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How the Bcl-2 family of proteins interact to regulate apoptosis.
van Delft, Mark F; Huang, David C S.
Afiliação
  • van Delft MF; The Walter and Eliza Hall Institute of Medical Research, and Department of Medical Biology, University of Melbourne, Parkville, Victoria 3010, Australia.
Cell Res ; 16(2): 203-13, 2006 Feb.
Article em En | MEDLINE | ID: mdl-16474435
Commitment of cells to apoptosis is governed largely by protein-protein interactions between members of the Bcl-2 protein family. Its three sub-families have distinct roles: the BH3-only proteins trigger apoptosis by binding via their BH3 domain to pro-survival relatives, while the pro-apoptotic Bax and Bak have an essential downstream role involving disruption of organellar membranes and induction of caspase activation. The BH3-only proteins act as damage sensors, held inert until their activation by stress signals. Once activated, they were thought to bind promiscuously to pro-survival protein targets but unexpected selectivity has recently emerged from analysis of their interactions. Some BH3-only proteins also bind to Bax and Bak. Whether Bax and Bak are activated directly by these BH3-only proteins, or indirectly as a consequence of BH3-only proteins neutralizing their pro-survival targets is the subject of intense debate. Regardless of this, a detailed understanding of the interactions between family members, which are often selective, has notable implications for designing anti-cancer drugs to target the Bcl-2 family.
Assuntos
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Base de dados: MEDLINE Assunto principal: Apoptose / Proteínas Proto-Oncogênicas c-bcl-2 Limite: Animals Idioma: En Ano de publicação: 2006 Tipo de documento: Article
Buscar no Google
Base de dados: MEDLINE Assunto principal: Apoptose / Proteínas Proto-Oncogênicas c-bcl-2 Limite: Animals Idioma: En Ano de publicação: 2006 Tipo de documento: Article