Linked Life Data

12397080

Source:http://linkedlifedata.com/resource/pubmed/id/12397080

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
51
pubmed:dateCreated
2002-12-16
pubmed:abstractText
Although loss of the inhibitor of apoptosis (IAP) protein DIAP1 has been shown to result in caspase activation and spontaneous cell death in Drosophila cells and embryos, the point at which DIAP1 normally functions to inhibit caspase activation is unknown. Depletion of the DIAP1 protein in Drosophila S2 cells or the Sf-IAP protein in Spodoptera frugiperda Sf21 cells by RNA interference (RNAi) or cycloheximide treatment resulted in rapid and widespread caspase-dependent apoptosis. Co-silencing of dronc or dark largely suppressed this apoptosis, indicating that DIAP1 is normally required to inhibit an activity dependent on these proteins. Silencing of dronc also inhibited DRICE processing following stimulation of apoptosis, demonstrating that DRONC functions as an apical caspase in S2 cells. Silencing of diap1 or treatment with UV light induced DRONC processing, which occurred in two steps. The first step appeared to occur continuously even in the absence of an apoptotic signal and to be dependent on DARK, because full-length DRONC accumulated when dark was silenced in non-apoptotic cells. In addition, treatment with the proteasome inhibitor MG132 resulted in accumulation of this initially processed form of DRONC, but not full-length DRONC, in non-apoptotic cells. The second step in DRONC processing was observed only in apoptotic cells. These results indicate that the initial step in DRONC processing occurs continuously via a DARK-dependent mechanism in Drosophila cells and that DIAP1 is required to prevent excess accumulation of this first form of processed DRONC, presumably through its ability to act as a ubiquitin-protein ligase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
49644-50
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:12397080-Animals, pubmed-meshheading:12397080-Apoptosis, pubmed-meshheading:12397080-Caspases, pubmed-meshheading:12397080-Cell Death, pubmed-meshheading:12397080-Cell Line, pubmed-meshheading:12397080-Cell Survival, pubmed-meshheading:12397080-Cycloheximide, pubmed-meshheading:12397080-DNA, pubmed-meshheading:12397080-DNA Fragmentation, pubmed-meshheading:12397080-Drosophila, pubmed-meshheading:12397080-Drosophila Proteins, pubmed-meshheading:12397080-Gene Silencing, pubmed-meshheading:12397080-Immunoblotting, pubmed-meshheading:12397080-Inhibitor of Apoptosis Proteins, pubmed-meshheading:12397080-Insects, pubmed-meshheading:12397080-Ligases, pubmed-meshheading:12397080-Protein Binding, pubmed-meshheading:12397080-Protein Synthesis Inhibitors, pubmed-meshheading:12397080-RNA Interference, pubmed-meshheading:12397080-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:12397080-Spodoptera, pubmed-meshheading:12397080-Time Factors, pubmed-meshheading:12397080-Transfection, pubmed-meshheading:12397080-Ultraviolet Rays
pubmed:year
2002
pubmed:articleTitle
The Drosophila DIAP1 protein is required to prevent accumulation of a continuously generated, processed form of the apical caspase DRONC.
pubmed:affiliation
Molecular, Cellular, and Developmental Biology Program, Division of Biology, Kansas State University, Manhattan, KS 66506, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't