Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death

Article Abstract:

The Drosophila inhibitor of apoptosis 1 (DIAP1) encoded by the thread gene prevents cell death caused by mutations in the reaper (rpr) or the head involution defective (hid) genes. The inhibition of cell death is controlled by the baculovirus IAP repeats in the N-terminal of the proteins. Removal of the C-terminal RING motif increases the cell death inhibition of the proteins. Drosophila also produces DIAP2 which is similar in activity to DIAP1. DIAP1 and DIAP2 are structurally similar to the IAPs produced by baculoviruses.

Proteins

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The Drosophila caspase inhibitor DIAP1 is essential for cell survival and is negatively regulated by HID

Article Abstract:

Head Involution Defective (HID) is shown to be capable of blocking the ability of the caspase-dependent cell death inhibitor DIAP1 to inhibit caspase activity. The experiment also provide evidence to indicate that the same type of behavior can be elicited by both Drosophila reaper (RPR) and GRIM genes. The results indicate that HID, RPR and GRIM promotes cell death by disrupting IAP-caspase interactions and that DIAP1 is needed to block caspase activity that induces cell death.

Genetic aspects, Drosophila

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KSR, a novel protein kinase required for RAS signal transduction

Article Abstract:

The kinase suppressor of RAS (KSR) is necessary for the signaling activity of activated RAS by a receptor tyrosine kinase pathway. KSR mutants suppress the phenotype caused by activated RAS. KSR acts upstream or parallel to RAF protein and has no effect on the RAF signaling. The amino acid sequence of KSR is similar to that of RAF kinases. Homologes of KSR are present in Drosophila, Caenorhabditis elegans and mammals.

Analysis, Cellular signal transduction, Mutation (Biology), Mutation, Protein kinases

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