Chapter 16
16.1 Introduction
Review
Kerr, J. F., Wyllie, A. H., and Currie, A. R., 1972. Apoptosis: A basic biological
phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer v.
26 p. 239–257.
Wyllie, A. H., Kerr, J. F., and Currie, A. R., 1980. Cell death: the significance of
apoptosis. Int. Rev. Cytol. v. 68 p. 251–306.
16.2 Caspases orchestrate apoptosis by cleaving specific substrates
Review
Fischer, U., Jänicke, R. U., and Schulze-Osthoff, K., 2003. Many cuts to ruin: A
comprehensive update of caspase substrates. Cell Death Differ. v. 10 p. 76–100.
16.3 Executioner caspases are activated by cleavage, whereas initiator caspases are
activated by dimerization
Review
Boatright, K. M., and Salvesen, G. S., 2003. Mechanisms of caspase activation. Curr.
Opin. Cell Biol. v. 15 p. 725–731.
Fuentes-Prior, P., and Salvesen, G. S., 2004. The protein structures that shape caspase
activity, specificity, activation and inhibition. Biochem. J. v. 384 p. 201–232.
Lahm, A., Paradisi, A., Green, D. R., and Melino, G., 2003. Death fold domain
interaction in apoptosis. Cell Death Differ. v. 10 p. 10–12.
Research
Berglund, H., Olerenshaw, D., Sankar, A., Federwisch, M., Mcdonald, N. Q., Driscoll,
P.C. 2000. The Three-Dimensional Solution Structure and Dynamic Properties of
the Human Fadd Death Domain. J. Mol. Biol. v. 302 p. 171–188.
Boatright, K. M., et al., 2003. A unified model for apical caspase activation. Mol. Cell v.
11 p. 529–541.
Huang, B., Eberstadt, M., Olejniczak, E. T., Meadows, R. P., Fesik, S. W. 1996. NMR
structure and mutagenesis of the Fas (APO-1/CD95) death domain. Nature v. 384
p. 638–641.
Riedl, S. J., Fuentes-Prior, P., Renatus, M., Kairies, N., Krapp, S., Huber, R., Salvesen,
G. S., and Bode, W., 2001. Structural basis for the activation of human
procaspase-7. Proc. Natl. Acad. Sci. USA v. 98 p. 14790–14795.
Vaughn, D. E., Rodriguez, J., Lazebnik, Y., Joshua-Tor, L., 1999. Crystal structure of
Apaf-1 caspase recruitment domain: An alpha-helical Greek key fold for
apoptotic signaling. J. Mol. Biol. v. 293 p. 439–447.
16.4 Some inhibitors of apoptosis proteins (IAPs) block caspases
Review
Shi, Y., 2004. Caspase activation, inhibition, and reactivation: A mechanistic view.
Protein Sci. v. 13 p. 1979–1987.
Vaux, D. L., and Silke, J., 2005. IAPs, RINGs and ubiquitylation. Nat. Rev. Mol. Cell
Biol. v. 6 p. 287–297.
16.5 Some caspases have functions in inflammation
Review
Martinon, F., and Tschopp, J., 2004. Inflammatory caspases: Linking an intracellular
innate immune system to autoinflammatory diseases. Cell v. 117 p. 561–574.
16.6 The death receptor pathway of apoptosis transmits external signals
Review
Bodmer, J. L., Schneider, P., and Tschopp, J., 2002. The molecular architecture of the
TNF superfamily. Trends Biochem. Sci. v. 27 p. 19–26.
16.7 Apoptosis signaling by TNFR1 is complex
Review
Aggarwal, B. B., 2003. Signalling pathways of the TNF superfamily: A double-edged
sword. Nat. Rev. Immunol. v. 3 p. 745–756.
Research
Barnhart, B. C., and Peter, M. E., 2003. The TNF receptor 1: A split personality complex.
Cell v. 114 p. 148–150.
16.8 The mitochondrial pathway of apoptosis
Review
Green, D. R., 2000. Apoptotic pathways: paper wraps stone blunts scissors. Cell v. 102 p.
1–4.
16.9 Bcl-2 family proteins mediate and regulate MOMP and apoptosis
Research
Liu, X., Dai, S., Zhu, Y., Marrack, P., and Kappler, J.W. 2003. The structure of a Bclxl/Bim fragment complex: Implications for Bim function. Immunity v. 19 p. 341–
352.
Suzuki, M.,Youle, R. J., and Tjandra, N. 2000. Structure of Bax: Coregulation of dimer
formation and intracellular localization. Cell v. 103 p. 645–654,
McDonnell, J. M., Fushman, D., Milliman, C. L., Korsmeyer, S. J., and Cowburn, D.
1999. Solution structure of the proapoptotic molecule BID: A structural basis for
apoptotic agonists and antagonists. Cell v. 96 p. 625–634,
16.11 The activation of Bax and Bak are controlled by other Bcl-2 family proteins
Review
Danial, N. N., and Korsmeyer, S. J., 2004. Cell death: Critical control points. Cell v. 116
p. 205–219.
16.12 Cytochrome c, released upon MOMP, induces caspase activation
Review
Hill, M. M., Adrain, C., and Martin, S. J., 2003. Portrait of a killer: The mitochondrial
apoptosome emerges from the shadows. Mol. Interv. v. 3 p. 19–26.
Research
Bao, Q., Riedl, S. J., and Shi, Y., 2005. Structure of Apaf-1 in the auto-inhibited form: A
critical role for ADP. Cell Cycle v. 4 p. 1001–1003.
16.15 MOMP can cause caspase-independent cell death
Review
Chipuk, J. E., and Green, D. R., 2005. Do inducers of apoptosis trigger caspaseindependent
cell death? Nat. Rev. Mol. Cell Biol. v. 6 p. 268–275.
16.16 The mitochondrial permeability transition can cause MOMP
Review
Halestrap, A., 2005. Biochemistry: A pore way to die. Nature v. 434 p. 578–579.
16.17 Many discoveries about apoptosis were made in nematodes
Review
Kinchen, J. M., and Hengartner, M. O., 2005. Tales of cannibalism, suicide, and murder:
Programmed cell death in C. elegans. Curr. Top. Dev. Biol. v. 65 p. 1–45.
16.18 Apoptosis in insects has features distinct from mammals and nematodes
Review
Hay, B. A., Huh, J. R., and Guo, M., 2004. The genetics of cell death: Approaches,
insights and opportunities in Drosophila. Nat. Rev. Genet. v. 5 p. 911–922.
16.19 The clearance of apoptotic cells requires cellular interaction
Review
Lauber, K., Blumenthal, S. G., Waibel, M., and Wesselborg, S., 2004. Clearance of
apoptotic cells: getting rid of the corpses. Mol. Cell v. 14 p. 277–287.
Reddien, P. W., and Horvitz, H. R., 2004. The engulfment process of programmed cell
death in Caenorhabditis elegans. Annu. Rev. Cell Dev. Biol. v. 20 p. 193–221.
16.20 Apoptosis plays a role in diseases such as viral infection and cancer
Review
Clem, R. J., 2005. The role of apoptosis in defense against baculovirus infection in
insects. Curr. Top. Microbiol. Immunol. v. 289 p. 113–129.
Green, D. R., and Evan, G. I., 2002. A matter of life and death. Cancer Cell v. 1 p. 19–
30.
Polster, B. M., Pevsner, J., and Hardwick, J. M., 2004. Viral Bcl-2 homologs and their
role in virus replication and associated diseases. Biochim. Biophys. Acta v. 1644
p. 211–227.
16.21 Apoptotic cells are gone but not forgotten
Review
Munoz, L. E., Gaipl, U. S., Franz, S., Sheriff, A., Voll, R. E., Kalden, J. R., and
Herrmann, M., 2005. SLE—a disease of clearance deficiency? Rheumatology
(Oxford) v. 44 p. 1101–1107.
Skoberne, M., Beignon, A. S., Larsson, M., and Bhardwaj, N., 2005. Apoptotic cells at
the crossroads of tolerance and immunity. Curr. Top. Microbiol. Immunol. v. 289
p. 259–292.