Role of CED-9/cl-2 family proteins in mitochondrial fission and fusion dynamics

Abstract

Programmed cell death in the nematode C. elegans is the equivalent process to human apoptosis. Studying this process in the model organism has led to a great amount of knowledge about the details of pathway steps and proteins that are involved. While the system in the worm appears trivial with only four regulating proteins, in mammalian cells at least twenty proteins are already involved in the initiation of apoptosis. In this study we set out to investigate worm cell death proteins in vivo and in vitro. Although many things are already known, it has never been shown before, where and when the only worm caspase CED-3 is expressed in vivo. In the first part of our study we initially wanted to analyze the localization and in vivo expression pattern of CED-3 in C. elegans worm embryos. Although we employed several commercially available and self-generated anti-CED-3 antibodies, we were not able to achieve CED-3 staining in worm cells. However, during these experiments we found reorganization of the mitochondrial network by the expression of CED-9 in HeLa cells.