Related Experiment Video
Updated: Jun 4, 2026

07:49
Transmitochondrial Cybrid Generation Using Cancer Cell Lines
Published on: March 17, 2023
Hit proteins, mitochondria and cancer
Juliette Martin1, Marie V St-Pierre, Jean-François Dufour
1Institute of Clinical Pharmacology and Visceral Research, University of Bern, Switzerland.
Biochimica Et Biophysica Acta
|February 15, 2011
Summary
The histidine triad (HIT) superfamily proteins, including HINT and FHIT, show tumor suppressor activity. Their precise roles in cancer bioenergetics and physiology are under investigation.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- The histidine triad (HIT) superfamily is a conserved protein group found in all domains of life.
- HIT proteins share a characteristic His-ϕ-His-ϕ-His-ϕ-ϕ motif and bind nucleotides.
- Five distinct families of HIT proteins exist in humans, each with unique functions.
Purpose of the Study:
- To review the tumor suppressor properties of HINT (Histidine Triad Nucleotide Binding) and FHIT (Fragile Histidine Triad) members.
- To explore the potential roles of HIT proteins in cancer bioenergetics.
- To discuss the known functions and disease associations of different HIT superfamily branches.
Main Methods:
- Literature review of epidemiological and experimental evidence.
- Analysis of protein structures and enzymatic activities.
- Discussion of genetic links to diseases and cancer.
Main Results:
- HINT and FHIT proteins exhibit tumor suppressor properties, though their exact physiological roles are not fully elucidated.
- Aprataxin, a HIT member, is involved in DNA repair and linked to ataxia with oculomotor apraxia type 1.
- DcpS and GalT enzymes represent other HIT branches with distinct functions, not directly linked to tumorigenesis.
Conclusions:
- The molecular mechanisms underlying the involvement of HINT and FHIT proteins in cancer bioenergetics are emerging.
- Further research is needed to fully understand the physiological roles and therapeutic potential of HIT superfamily members in cancer suppression.
Related Concept Videos
mTOR Signaling and Cancer Progression
The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
The mTOR pathway or the...
mTOR Signaling and Cancer Progression
The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
The mTOR pathway or the...
Electron Transport Chain: Complex I and II
The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
ROS generation is regulated and maintained at moderate levels necessary...
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,...
Protein Networks
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
PI3K/mTOR/AKT Signaling Pathway
The mammalian target of rapamycin (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1 (mTORC1) and mTOR complex 2 (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast, mTORC2 consists of a rapamycin-insensitive companion...

