Key to the mitochondrial gate

Article Abstract:

Bax and Bak, the proteins of the Bcl-2 family that promote cell death, stimulate opening of the voltage-dependent anion channel (VDAC), a mitochondrial channel through which the cytochrome c permeates. Researchers have developed two competing models to indicate how cytochrome c is released from mitochondria. It was shown that Bax and Bak permit cytochrome c to pass through VDAC, even though the diameter of VDAC is usually too small to allow cytochrome c to pass. It is proposed that the conformation of VDAC changes after it interacts with Bax and Bak.

Mitochondrial membranes, Mitochondrial membrane

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A death-domain-containing receptor that mediates apoptosis

Article Abstract:

The transfected wsl-1 gene in the 3T3 and 292 cells induces apoptosis. The death domain region of the WSL-1 protein is similar to that of the cell surface receptor, TNFR1. WSL-1 interacts with the TNFR-related molecule TRADD. It also stimulates the NF-KB transcription factor in the 293 cells. The distribution of tissues in the WSL-1 protein is restricted and different from the tissue distribution of the Fas and TNFR1 receptors. The tissues of the WSL-1 are mostly present in the spleen, thymus and peripheral blood lymphocytes.

Cell membranes, Cell receptors, Plasma membranes

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Cloning of a bcl-2 homologue by interaction with adenovirus E1B 19K

Article Abstract:

The E1B 19k protein is part of a DNA virus and aids the virus' apoptosis-inhibiting characteristics. This inhibiting mechanism appears to involve binding a new member of the bcl-2 family called bak for bcl-2 homologous antagonist/killer. Enhanced apoptosis occurs when bak is overexpressed, indicating that E1B 19k inhibits apoptosis by binding one of the genes producing proteins responsible for apoptosis. E1B 19k appears to be a homologue of Bcl-xL which is the cellular protein equivalent in that it also binds bcl-2 proteins.

Proteins, Adenoviruses

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