Lifespan extension in any organism literally means a delay in the aging process. Many of the pathways found to be involved in lifespan regulation in different organisms are dependent on the autophagy pathway or autophagic genes. In Caenorhabditis elegans, the target of rapamycin (TOR) pathway, which is responsible for sensing nutrients (inhibited by dietary restriction) and the insulin/IGF-1 pathway, which responds to different environmental cues, are well known pathways involved in lifespan extension and are reportedly dependent on the autophagy. In addition, it has recently been reported that lifespan extension in mutants with lowered mitochondrial respiration and
cep-1 mutants (orthologue of
p53) is also dependent on autophagic genes. The results of a study that we conducted also suggested that calcineurin regulates lifespan through the autophagy genes. Calcineurin (CaN) is a serine/threonine phosphatase, activated by Ca2+/calmodulin (Ca2+/CaM). CaN is known to regulate various cellular responses in different organisms. In this study, we report that calcineurin defective strains exhibit enhanced autophagy as assessed by the increased formation of GFP::LGG-1 associated autophagic structures in the seam cells. In addition to enhanced autophagy in calcineurin loss-of-function/null mutants, extended lifespan was also observed in
cnb-1(
jh103) calcineurin B null mutant and
tax-6(
ok2065) loss-of-function mutant of calcineurin A when compared to wild-type and
tax-6(
jh107) gain-of-function mutants. The RNAi knock-down of two essential autophagy genes,
bec-1 and
atg-7, suppress both the number of autophagic puncta and the lifespan extension observed in the calcineurin-defective mutants. The suppression of lifespan extension to the levels similar to wild-type animals fed with control vector only was observed in both
cnb-1(
jh103) and
tax-6(
ok2065) mutants treated with
bec-1 RNAi. Thus, for the first time we suggest that pathway operating for lifespan extension in calcineurin mutants converge at the autophagic pathway. This activated autophagic pathway in calcineurin mutants may be due to the disruption in calcium signaling pathway, which remains to be elucidated.