Animals use neutral lipids, particularly triacylglycerols (TAGs), to store energy. TAGs are universally organized into dynamic cytoplasmic structures called lipid droplets (LDs). In mammals TAG breakdown is catalysed by lipases, such as hormonesensitive lipase (HSL). LD membrane-resident proteins called perilipins (PLINs) regulate some of these lipases. The model organism Caenorhabditis elegans has a single known PLIN homologue and orthologues of most lipases including HSL. HOSL-1 (the HSL orthologue in C. elegans) is responsible for production of cryoprotective glycerol in cold conditions, in addition to its role in fasting-induced lipolysis. We employed this model of cold exposure to study the role of PLIN-1 in the regulation of HOSL-1. Our results suggest that both HOSL-1 and PLIN-1 are required for cold tolerance and for lipid breakdown in cold. However, the loss of PLIN-1 partially rescued the phenotype of hosl-1 null mutants exposed to cold, suggesting the presence of an alternative pathway generating glycerol via lipolysis. In early embryos, PLIN-1 knock-out results in accumulation of lipids and formation of cytoplasmic clusters of autophagic marker LGG-1, supporting the role of autophagy as an alternative lipolytic pathway in C. elegans, as is the case in mammals.