Daish T, Cakouros D, Kumar S (2003) Distinct promoter regions regulate spatial and temporal expression of the Drosophila caspase dronc. Cell Death Differ 10: 1348–1356.

Kumar S, Cakouros D (2004) Transcriptional control of the core cell death machinery. Trends Biochem Sci 29: 193–199.

Dorstyn L, Read S, Cakouros D, Huh JR, Hay BA, Kumar S (2002) The role of cytochrome c in caspase activation in Drosophila cells. J Cell Biol 156: 1089–1098.

Kuranaga E, Kanuka H, Tonoki A, Takemoto K, Tomioka T, Kobayashi M et al. (2006) Drosophila IKK-related kinase regulates nonapoptotic function of caspases via degradation of IAPs. Cell 126: 583–596.

Muro I, Berry DL, Huh JR, Chen CH, Huang H, Yoo SJ et al. (2006) The Drosophila caspase Ice is important for many apoptotic cell deaths and for spermatid individualization, a nonapoptotic process. Development 133: 3305–3315.

Xu D, Wang Y, Willecke R, Chen Z, Ding T, Bergmann A (2006) The effector caspases drICE and dcp-1 have partially overlapping functions in the apoptotic pathway in Drosophila. Cell Death Differ 13: 1697–1706.

Kilpatrick ZE, Cakouros D, Kumar S (2005) Ecdysone-mediated up-regulation of the effector caspase DRICE is required for hormone-dependent apoptosis in Drosophila cells. J Biol Chem 280: 11981–11986.

Fraser AG, McCarthy NJ, Evan GI (1997) drICE is an essential caspase required for apoptotic activity in Drosophila cells. EMBO J 16: 6192–6199.

Enari M, Sakahira H, Yokoyama H, Okawa K, Iwamatsu A, Nagata S (1998) A caspase activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391: 43–50.

Yokoyama H, Mukae N, Sakahira H, Okawa K, Iwamatsu A, Nagata S (2000) A novel activation mechanism of caspase-activated DNase from Drosophila melanogaster. J Biol Chem 275: 12978–12986.

McCall K, Steller H (1998) Requirement for DCP-1 caspase during Drosophila oogenesis. Science 279: 230–234.

Laundrie B, Peterson JS, Baum JS, Chang JC, Fileppo D, Thompson SR et al. (2003) Germline cell death is inhibited by P-element insertions disrupting the dcp-1/pita nested gene pair in Drosophila. Genetics 165: 1881–1888.

Lee CY, Clough EA, Yellon P, Teslovich TM, Stephan DA, Baehrecke EH (2003) Genome-wide analyses of steroid- and radiation-triggered programmed cell death in Drosophila. Curr, Biol 13: 350–357.

Wang SL, Hawkins CJ, Yoo SJ, Muller HA, Hay BA (1999) The Drosophila caspase inhibitor DIAP1 is essential for cell survival and is negatively regulated by HID. Cell 98: 453–463.

Goyal L, McCall K, Agapite J, Hartwieg E, Steller H (2000) Induction of apoptosis by Drosophila reaper, hid and grim through inhibition of IAP function. EMBO J 19: 589–597.

Colussi PA, Quinn LM, Huang DCS, Coombe M, Read SH, Richardson H et al. (2000) Debcl, a pro-apoptotic Bcl-2 homologue, is a component of the Drosophila cell death machinery. J Cell Biol 148: 703–714.

Quinn L, Coomb M, Mills K, Daish T, Colussi P, Kumar S et al. (2003) Buffy, a Drosophila Bcl-2 related protein, has anti-apoptotic and cell cycle inhibitory function. EMBO J 22: 3568–3579.

Vaux DL, Silke J (2005) IAPs, RINGs and ubiquitylation. Nat Rev Mol Cell Biol 6: 287–297.

Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES et al. (1997) Cytochrome c and dATP-dependent formation of Apaf1/caspase-9 complex initiates the apoptotic protease cascade. Cell 91: 479–489.

Dorstyn L, Kumar S (2006) A cytochrome c-free fly apoptosome. Cell Death Differ 13: 1049–1051.

Mills K, Daish T, Harvey KF, Pfleger CM, Hariharan IK, Kumar S (2006) The Drosophila melanogaster Apaf-1 homologue ARK is required for most, but not all, programmed cell death. J Cell Biol 172: 809–815.

Srivastava M, Scherr H, Lackey M, Xu D, Chen Z, Lu J et al. (2006) ARK, the Apaf-1 related killer in Drosophila, requires diverse domains for its apoptotic activity. Cell Death Differ (in press).

Akdemir F, Farkas R, Chen P, Juhasz G, Medved’ova L, Sass M et al. (2006) Autophagy occurs upstream or parallel to the apoptosome during histolytic cell death. Development 133: 1457–1465.

Varkey J, Chen P, Jemmerson R, Abrams JM (1999) Altered cytochrome c display precedes apoptotic cell death in Drosophila. J Cell Biol 144: 701–710.

Zimmermann KC, Ricci JE, Droin NM, Green DR (2002) The role of ARK in stress-induced apoptosis in Drosophila cells. J Cell Biol 156: 1077–1087.

Dorstyn L, Mills K, Lazebnik Y, Kumar S (2004) The two cytochrome c species, DC3 and DC4, are not required for caspase activation and apoptosis in Drosophila cells. J Cell Biol 167: 405–410.

Means JC, Muro I, Clem RJ (2006) Lack of involvement of mitochondrial factors in caspase activation in a Drosophila cell-free system. Cell Death Differ 13: 1222–1234.

Yu X, Wang L, Acehan D, Wang X, Akey CW (2006) Three-dimensional structure of a double apoptosome formed by the Drosophila Apaf-1 related killer. J Mol Biol 355: 577–589.

Acehan D, Jiang X, Morgan DG, Heuser JE, Wang X, Akey CW (2002) Three-dimensional structure of the apoptosome. Implications for assembly, procaspase-9 binding, and activation. Mol Cell 9: 423–432.

Hakem R, Hakem A, Duncan GS, Henderson JT, Woo M, Soengas MS et al. (1998) Differential requirement for caspase-9 in apoptotic pathways in vivo. Cell 94: 339–352.

Kuida K, Haydar TF, Kuan C-Y, Gu Y, Taya C, Karasuyama H et al. (1998) Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9. Cell 94: 325–337.

Kuida K, Zheng TS, Na S, Kuan C, Yang D, Karasuyama H et al. (1996) Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature 384: 368–372.

Cecconi F, Alvarez-Bolado G, Meyer BI, Roth KA, Gruss P (1998) Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development. Cell 94: 727–737.

Yoshida H, Kong YY, Yoshida R, Elia AJ, Hakem A, Hakem R et al. (1998) Apaf1 is required for mitochondrial pathways of apoptosis and brain development. Cell 94: 739–750.

Honarpour N, Du C, Richardson JA, Hammer RE, Wang X, Herz J (2000) Adult Apaf-1-deficient mice exhibit male infertility. Dev Biol 218: 248–258.

Okamoto H, Shiraishi H, Yoshida H (2006) Histological analyses of normally grown, fertile Apaf1-deficient mice. Cell Death Differ 13: 668–671.

Marsden VS, O’Connor L, O’Reilly LA, Silke J, Metcalf D, Ekert PG et al. (2002) Apoptosis initiated by Bcl-2-regulated caspase activation independently of the cytochrome c/Apaf-1/caspase-9 apoptosome. Nature 419: 634–637.

Marsden VS, Ekert PG, Van Delft M, Vaux DL, Adams JM, Strasser A (2004) Bcl-2-regulated apoptosis and cytochrome c release can occur independently of both caspase-2 and caspase-9. J Cell Biol 165: 775–780.

Ekert PG, Read SH, Silke J, Marsden VS, Kaufmann H, Hawkins CJ et al. (2004) Apaf-1 and caspase-9 accelerate apoptosis, but do not determine whether factor-deprived or drug-treated cells die. J Cell Biol 165: 835–842.

Baliga C, Kumar S (2003) The Apaf-1/cytochrome c apoptosome: an essential initiator of caspase activation or just a sideshow? Cell Death Differ 10: 15–17.

Hao Z, Duncan GS, Chang CC, Elia A, Fang M, Wakeham A et al. (2005) Specific ablation of the apoptotic functions of cytochrome c reveals a differential requirement for cytochrome c and Apaf-1 in apoptosis. Cell 121: 579–591.

Boldin MP, Goncharov TM, Goltsev YV, Wallach D (1996) Involvement of MACH, a novel Mort1/FADD-interacting protease, in Fas/APO1- and TNF receptor-induced cell death. Cell 85: 803–815.

Muzio M, Chinnaiyan AM, Kischkel FC, O’Rourke K, Shevchenko A, Scaffidi C et al. (1996) FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 85: 817–827.

Varfolomeev EE, Schuchmann M, Luria V, Chiannilkulchai N, Beckmann JS, Mett IL et al. (1998) Targeted disruption of the mouse caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally. Immunity 9: 267–276.

Kang TB, Ben-Moshe T, Varfolomeev EE, Pewzner-Jung Y, Yogev N, Jurewicz A et al. (2004) Caspase-8 serves both apoptotic and nonapoptotic roles. J Immunol 173: 2976–2984.

Chun HJ, Zheng L, Ahmad M, Wang J, Speirs CK, Siegel RM et al. (2002) Pleiotropic defects in lymphocyte activation caused by caspase-8 mutations lead to human immunodeficiency. Nature 419: 395–399.

Yeh WC, de la Pompa JL, McCurrach ME, Shu H-B, Elia AJ, Shahinian A et al. (1998) FADD: essential for embryo development and signaling from some, but not all, inducers of apoptosis. Science 279: 1954–1958.

Zhang J, Cado D, Kabra NH, Winoto A (1998) Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/MORT1. Nature 392: 296–299.

Kabra NH, Kang C, Hsing LC, Zhang J, Winoto A (2001) T cell-specific FADD-deficient mice: FADD is required for early T cell development. Proc Natl Acad Sci USA 98: 6307–6312.

Zhang Y, Rosenberg S, Wang H, Imtiyaz HZ, Hou YJ, Zhang J (2005) Conditional Fas-associated death domain protein (FADD): GFP knockout mice reveal FADD is dispensable in thymic development but essential in peripheral T cell homeostasis. J Immunol 175: 3033–3044.

Kischkel FC, Lawrence DA, Tinel A, LeBlanc H, Virmani A, Schow P et al. (2001) Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8. J Biol Chem 276: 46639–46646.

Milhas D, Cuvillier O, Therville N, Clave P, Thomsen M, Levade T et al. (2005) Caspase-10 triggers Bid cleavage and caspase cascade activation in FasL-induced apoptosis. J Biol Chem 280: 19836–19842.

Engels IH, Totzke G, Fischer U, Schulze-Osthoff K, Janicke RU (2005) Caspase-10 sensitizes breast carcinoma cells to TRAIL-induced but not tumor necrosis factor-induced apoptosis in a caspase-3-dependent manner. Mol Cell Biol 25: 2808–2818.

Takahashi K, Kawai T, Kumar H, Sato S, Yonehara S, Akira S (2006) Roles of caspase-8 and caspase-10 in innate immune responses to double-stranded RNA. J Immunol 176: 4520–4524.

Zhu S, Hsu AP, Vacek MM, Zheng L, Schaffer AA, Dale JK et al. (2006) Genetic alterations in caspase-10 may be causative or protective in autoimmune lymphoproliferative syndrome. Hum Genet 119: 284–294.

Shin MS, Kim HS, Kang CS, Park WS, Kim SY, Lee SN et al. (2002) Inactivating mutations of CASP10 gene in non-Hodgkin lymphomas. Blood 99: 4094–4099.

Park WS, Lee JH, Shin MS, Park JY, Kim HS, Lee JH et al. (2002) Inactivating mutations of the caspase-10 gene in gastric cancer. Oncogene 21: 2919–2925.

Butt AJ, Harvey NL, Parasivam G, Kumar S (1998) Dimerization and autoprocessing of the Nedd2(caspase-2) precursor requires both the prodomain and the carboxyl-terminal regions. J Biol Chem 273: 6763–6768.

Baliga BC, Read SH, Kumar S (2004) The biochemical mechanism of caspase-2 activation. Cell Death Differ 11: 1234–1241.

Shearwin-Whyatt LM, Harvey NL, Kumar S (2000) Subcellular localization and CARD-dependent oligomerization of the death adaptor RAIDD. Cell Death Diff 7: 155–165.

Read SH, Baliga BB, Ekert P, Vaux DL, Kumar S (2002) A novel Apaf-1-independent putative caspase-2 activation complex. J Cell Biol 159: 739–745.

Tinel A, Tschopp J (2004) The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress. Science 304: 843–846.

O’Reilly LA, Ekert P, Harvey N, Marsden V, Cullen L, Vaux DL et al. (2002) Caspase-2 is not required for thymocyte or neuronal apoptosis even though cleavage of caspase-2 is mediated by Apaf-1 and caspase-9. Cell Death Diff 9: 832–841.

Colussi PA, Harvey NL, Kumar S (1998) Prodomain-dependent nuclear localization of the caspase-2(Nedd2) precursor. J Biol Chem 273: 24535–24542.

Mancini M, Machamer CE, Roy S, Nicholson DW, Thornberry NA, Casciola-Rosen LA et al. (2000) Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis. J Cell Biol 149: 603–612.

Baliga BC, Colussi PA, Read SH, Dias MM, Jans DA, Kumar S (2003) Role of prodomain in importin-mediated nuclear localization and activation of caspase-2. J Biol Chem 278: 4899–4905.

Zhivotovsky B, Orrenius S (2005) Caspase-2 function in response to DNA damage. Biochem Biophys Res Commun 331: 859–867.

Wagner KW, Engels IH, Deveraux QL (2004) Caspase-2 can function upstream of bid cleavage in the TRAIL apoptosis pathway. J Biol Chem 279: 35047–35052.

Shin S, Lee Y, Kim W, Ko H, Choi H, Kim K (2005) Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing procaspase-8. EMBO J 24: 3532–3542.

Tu S, McStay GP, Boucher LM, Mak T, Beere HM, Green DR (2006) In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis. Nat Cell Biol 8: 72–77.

Bonzon C, Bouchier-Hayes L, Pagliari LJ, Green DR, Newmeyer DD (2006) Caspase-2-induced apoptosis requires bid cleavage: a physiological role for bid in heat shock-induced death. Mol Biol Cell 17: 2150–2157.

Nutt LK, Margolis SS, Jensen M, Herman CE, Dunphy WG, Rathmell JC et al. (2005) Metabolic regulation of oocyte cell death through the CaMKII-mediated phosphorylation of caspase-2. Cell 123: 89–103.

Lavrik IN, Golks A, Baumann S, Krammer PH (2006) Caspase-2 is activated at the CD95 death-inducing signaling complex in the course of CD95-induced apoptosis. Blood 108: 559–565.

Harvey NL, Butt A, Kumar S (1997) Functional activation of Nedd2/ICH-1 (caspase-2) is an early process in apoptosis. J Biol Chem 272: 13134–13139.

Kumar S (1995) Inhibition of apoptosis by antisense Nedd2 expression. FEBS Lett 368: 69–72.

Guo Y, Srinivasula SM, Druilhe A, Fernandes-Alnemri T, Alnemri ES (2002) Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria. J Biol Chem 277: 13430–13437.

Troy CM, Shelanski ML (2003) Caspase-2 redux. Cell Death Differ 10: 101–107.

Paroni G, Henderson C, Schneider C, Brancolini C (2002) Caspase-2 can trigger cytochrome c release and apoptosis from the nucleus. J Biol Chem 277: 15147–15161.

Colussi PA, Harvey NL, Shearwin-Whyatt LM, Kumar S (1998) Conversion of procaspase-3 to an autoactivating caspase by fusion to the caspase-2 prodomain. J Biol Chem 273: 26566–26570.

Lassus P, Opitz-Araya X, Lazebnik Y (2002) Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization. Science 297: 1352–1354.

Robertson JD, Enoksson M, Suomela M, Zhivotovsky B, Orrenius S (2002) Caspase-2 acts upstream of mitochondria to promote cytochrome c release during etoposide-induced apoptosis. J Biol Chem 277: 29803–29809.

Bergeron L, Perez GI, Macdonald G, Shi L, Sun Y, Jurisicova A et al. (1998) Defects in regulation of apoptosis in caspase-2-deficient mice. Genes Dev 12: 1304–1314.

Milleron RS, Bratton SB (2006) Heat shock induces apoptosis independently of any known initiator caspase-activating complex. J Biol Chem 281: 16991–17000.

Troy CM, Rabacchi SA, Hohl JB, Angelastro JM, Greene LA, Shelanski ML (2001) Death in the balance: alternative participation of the caspase-2 and -9 pathways in neuronal death induced by nerve growth factor deprivation. J Neurosci 21: 5007–5016.

Porter AG, Janicke RU (1999) Emerging roles of caspase-3 in apoptosis. Cell Death Differ 6: 99–104.

Lakhani SA, Masud A, Kuida K, Porter Jr GA, Booth CJ, Mehal WZ et al. (2006) Caspases 3 and 7: key mediators of mitochondrial events of apoptosis. Science 311: 847–851.

Thornberry NA, Rano TA, Peterson EP, Rasper DM, Timkey T, Garcia-Calvo M et al. (1997) A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J Biol Chem 272: 17907–17911.

Takahashi A, Alnemri ES, Lazebnik YA, Fernandes-Alnemri T, Litwack G, Moir RD et al. (1996) Cleavage of lamin A by Mch2 alpha but not CPP32: multiple interleukin 1 beta-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis. Proc Natl Acad Sci USA 93: 8395–8400.

Zheng TS, Hunot S, Kuida K, Flavell RA (1999) Caspase knockouts: matters of life and death. Cell Death Differ 6: 1043–1053.

Loegering DA, Ruchaud S, Earnshaw WC, Kaufmann SH (2006) Evaluation of the role of caspase-6 in anticancer drug-induced apoptosis. Cell Death Differ 13: 346–347.

Thome M, Schneider P, Hofmann K, Fickenscher H, Meinl E, Neipel F et al. (1997) Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. Nature 386: 517–521.

Irmler M, Thome M, Hahne M, Schneider P, Hofmann K, Steiner V et al. (1997) Inhibition of death receptor signals by cellular FLIP. Nature 388: 190–195.

Thome M, Tschopp J (2001) Regulation of lymphocyte proliferation and death by FLIP. Nat Rev Immunol 1: 50–58.

Micheau O, Tschopp J (2003) Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 114: 181–190.

Chang L, Kamata H, Solinas G, Luo JL, Maeda S, Venuprasad K et al. (2006) The E3 ubiquitin ligase itch couples JNK activation to TNFalpha-induced cell death by inducing c-FLIP(L) turnover. Cell 124: 601–613.

Yeh WC, Itie A, Elia AJ, Ng M, Shu HB, Wakeham A et al. (2000) Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development. Immunity 12: 633–642.

Vaux DL, Silke J (2003) Mammalian mitochondrial IAP binding proteins. Biochem Biophys Res Commun 304: 499–504.

Okada H, Suh WK, Jin J, Woo M, Du C, Elia A et al. (2002) Generation and characterization of Smac/DIABLO-deficient mice. Mol Cell Biol 22: 3509–3517.

Martins LM, Morrison A, Klupsch K, Fedele V, Moisoi N, Teismann P et al. (2004) Neuroprotective role of the Reaper-related serine protease HtrA2/Omi revealed by targeted deletion in mice. Mol Cell Biol 24: 9848–9862.

Harlin H, Reffey SB, Duckett CS, Lindsten T, Thompson CB (2001) Characterization of XIAP-deficient mice. Mol Cell Biol 21: 3604–3608.

Beauparlant P, Shore GC (2003) Therapeutic activation of caspases in cancer: a question of selectivity. Curr Opin Drug Discov Devel 6: 179–187.

Schimmer AD, Dalili S, Batey RA, Riedl SJ (2006) Targeting XIAP for the treatment of malignancy. Cell Death Differ 13: 179–188.