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Significance Nuclear envelopathies are a complex group of human diseases caused by mutations in nuclear envelope proteins, including progeria, myopathy, and dystonia. Here, we used the Caenorhabditis elegans germline as a model system to investigate the function of the OOC-5/torsinA AAA+ ATPase, which localizes to the nuclear envelope and is mutated in early-onset DYT1 dystonia in humans. We show that OOC-5/torsinA promotes the function of the LINC complex, which spans the nuclear envelope and transmits forces to the nuclear lamina. Remarkably, decreasing the function of OOC-5/torsinA or the LINC complex prevents nuclear collapse in the absence of a functional nuclear lamina. Therapeutics targeting torsinA or the LINC complex might prevent nuclear damage from endogenous forces in certain nuclear envelopathies., The function of the nucleus depends on the integrity of the nuclear lamina, an intermediate filament network associated with the linker of nucleoskeleton and cytoskeleton (LINC) complex. The LINC complex spans the nuclear envelope and mediates nuclear mechanotransduction, the process by which mechanical signals and forces are transmitted across the nuclear envelope. In turn, the AAA+ ATPase torsinA is thought to regulate force transmission from the cytoskeleton to the nucleus. In humans, mutations affecting nuclear envelope-associated proteins cause laminopathies, including progeria, myopathy, and dystonia, though the extent to which endogenous mechanical stresses contribute to these pathologies is unclear. Here, we use the Caenorhabditis elegans germline as a model to investigate mechanisms that maintain nuclear integrity as germ cell nuclei progress through meiotic development and migrate for gametogenesis—processes that require LINC complex function. We report that decreasing the function of the C. elegans torsinA homolog, OOC-5, rescues the sterility and premature aging caused by a null mutation in the single worm lamin homolog. We show that decreasing OOC-5/torsinA activity prevents nuclear collapse in lamin mutants by disrupting the function of the LINC complex. At a mechanistic level, OOC-5/torsinA promotes the assembly or maintenance of the lamin-associated LINC complex and this activity is also important for interphase nuclear pore complex insertion into growing germline nuclei. These results demonstrate that LINC complex-transmitted forces damage nuclei with a compromised nuclear lamina. Thus, the torsinA–LINC complex nexus might comprise a therapeutic target for certain laminopathies by preventing damage from endogenous cellular forces.