Sandbox Reserved 1122: Difference between revisions

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Bcl-2 localized on external mitochondrial membrane can also inhibit the release of cytochrome c from mitochondria. <ref>[http://science.sciencemag.org/content/275/5303/1132.full The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis] </ref> <ref>[http://science.sciencemag.org/content/275/5303/1129.full Prevention of Apoptosis by Bcl-2: Release of Cytochrome c from Mitochondria Blocked] </ref>
Bcl-2 localized on external mitochondrial membrane can also inhibit the release of cytochrome c from mitochondria. <ref>[http://science.sciencemag.org/content/275/5303/1132.full The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis] </ref> <ref>[http://science.sciencemag.org/content/275/5303/1129.full Prevention of Apoptosis by Bcl-2: Release of Cytochrome c from Mitochondria Blocked] </ref>
=== Regulation of proinflammatory caspase-1 activation ===
NALP1 is a member of a NLR-family proteins. Its function is to activate the members of the proinflammatory caspase family which participate in cytokines activation pathway (especially caspase-1). The Bcl-2 loop regions between the BH3 and BH4 bind NALP1. This interaction is exclusively reserved to two members of Bcl-2 family: Bcl-XL and Bcl-2 itself because this interacting region is highly variable in Bcl-2 family. By binding to NALP1, Bcl-2 inhibits the inflammatory caspase activation. Hence, it protects cell from the stress.
The posttranslational modifications found on the loops between BH3 and BH4 modify the anti-apoptotic activity of Bcl-2. Hence, the Bcl-2 binding to NALP1 can be affected by these modifications. <ref>[http://www.sciencedirect.com/science/article/pii/S0092867407003042 Bcl-2 and Bcl-XL Regulate Proinflammatory Caspase-1 Activation by Interaction with NALP1] </ref>


== Disease ==
== Disease ==