Cell death is an important cellular process in development and disease. While caspase-dependent apoptosis has been extensively studied, cell death still occurs in animals lacking these proteases, suggesting that cells must be able to engage non-apoptotic cell death pathways. One such example is the non-apoptotic cell death of the C. elegans linker cell, which leads the elongation of the developing male gonad during larval development. At the L4-to-adult transition, when the linker cell reaches the cloaca, it dies. Linker cell death is not apoptotic, as assessed by mechanism and morphology, and relies in part on a poly-glutamine protein, PQN-41C. We are interested in identifying binding partners of PQN-41C to determine its functions during linker cell death and outside the linker cell. We used a yeast two-hybrid screen to isolate 33 putative PQN-41C interactors. Gene ontology and protein domains identify five subclasses of interactors affecting proteolysis (
asp-3, F32A5.3, K10C2.1, F57F5.1,
nep-17), or possessing coiled-coil domains (
pqn-41,
pqn-59, R11A8.7,
pqn-85,
npp-4), ubiquitin-related domains (
tag-214,
pqn-59, F52G3.1,
sao-1), and RNA-related (
etr-1,
asd-1,
asd-2,
pes-4), or DNA-associated domains (
chd-7,
zfp-1,
tag-153,
eef-2, T19D12.2,
pqn-85). We tested the functions of the interacting proteins in linker cell death by examining whether RNAi against each candidate promotes linker cell survival. Of the genes we tested thus far, seven appear to have a function in linker cell death, with linker cell survival rates ranging from 12% to 33% upon RNAi knockdown. Two candidates may cause enhanced linker cell death or cell clearance upon knockdown. Our results therefore suggest that PQN-41C may act in complex with other proteins to promote linker cell death.