SWISS-PROT: RETARDS APOPTOSIS INDUCED BY IL-3 DEPRIVATION. MAY FUNCTION IN THE RESPONSE OF HEMOPOIETIC CELLS TO EXTERNAL SIGNALS AND IN MAINTAINING ENDOTHELIAL SURVIVAL DURING INFECTION.
AIF, apoptosis-inducing factor, provides a caspase-independent link between mitochondria and apoptotic response in the nucleus. When apoptosis is induced, AIF if released from the mitochondria to the cytosol and the nucleus. Microinjected AIF is sufficient to induce apoptosis (independently of caspases).
SWISS-PROT: ATTACH INTEGRAL MEMBRANE PROTEINS TO CYTOSKELETAL ELEMENTS; BIND TO THE ERYTHROCYTE MEMBRANE PROTEIN BAND 4.2, TO NA-K ATPASE, TO THE LYMPHOCYTE MEMBRANE PROTEIN GP85, AND TO THE CYTOSKELETAL PROTEINS FODRIN, TUBULIN, VIMENTIN AND DESMIN. ERYTHROCYTE ANKYRINS ALSO LINK SPECTRIN (BETA CHAIN) TO THE CYTOPLASMIC DOMAIN OF THE ERYTHROCYTES ANION EXCHANGE PROTEIN; THEY RETAIN MOST OR ALL OF THESE BINDING NGE PROTEIN; THEY RETAIN MOST OR ALL OF THESE BINDING FUNCTIONS.
Links release of cytochome-c from the mitochondria to the activation of caspases (caspase-9 then caspase-3) which commits a cell to apoptosis. APAF-1 oligomerizes to form the "apoptosome" along with cytochome-c and caspase-9.
Inhibitor of apoptosis with CARD and Glu-,Pro-rich region. Interacts with Caspase-2,-8 and CED-3, but not with Caspase-1, -3, -9. Selective expression in skeletal muscle and cardiac tissue. [PNAS-USA 95, 5156-5160 (1998)]
BAG-1="Bcl-2 Associated Athanogene-1". SWISS-PROT: BCL-2 BINDING PROTEIN WITH ANTI-APOPTOTIC ACTIVITY. MARKEDLY INCREASES THE ANTI-CELL DEATH FUNCTION OF BCL-2 INDUCED BY VARIOUS STIMULI. INTERACTS WITH ACTIVATED GLUCOCORTICOID RECEPTOR, PROGESTERONE RECEPTOR, AND WITH OTHER MEMBERS OF THE NUCLEAR HORMONE RECEPTOR FAMILY.
SWISS-PROT: IN THE PRESENCE OF AN APPROPRIATE STIMULUS, ACCELERATES PROGRAMED CELL DEATH BY BINDING TO, AND ANTAGONIZING THE A REPRESSOR BCL-2 OR ITS ADENOVIRUS HOMOLOG E1B 19K PROTEIN.
Associated with IgD and (weakly) IgM immunoglobulins on the cell surface of mature B cells. Also associated with Bcl-2/Bcl-XL- and procaspase-8 proteins in the endoplasmic reticulum. Believed to bridge an apoptosis-initiating caspase, like procaspase-8, with the anti-apoptotic regulator Bcl-2 or Bcl-XL.
SWISS-PROT: ACCELERATES PROGRAMED CELL DEATH BY BINDING TO, AND ANTAGONIZING THE APOPTOSIS REPRESSOR BCL-2 OR ITS ADENOVIRUS HOMOLOG E1B 19K PROTEIN. INDUCES THE RELEASE OF CYTOCHROME C, ACTIVATION OF CASPASE-3, AND THEREBY APOPTOSIS.
Bcl-10 (CLAP/CIPER/RCD-1), a caspase recruitment domain-containing protein in the tumor necrosis factor receptor pathway, regulates NF-kappaB activation and apoptosis.
SWISS-PROT:PROLONGS THE SURVIVAL OF HEMATOPOIETIC CELLS IN THE ABSENCE OF REQUIRED GROWTH FACTORS AND ALSO IN THE PRESENCE OF VARIOUS STIMULI INDUCING CELLULAR DEATH. BCL2 BLOCKS APOPTOSIS BECAUSE IT INTERFERES WITH THE ACTIVATION OF CASPASES BY PREVENTING THE RELEASE OF CYTOCHROME C. MIGHT FUNCTION IN AN ANTIOXIDANT PATHWAY TO PREVENT APOPTOSIS AT SITES OF FREE RADICAL GENERATION SUCH AS MITOCHONDRIA
SWISS-PROT: DOMINANT REGULATOR OF APOPTOTIC CELL DEATH. THE LONG FORM DISPLAYS CELL DEATH REPRESSOR ACTIVITY, WHEREAS THE SHORT ISOFORM PROMOTES APOPTOSIS.