GRP75-dependent SIMPA pathway clears damaged proteins via mitochondria-ER contacts
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Research published in Nature describes a new inter-organellar quality-control mechanism. Under proteotoxic stress, protein aggregates dependent on GRP75 signal through mitochondria-ER contact sites, activating a selective pathway with SIMPA as a key node. This pathway clears damaged proteins and preserves mitochondrial integrity, linking protein aggregation to organellar communication and suggesting how cells coordinate degradation of toxic proteins with mitochondrial protection. The findings identify SIMPA as a candidate target for conditions involving proteotoxic stress and mitochondrial dysfunction. Follow-up work clarifying the pathway's components and its relevance to disease models has not yet been reported.
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- NaturePickGRP75-dependent SIMPA mediates inter-organellar quality control
Under proteotoxic stress, GRP75-dependent protein aggregates signal through mitochondria-ER contact sites, activating a selective quality-control pathway with SIMPA as a key node that clears damaged proteins and maintains mitochondrial integrity. DOI: 10.1038/s41586-026-10733-y.
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