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Drosophila IAP1-mediated ubiquitylation controls activation of the initiator caspase DRONC independent of protein degradation.

PLoS genetics - 1 Sept 2011

Lee Tom V, Fan Yun, Wang Shiuan, Srivastava Mayank, Broemer Meike, Meier Pascal, Bergmann Andreas

Abstract excerpt

Ubiquitylation targets proteins for proteasome-mediated degradation and plays important roles in many biological processes including apoptosis. However, non-proteolytic functions of ubiquitylation are also known. In Drosophila, the inhibitor of apoptosis protein 1 (DIAP1) is known to ubiquitylate the initiator caspase DRONC in vitro. Because DRONC protein accumulates in diap1 mutant cells that are kept alive by...

Topics

Animals
Apoptosis
Caspases
Cell Line
Drosophila Proteins
Drosophila melanogaster
Inhibitor of Apoptosis Proteins
Mutation
Proteolysis
Ubiquitin-Activating Enzymes
Ubiquitination

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Identifiers

PMID: 21909282
DOI: 10.1371/journal.pgen.1002261
PMCID: PMC3164697

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Drosophila IAP1-mediated ubiquitylation controls activation of the initiator caspase DRONC independent of protein degradation.PMID 21909282Read ↗

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