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The mitochondrial  U nfolded  P rotein  R esponse (UPR mt ) pathway confers protection from misfolded and aggregated proteins by activating factors that promote protein folding and degradation. Our recent work on Lon protease, a member of the mitochondrial  A TPase  A ssociated with diverse cellular  A ctivities (AAA + ) family of mitochondrial resident proteases, suggests that mitochondrial translational inhibition may also be a feature of the UPR mt  pathway.

Inactivation of Lon protease reveals a link between mitochondrial unfolded protein stress and mitochondrial translation inhibition