Research

The apoptosome in insect cells

       In mammalian cells, caspase activation is initiated by a macromolecular complex called the apoptosome, consisting of Apaf-1, caspase-9, and cytochrome c.  While the mammalian apoptosome has been studied extensively, little is known about the apoptosome in insect cells.  Using a variety of biochemical and molecular biology techniques, we are investigating the proteins that make up the insect apoptosome and studying how it becomes activated.  In addition, we are studying the role of IAP proteins in apoptosome regulation.

Means, J.C., Muro, I., and R.J. Clem.  Lack of involvement of mitochondrial factors in caspase activation in a Drosophila cell-free system.  Cell Death Differ.  In press.

Muro, I., Means, J.C., and R.J. Clem.  2005.  Cleavage of the apoptosis inhibitor DIAP1 by the apical caspase DRONC in both normal and apoptotic Drosophila cells.  J. Biol. Chem. 280:18683-18688.

Muro, I., Monser, K., and R.J. Clem. 2004. Mechanism of Dronc activation in Drosophila cells.  J. Cell Sci. 117: 5035-5041.

Muro, I., Hay, B.A., and R.J. Clem. 2002.  The Drosophila DIAP1 protein is required to prevent accumulation of a continuously generated, processed form of the apical caspase DRONC.  J. Biol. Chem. 277:49644-49650.

Yoo, S.J., Huh, J.R., Muro, I., Yu, H., Wang, L., Wang, S.L., Feldman, R.M.R., Clem, R.J., Muller, H.-A.J., and B.A. Hay.  2002.  Hid, Rpr and Grim negatively regulate DIAP1 levels through distinct mechanisms. Nature Cell Biol. 4:416-424.