Bcl-2 proteins: regulators of apoptosis or of mitochondrial homeostasis?
| Autor: | Vander Heiden Mg, Craig B. Thompson |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Programmed cell death
biology Mitochondrial Permeability Transition Pore Endoplasmic reticulum Bcl-2 family Membrane Proteins Apoptosis Cytochrome c Group Cell Biology Mitochondrion Mitochondrial Membrane Transport Proteins Ion Channels Mitochondria Cell biology Necrosis Mitochondrial membrane transport protein Proto-Oncogene Proteins c-bcl-2 Caspases biology.protein Animals Homeostasis Humans Gene Ion channel |
| Zdroj: | Nature Cell Biology. 1:E209-E216 |
| ISSN: | 1476-4679 1465-7392 |
| Popis: | Programmed cell death (apoptosis) is used by multicellular organisms during development and to maintain homeostasis within mature tissues. One of the first genes shown to regulate apoptosis was bcl-2. Subsequently, a number of Bcl-2-related proteins have been identified. Despite overwhelming evidence that Bcl-2 proteins are evolutionarily conserved regulators of apoptosis, their precise biochemical function remains controversial. Three biochemical properties of Bcl-2 proteins have been identified: their ability to localize constitutively and/or inducibly to the outer mitochondrial, outer nuclear and endoplasmic reticular membranes, their ability to form heterodimers with proteins bearing an amphipathic helical BH3 domain, and their ability to form ion-conducting channels in synthetic membranes. The discovery that mitochondria can play a key part in the induction of apoptosis has focused attention on the role that Bcl-2 proteins may have in regulating either mitochondrial physiology or mitochondria-dependent caspase activation. Here we attempt to synthesize our current understanding of the part played by mitochondria in apoptosis with a consideration of how Bcl-2 proteins might control cell death through an ability to regulate mitochondrial physiology. |
| Databáze: | OpenAIRE |
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