Related Experiment Video
Updated: Aug 6, 2026

05:52
Reconstitution of Msp1 Extraction Activity with Fully Purified Components
Published on: August 10, 2021
Positioning TERT at the apex of aging
1Department of Cancer Biology, The University of Texas MD Anderson Cancer Center, Houston, TX, USA. RDePinho@mdanderson.org.
Nature Aging
|July 20, 2026
Summary
Telomerase reverse transcriptase (TERT) influences aging hallmarks and healthspan. Modulating TERT shows promise for age-related conditions, but careful safety evaluations are crucial due to cancer risk links.
Area of Science:
- Gerontology
- Molecular Biology
- Biochemistry
Background:
- Aging is a complex biological process with identifiable hallmarks.
- Telomerase reverse transcriptase (TERT) is an upstream regulator of aging.
- TERT impacts telomere length, mitochondrial function, epigenetics, inflammation, and stem cell activity.
Purpose of the Study:
- To review the canonical and noncanonical roles of TERT in aging.
- To outline a therapeutic framework for TERT-directed geroprotective strategies.
- To highlight the potential of TERT in affecting healthspan.
Main Methods:
- Review of current scientific literature on TERT and aging.
- Analysis of preclinical models (mice) and human cell studies.
- Examination of human genetics linking TERT locus variation to cancer risk.
Main Results:
- TERT modulation, including restoration of physiological levels, improves age-related phenotypes in preclinical models.
- These improvements occur without a detectable increase in cancer in studied models.
- Human genetics indicates TERT locus variations are linked to increased cancer risk.
Conclusions:
- TERT plays a significant role in aging biology and healthspan.
- Therapeutic strategies targeting TERT require careful mechanistic and long-term safety evaluations.
- A cautious approach is needed for TERT-directed geroprotective interventions.
Related Concept Videos
Mitochondria
Mitochondria are eukaryotic cellular organelles that are known to produce energy through a process called oxidative phosphorylation. Besides their primary function, mitochondria are involved in various cellular processes, including cell growth, differentiation, signaling, metabolism, and senescence. Age-related changes cause a decline in mitochondrial quality and integrity due to increased mitochondrial mutations and oxidative damage. Thus, aging can severely impact mitochondrial functions,...
ATP Synthase: Structure
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
ATP Synthase: Mechanism
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
Energy to Drive Translocation
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
Generally, polypeptides are unfolded by two distinct...
Translocation of Proteins into the Mitochondria
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Allosteric Proteins-ATCase
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
