KEGG   PATHWAY: ko04215
Entry
ko04215                     Pathway                                
Name
Apoptosis - multiple species
Description
Apoptosis is an evolutionarily conserved process used by multicellular organisms to developmentally regulate cell number or to eliminate cells that are potentially detrimental to the organism. The major players are caspases, caspase inhibitors, members of the Bcl-2 family of pro- and anti-apoptotic proteins and adaptors of the Ced-4/APAF-1 type. Mammals, by comparison with Caenorhabditis and Drosophila, exhibit highly complex extrinsic and intrinsic pathways for apoptosis induction. However, recent analyses of whole genome sequences from cnidarians (e.g. Hydra) suggest that the caspase and Bcl-2 families were already highly complex in cnidarians and that Caenorhabditis and Drosophila lost many of the genes involved in apoptosis.
Class
Cellular Processes; Cell growth and death
Pathway map
ko04215  Apoptosis - multiple species
ko04215

Other DBs
GO: 0006915
Orthology
K03158  tumor necrosis factor receptor superfamily member 1A
K02373  FAS-associated death domain protein
K04398  caspase 8 [EC:3.4.22.61]
K04397  caspase 7 [EC:3.4.22.60]
K02187  caspase 3 [EC:3.4.22.56]
K04726  BH3 interacting domain death agonist
K16341  Bcl-2-like protein 11
K10131  phorbol-12-myristate-13-acetate-induced protein 1
K10132  Bcl-2-binding component 3
K02161  apoptosis regulator Bcl-2
K04570  Bcl-2-like 1 (apoptosis regulator Bcl-X)
K02159  apoptosis regulator BAX
K14021  Bcl-2 homologous antagonist/killer
K08738  cytochrome c
K02084  apoptotic protease-activating factor
K04399  caspase 9 [EC:3.4.22.62]
K10522  diablo
K08669  HtrA serine peptidase 2 [EC:3.4.21.108]
K16943  septin 4
K16060  baculoviral IAP repeat-containing protein 2/3
K04725  E3 ubiquitin-protein ligase XIAP [EC:2.3.2.27]
K08731  baculoviral IAP repeat-containing protein 5
K16679  wengen
K04440  mitogen-activated protein kinase 8/9/10 (c-Jun N-terminal kinase) [EC:2.7.11.24]
K20009  caspase Dronc [EC:3.4.22.-]
K20008  death caspase-1 [EC:3.4.22.-]
K02561  Bcl-2-related ovarian killer protein
K20017  Bcl-2 family protein
K20018  cell death protein Grim
K20014  cell death protein rpr
K20016  cell death protein hid
K16061  baculoviral IAP repeat-containing protein 7/8
K20104  programmed cell death activator egl-1 EGL-1
K20094  cell death protein 9
K20105  cell death protein 4
K20106  cell death protein 3
K02583  tumor necrosis factor receptor superfamily member 16
K08334  beclin
K10586  baculoviral IAP repeat-containing protein 6 (apollon) [EC:2.3.2.23]
K04489  caspase 3A [EC:3.4.22.-]
Reference
  Authors
Fuchs Y, Steller H
  Title
Live to die another way: modes of programmed cell death and the signals emanating from dying cells.
  Journal
Nat Rev Mol Cell Biol 16:329-44 (2015)
DOI:10.1038/nrm3999
Reference
  Authors
Kumar S, Cakouros D
  Title
Transcriptional control of the core cell-death machinery.
  Journal
Trends Biochem Sci 29:193-9 (2004)
DOI:10.1016/j.tibs.2004.02.001
Reference
  Authors
Bergmann A, Steller H
  Title
Apoptosis, stem cells, and tissue regeneration.
  Journal
Sci Signal 3:re8 (2010)
DOI:10.1126/scisignal.3145re8
Reference
  Authors
Zmasek CM, Godzik A
  Title
Evolution of the animal apoptosis network.
  Journal
Cold Spring Harb Perspect Biol 5:a008649 (2013)
DOI:10.1101/cshperspect.a008649
Reference
  Authors
Twomey C, McCarthy JV
  Title
Pathways of apoptosis and importance in development.
  Journal
J Cell Mol Med 9:345-59 (2005)
DOI:10.1111/j.1582-4934.2005.tb00360.x
Reference
  Authors
Nicholson DW
  Title
Caspase structure, proteolytic substrates, and function during apoptotic cell death.
  Journal
Cell Death Differ 6:1028-42 (1999)
DOI:10.1038/sj.cdd.4400598
Reference
  Authors
Wang C, Youle RJ
  Title
The role of mitochondria in apoptosis*.
  Journal
Annu Rev Genet 43:95-118 (2009)
DOI:10.1146/annurev-genet-102108-134850
Reference
  Authors
Choi D, Woo M
  Title
Executioners of apoptosis in pancreatic {beta}-cells: not just for cell death.
  Journal
Am J Physiol Endocrinol Metab 298:E735-41 (2010)
DOI:10.1152/ajpendo.00696.2009
Reference
  Authors
Joza N, Kroemer G, Penninger JM
  Title
Genetic analysis of the mammalian cell death machinery.
  Journal
Trends Genet 18:142-9 (2002)
DOI:10.1016/S0168-9525(01)02618-X
Reference
  Authors
Yan N, Wu JW, Chai J, Li W, Shi Y
  Title
Molecular mechanisms of DrICE inhibition by DIAP1 and removal of inhibition by Reaper, Hid and Grim.
  Journal
Nat Struct Mol Biol 11:420-8 (2004)
DOI:10.1038/nsmb764
Reference
  Authors
Reiter S, Crescenzi M, Galliot B, Buzgariu W
  Title
Hydra, a versatile model to study the homeostatic and developmental functions of cell death.
  Journal
Int J Dev Biol 56:593-604 (2012)
DOI:10.1387/ijdb.123499sr
Reference
  Authors
Lasi M, Pauly B, Schmidt N, Cikala M, Stiening B, Kasbauer T, Zenner G, Popp T, Wagner A, Knapp RT, Huber AH, Grunert M, Soding J, David CN, Bottger A
  Title
The molecular cell death machinery in the simple cnidarian Hydra includes an expanded caspase family and pro- and anti-apoptotic Bcl-2 proteins.
  Journal
Cell Res 20:812-25 (2010)
DOI:10.1038/cr.2010.66
Reference
  Authors
Lasi M, David CN, Bottger A
  Title
Apoptosis in pre-Bilaterians: Hydra as a model.
  Journal
Apoptosis 15:269-78 (2010)
DOI:10.1007/s10495-009-0442-7
Reference
  Authors
Romero A, Novoa B, Figueras A
  Title
The complexity of apoptotic cell death in mollusks: An update.
  Journal
Fish Shellfish Immunol 46:79-87 (2015)
DOI:10.1016/j.fsi.2015.03.038
Reference
  Authors
Potts MB, Cameron S
  Title
Cell lineage and cell death: Caenorhabditis elegans and cancer research.
  Journal
Nat Rev Cancer 11:50-8 (2011)
DOI:10.1038/nrc2984
Reference
  Authors
Lee EF, Young ND, Lim NT, Gasser RB, Fairlie WD
  Title
Apoptosis in schistosomes: toward novel targets for the treatment of schistosomiasis.
  Journal
Trends Parasitol 30:75-84 (2014)
DOI:10.1016/j.pt.2013.12.005
Related
pathway
ko04210  Apoptosis
ko04214  Apoptosis - fly
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