期刊
MOLECULAR CELL
卷 37, 期 2, 页码 172-182出版社
CELL PRESS
DOI: 10.1016/j.molcel.2009.12.036
关键词
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资金
- National Institutes of Health (NIH) [AI060025, AI074958, AI044220]
- Ellison Medical Foundation
- French Research Ministry [ANR 06 MIME 021 01]
- Centre National de la Recherche Scientifique
- Deutsche Forschungsgemeinschaft
- National Health Services (NHS)
Innate immune responses are critical for the immediate protection against microbial infection. In Drosophila, infection leads to the rapid and robust production of antimicrobial peptides through two NF-kappa B signaling pathways-IMD and Toll. The IMD pathway is triggered by DAP-type peptidoglycan, common to most Gram-negative bacteria. Signaling downstream from the peptidoglycan receptors is thought to involve K63 ubiquitination and caspase-mediated cleavage, but the molecular mechanisms remain obscure. We now show that PGN stimulation causes caspase-mediated cleavage of the imd protein, exposing a highly conserved IAP-binding motif (IBM) at its neo-N terminus. A functional IBM is required for the association of cleaved IMID with the ubiquitin E3-ligase DIAP2. Through its association with DIAP2, IMD is rapidly conjugated with K63-linked polyubiquitin chains. These results mechanistically connect caspase-mediated cleavage and K63 ubiquitination in immune-induced NF-kappa B signaling.
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