Related Experiment Video
Updated: Sep 11, 2025

Lipid Supplementation for Longevity and Gene Transcriptional Analysis in Caenorhabditis elegans
Published on: December 9, 2022
Mitochondrial stress orchestrates chromatin remodeling and longevity via phosphoregulation of the NuRD component
Jun Zhou1, Di Zhu1, Yibing Wang1,2
1Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, 100101, China.
Abstract:
Mitochondrial dysfunction is a hallmark of aging that elicits adaptive nuclear responses, yet how chromatin remodeling is coordinated under stress remains unclear. Here, we uncover a phosphorylation-dependent mechanism by which mitochondrial stress regulates the activity of the NuRD (nucleosome remodeling and deacetylase) complex via LIN-40, the Caenorhabditis elegans homolog of mammalian MTA proteins. Mitochondrial stress triggers dephosphorylation of LIN-40, enhancing its interaction with the transcription factor DVE-1 to activate the mitochondrial unfolded protein response (UPRmt) and chromatin remodeling. Phosphorylation of LIN-40 is mediated by p38 MAPK/PMK-3 and reversed by PP1c/GSP-2. Furthermore, the LIN-40(T654D) variant abolishes mitochondrial stress-induced lifespan extension. These findings establish a direct link between mitochondrial stress signaling and chromatin remodeling via NuRD, revealing an evolutionarily conserved strategy to coordinate cellular resilience and organismal longevity.
Related Concept Videos
Nucleosome Remodeling
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
Mitochondria
Replication in Eukaryotes
Many Proteins Orchestrate Replication at the Origin
Eukaryotic replication follows many of the same...
Replicative Cell Senescence
The Nucleolus
Chromatin Modification in iPS Cells
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...

