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PreprintCC BY-NC-NDbioRxiv

TERT interacts with TFAM to activate mitochondrial fragmentation and auto/mitophagy

  • E. Rossi
  • J. Marinaccio
  • I. Festo
  • I. Udroiu
  • E. Micheli
  • G. Bertolin1
  • A. Sgura
  1. 1CNRS, Univ Rennes, IGDR
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Abstract

Previous studies have demonstrated that Telomerase Reverse Transcriptase (TERT) is localized inside mitochondria, where it associates with mitochondrial DNA (mtDNA), thereby influencing replication and transcription. Using a combination of quantitative fluorescence microscopy and biochemistry, we demonstrate that TERT binds indirectly to mtDNA through the interaction with mitochondrial transcription factor A (TFAM) to induce mitochondrial fragmentation. These findings reveal a novel mitochondrial interaction involving TERT and highlight a role for TERT and TFAM in the regulation of auto/mitophagy. This interaction is an important factor for mitochondrial function and contributes to the remodelling of mitochondrial respiratory capacity.

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Cite

BibTeXRIS
BibTeX
@misc{rossi2026tert,
  title = {{TERT interacts with TFAM to activate mitochondrial fragmentation and auto/mitophagy}},
  author = {E. Rossi and J. Marinaccio and I. Festo and I. Udroiu and E. Micheli and G. Bertolin and A. Sgura},
  howpublished = {bioRxiv},
  year = {2026},
  month = sep,
  doi = {10.64898/2026.09.18.752609},
  url = {https://www.biorxiv.org/content/10.64898/2026.09.18.752609v1},
  note = {CC BY-NC-ND},
}
RIS
TY  - UNPB
TI  - TERT interacts with TFAM to activate mitochondrial fragmentation and auto/mitophagy
AU  - E. Rossi
AU  - J. Marinaccio
AU  - I. Festo
AU  - I. Udroiu
AU  - E. Micheli
AU  - G. Bertolin
AU  - A. Sgura
PY  - 2026
DA  - 2026/09/18
PB  - bioRxiv
DO  - 10.64898/2026.09.18.752609
UR  - https://www.biorxiv.org/content/10.64898/2026.09.18.752609v1
AB  - Previous studies have demonstrated that Telomerase Reverse Transcriptase (TERT) is localized inside mitochondria, where it associates with mitochondrial DNA (mtDNA), thereby influencing replication and transcription. Using a combination of quantitative fluorescence microscopy and biochemistry, we demonstrate that TERT binds indirectly to mtDNA through the interaction with mitochondrial transcription factor A (TFAM) to induce mitochondrial fragmentation. These findings reveal a novel mitochondrial interaction involving TERT and highlight a role for TERT and TFAM in the regulation of auto/mitophagy. This interaction is an important factor for mitochondrial function and contributes to the remodelling of mitochondrial respiratory capacity.
ER  -