DRP-1-dependent autophagy, heat stress and mitochondrial rebuilding


Yanfang Chen, Romane Leboutet, Céline Largeau, Siham Zentout, Christophe Lefebvre, Agnès Delahodde, Emmanuel Culetto, Renaud Legouis. Contact: renaud.legouis@i2bc.paris-saclay.fr

Link to the original article

Year of publication



J Cell Biol


A DRP-1 dependent autophagy facilitates mitochondrial rebuilding and adaptation to acute heat-stress Environmental heterogeneity, such as variations in ambient temperature, induces stressful conditions that challenges the ability of organisms to maintain cell homeostasis. The intensity and duration of heat stress can affect cell response very differently, ranging from a beneficial effect to cell death. Autophagy, a mechanism for degrading and recycling of cellular constituents, is one of the main responses induced by heat stress. Using the model animal Caenorhabditis elegans, Renaud Legouis’ laboratory has developed a new paradigm to study adaptation to acute non-lethal heat-stress (aHS). This stress results in transient fragmentation of mitochondria, formation of aggregates in the mitochondrial matrix, decreased cellular respiration, and delayed development. Moreover, an active autophagy flux associated to mitophagy events is triggered in many tissues. It enables the rebuilding of the mitochondrial network and modulates the adaptive capacity of the C. elegans during development, showing that the autophagic response is protective for the animal. Using genetic and cellular approaches, the authors showed that mitochondria are a major site for autophagosome biogenesis in the epidermis, under both standard and heat stress conditions. They identified DRP-1 (dynamin-related protein 1), involved in mitochondrial fission, as an important player for the autophagy process and the adaptation to aHS. They propose that DRP-1 is involved in coordinating mitochondrial fission and autophagosomes biogenesis in stress conditions.

Graphical abstract

Autophagy facilitates mitochondrial rebuilding after acute heat stress via a DRP-1–dependent process