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Temporal regulation of Drosophila IAP1 determines caspase functions in sensory organ development

¹ Department of Genetics, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan
² Core Research of Evolutional Science & Technology, Japan Science and Technology Agency, Bunkyo-ku, Tokyo 113-0033, Japan

Correspondence to Masayuki Miura: miura{at}mol.f.u-tokyo.ac.jp

The caspases comprise a family of cysteine proteases that function in various cellular processes, including apoptosis. However, how the balance is struck between the caspases’ role in cell death and their nonapoptotic functions is unclear. To address this issue, we monitored the protein turnover of an endogenous caspase inhibitor, Drosophila IAP1 (DIAP1). DIAP1 is an E3 ubiquitin ligase that promotes the ubiquitination of caspases and thereby prevents caspase activation. For this study, we developed a fluorescent probe to monitor DIAP1 turnover in the external sensory organ precursor (SOP) lineage of living Drosophila. The SOP divides asymmetrically to make the shaft, socket, and sheath cells, and the neuron that comprise each sensory organ. We found that the quantity of DIAP1 changed dramatically depending on the cell type and maturity, and that the temporal regulation of DIAP1 turnover determines whether caspases function nonapoptotically in cellular morphogenesis or cause cell death.

Abbreviations used in this paper: APF, after puparium formation; DIAP1, Drosophila inhibitor of apoptosis protein 1; DmIKK, Drosophila IKK-related kinase; IAP, inhibitor of apoptosis protein; MARCM, mosaic analysis with a repressive cell marker; SOP, sensory organ precursor.

© 2009 Koto et al.
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This article has been cited by other articles:

• Powell, K. (2009). Walking a fine caspase line. JCB 187: 150-150 [Full Text]  

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