Editing Apoptosis (section)

==== Common components ====

Following ''TNF-R1'' and ''Fas'' activation in mammalian cells{{Citation needed|reason=This is only relevant Type II (pancreatic B-cells and hemaetapoetic stem cells), FAS depdnent apoptosis is indepdnent of MOMP|date=October 2020}} a balance between proapoptotic ([[Bcl-2-associated X protein|BAX]],<ref name="bax">{{cite journal | vauthors = Murphy KM, Ranganathan V, Farnsworth ML, Kavallaris M, Lock RB | title = Bcl-2 inhibits Bax translocation from cytosol to mitochondria during drug-induced apoptosis of human tumor cells | journal = Cell Death and Differentiation | volume = 7 | issue = 1 | pages = 102–111 | date = January 2000 | pmid = 10713725 | doi = 10.1038/sj.cdd.4400597 | doi-access = free | author-link4 = Maria Kavallaris }}</ref> [[BH3 interacting domain death agonist|BID]], [[Bcl-2 homologous antagonist killer|BAK]], or [[Bcl-2-associated death promoter|BAD]]) and anti-apoptotic (''[[Bcl-Xl]]'' and ''[[Bcl-2]]'') members of the ''Bcl-2'' family are established. This balance is the proportion of proapoptotic [[Protein dimer|homodimers]] that form in the outer-membrane of the mitochondrion. The proapoptotic homodimers are required to make the mitochondrial membrane permeable for the release of caspase activators such as cytochrome c and SMAC. Control of proapoptotic proteins under normal cell conditions of nonapoptotic cells is incompletely understood, but in general, Bax or Bak are activated by the activation of BH3-only proteins, part of the [[Bcl-2]] family.<ref>{{cite journal | vauthors = Westphal D, Kluck RM, Dewson G | title = Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis | journal = Cell Death and Differentiation | volume = 21 | issue = 2 | pages = 196–205 | date = February 2014 | pmid = 24162660 | pmc = 3890949 | doi = 10.1038/cdd.2013.139 }}</ref>