Dissection of DIAP1 functional domains via a mutant replacement strategy.

Inhibitor of apoptosis proteins (IAPs) act as endogenous inhibitors of active caspases. Drosophila IAP1 (DIAP1) activity is required to keep cells from undergoing apoptosis. The central cell death regulators Reaper and Hid induce apoptosis very rapidly by inhibiting DIAP1 function.

Molecular mechanisms of cell death and phagocytosis in Drosophila.

The genetic tools available in Drosophila have facilitated our understanding of how apoptosis is regulated and executed in the context of the developing organism. All embryonic apoptosis is initiated by the activity of three genes, rpr, grim and hid. Each of these genes is independently regulated, allowing developmental apoptosis to be finely controlled.

Regulation and execution of apoptosis during Drosophila development.

The development of the Drosophila embryo into an adult fly is a process that integrates cell proliferation and differentiation with programmed cell death, or apoptosis. Apoptosis is an evolutionarily conserved process that is controlled in the developing fly by the products of the genes reaper, grim, and hid. We discuss the role of programmed cell death in the establishment and maintenance of correct patterning in the embryo, and examine the coordination of apoptosis with the hormonally controlled degeneration of larval tissues during metamorphosis.

Functional analysis of Tpr: identification of nuclear pore complex association and nuclear localization domains and a role in mRNA export.

Tpr is a 270-kD coiled-coil protein localized to intranuclear filaments of the nuclear pore complex (NPC). The mechanism by which Tpr contributes to the structure and function of the nuclear pore is currently unknown. To gain insight into Tpr function, we expressed the full-length protein and several subdomains in mammalian cell lines and examined their effects on nuclear pore function.