KEGG   PATHWAY: rro04215
Entry
rro04215                    Pathway                                
Name
Apoptosis - multiple species - Rhinopithecus roxellana (golden snub-nosed monkey)
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
rro04215  Apoptosis - multiple species
rro04215

Other DBs
GO: 0006915
Organism
Rhinopithecus roxellana (golden snub-nosed monkey) [GN:rro]
Gene
104680127  TNFRSF1A; tumor necrosis factor receptor superfamily member 1A [KO:K03158]
104677132  FADD; FAS-associated death domain protein [KO:K02373]
104671864  CASP8; caspase-8 isoform X1 [KO:K04398] [EC:3.4.22.61]
104662231  CASP7; caspase-7 isoform X1 [KO:K04397] [EC:3.4.22.60]
104666783  caspase-3-like [KO:K02187] [EC:3.4.22.56]
104673791  CASP3; caspase-3 [KO:K02187] [EC:3.4.22.56]
104676299  BID; BH3-interacting domain death agonist isoform X1 [KO:K04726]
104680402  BCL2L11; bcl-2-like protein 11 isoform X1 [KO:K16341]
104673006  PMAIP1; phorbol-12-myristate-13-acetate-induced protein 1 [KO:K10131]
104673391  BBC3; bcl-2-binding component 3 [KO:K10132]
104682248  BCL2; apoptosis regulator Bcl-2 isoform X1 [KO:K02161]
104653720  BCL2L1; bcl-2-like protein 1 isoform X1 [KO:K04570]
104666540  BAX; apoptosis regulator BAX isoform X1 [KO:K02159]
104658958  BAK1; bcl-2 homologous antagonist/killer [KO:K14021]
104661761  cytochrome c-like [KO:K08738]
104679886  cytochrome c [KO:K08738]
104672188  cytochrome c [KO:K08738]
104681924  cytochrome c-like [KO:K08738]
115898126  cytochrome c-like [KO:K08738]
115894533  cytochrome c-like [KO:K08738]
115893266  cytochrome c-like [KO:K08738]
115893541  cytochrome c-like [KO:K08738]
115899152  cytochrome c-like [KO:K08738]
104656342  APAF1; apoptotic protease-activating factor 1 isoform X1 [KO:K02084]
104677696  CASP9; caspase-9 isoform X1 [KO:K04399] [EC:3.4.22.62]
104666297  DIABLO; diablo homolog, mitochondrial isoform X1 [KO:K10522]
104674825  HTRA2; serine protease HTRA2, mitochondrial isoform X1 [KO:K08669] [EC:3.4.21.108]
104668438  SEPTIN4; septin-4 isoform X2 [KO:K16943]
104674657  BIRC3; baculoviral IAP repeat-containing protein 3 [KO:K16060]
104674658  BIRC2; baculoviral IAP repeat-containing protein 2 isoform X2 [KO:K16060]
104655196  XIAP; E3 ubiquitin-protein ligase XIAP [KO:K04725] [EC:2.3.2.27]
104659300  BIRC5; baculoviral IAP repeat-containing protein 5 [KO:K08731]
104676194  MAPK9; mitogen-activated protein kinase 9 isoform X1 [KO:K04440] [EC:2.7.11.24]
104678447  MAPK8; mitogen-activated protein kinase 8 isoform X1 [KO:K04440] [EC:2.7.11.24]
104668007  MAPK10; mitogen-activated protein kinase 10 isoform X1 [KO:K04440] [EC:2.7.11.24]
104673078  BOK; bcl-2-related ovarian killer protein [KO:K02561]
104663843  BIRC7; baculoviral IAP repeat-containing protein 7 isoform X1 [KO:K16061]
104659825  NGFR; tumor necrosis factor receptor superfamily member 16 [KO:K02583]
104680067  BECN1; beclin-1 isoform X1 [KO:K08334]
104679208  BECN2; beclin-2 [KO:K08334]
104669445  BIRC6; baculoviral IAP repeat-containing protein 6 isoform X8 [KO:K10586] [EC:2.3.2.23]
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
rro04210  Apoptosis
KO pathway
ko04215   
LinkDB

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