bioRxiv Science⌕ Search

Biology subjects

Defour, J.-P.

Publications and source records attributed to Defour, J.-P..

2 recordsLinked to original sources

Human mitochondrial DNA variants influence telomere length: evidence from a transmitochondrial cybrid model

Telomere shortening is a hallmark of aging, yet telomere length (TL) varies considerably among individuals and is strongly influenced by inheritance. In mice, efficient mitochondrial function-characterized by low reactive oxygen species (ROS) production-is critical for telomere elongation during early embryogenesis. Since mitochondrial DNA (mtDNA) encodes several subunits of the electron transport chain, it may influence TL at birth by regulating mitochondrial function in utero. To explore the relationship between mtDNA and TL in human, we used a transmitochondrial cybrid approach, introducing mitochondria from donor platelets with varying telomere lengths into mtDNA-depleted cells. This revealed an inverse correlation between donor blood TL and mitochondrial ROS levels measured in the resulting cybrids, suggesting that specific mtDNA variants may contribute to the maintenance of long telomeres in humans by enhancing mitochondrial fitness. During in vitro cybrid formation, a transient phase of oxidative stress precedes cellular adaptation. In this specific window, mtDNA variants associated with reduced complex I (CI) activity induced rapid telomere shortening--an effect rescued by antioxidant and NAD precursor supplementation. While these variants occur naturally in certain individuals with long telomeres, our data suggest that, at least under in vitro conditions of acute oxidative stress, CI is critical to support PARP1 activity by maintaining the NAD/NADH balance, thereby preserving telomere integrity. Collectively, these findings solidify the link between mtDNA variants and human TL regulation, highlighting potential therapeutic opportunities for mitochondrial replacement strategies. Significance StatementTelomere length at birth influences aging trajectories and disease risk later in life, yet the mechanisms governing this trait remain incompletely understood. Using a transmitochondrial cybrid approach, we show that single-nucleotide variants in the mitochondrial genome of healthy donors directly affect mitochondrial metabolism and reactive oxygen species production. In addition, mitochondrial ROS levels measured in cybrids inversely correlate with blood cell telomere length in donors. During cybrid formation, mitochondrial DNA variants associated with reduced CI activity promote telomere shortening. Attrition was reversed by antioxidant and NAD precursor supplementation, pointing to an essential role for robust CI function in sustaining telomere length during acute oxidative stress, at least under in vitro conditions. Together, these findings establish a direct link between mitochondrial genetics, redox homeostasis, and telomere maintenance in human cells.

cell biology↗

Constitutive Activation and Oncogenicity Are Mediated by Loss of Helical Structure at the Cytosolic Boundary of the Thrombopoietin Receptor

Dimerization of the thrombopoietin receptor (TpoR) is necessary for receptor activation and downstream signaling through activated Janus kinase 2. We have shown previously that different orientations of the transmembrane (TM) helices within a receptor dimer can lead to different signaling outputs. Here we addressed the structural basis of activation for receptor mutations S505N and W515K that induce myeloproliferative neoplasms. We show using in vivo bone marrow reconstitution experiments that ligand-independent activation of TpoR by TM asparagine (Asn) substitutions is proportional to the proximity of the mutation to the intracellular membrane surface. Solid-state NMR experiments on TM peptides indicate a progressive loss of helical structure in the juxtamembrane (JM) R/KWQFP motif with either proximity of Asn substitutions to the cytosolic boundary or mutation of W515 in the motif. Mutational studies in the TpoR cytosolic JM region show that the helical loss by itself can induce activation, but is localized to a maximum of 6 amino acids downstream of W515, the rest of the region until Box 1 requiring helicity for receptor function. The constitutive activation of TpoR mutants S505N and W515K can be inhibited by rotation of TM helices within the TpoR dimer, which also restores helicity around W515. Together these data allow us to develop a general model for activation and to explain the critical role of the JM W515 residue in the regulation of receptor activity. (Total manuscript without References and Figure Legends 6507 words, main text (without methods and materials):)

molecular biology↗