Evidence map›Paper›PMID 36310382›Full record

ArticleAutophagy2023

The telomeric protein TERF2/TRF2 impairs HMGB1-driven autophagy.

Sara Iachettini, Fabio Ciccarone, Carmen Maresca, Carmen D' Angelo, Eleonora Petti, Serena Di Vito, Maria Rosa Ciriolo, Pasquale Zizza, Annamaria Biroccio

Open access · greenAbstract read
In one paragraph

Article in Autophagy, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.1field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. HMGB1: A Central Node in Cancer Therapy Resistance.International journal of molecular sciences · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. A blood- and brain-based EWAS of smoking.Nature communications · 2025
    Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. The Altered Functions of Shelterin Components in ALT Cells.International journal of molecular sciences · 2023
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Sara IachettiniTranslational Oncology Research Unit, IRCCS - Regina Elena National Cancer Institute, Rome, Italy.
Fabio CiccaroneDepartment of Biology, University of Rome "Tor Vergata", Rome, Italy.
Carmen MarescaTranslational Oncology Research Unit, IRCCS - Regina Elena National Cancer Institute, Rome, Italy.
Carmen D' AngeloTranslational Oncology Research Unit, IRCCS - Regina Elena National Cancer Institute, Rome, Italy.
Eleonora PettiTranslational Oncology Research Unit, IRCCS - Regina Elena National Cancer Institute, Rome, Italy.
Serena Di VitoTranslational Oncology Research Unit, IRCCS - Regina Elena National Cancer Institute, Rome, Italy.
Maria Rosa CirioloDepartment of Biology, University of Rome "Tor Vergata", Rome, Italy.
Pasquale ZizzaTranslational Oncology Research Unit, IRCCS - Regina Elena National Cancer Institute, Rome, Italy.
Annamaria BiroccioTranslational Oncology Research Unit, IRCCS - Regina Elena National Cancer Institute, Rome, Italy.
Istituti di Ricovero e Cura a Carattere Scientifico · ITIstituto di Ricovero e Cura a Carattere Scientifico San RaffaeleVita-Salute San Raffaele University · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TERF2/TRF2 is a pleiotropic telomeric protein that plays a crucial role in tumor formation and progression through several telomere-dependent and -independent mechanisms. Here, we uncovered a novel function for this protein in regulating the macroautophagic/autophagic process upon different stimuli. By using both biochemical and cell biology approaches, we found that TERF2 binds to the non-histone chromatin-associated protein HMGB1, and this interaction is functional to the nuclear/cytoplasmic protein localization. Specifically, silencing of TERF2 alters the redox status of the cells, further exacerbated upon EBSS nutrient starvation, promoting the cytosolic translocation and the autophagic activity of HMGB1. Conversely, overexpression of wild-type TERF2, but not the mutant unable to bind HMGB1, negatively affects the cytosolic translocation of HMGB1, counteracting the stimulatory effect of EBSS starvation. Moreover, genetic depletion of HMGB1 or treatment with inflachromene, a specific inhibitor of its cytosolic translocation, completely abolished the pro-autophagic activity of TERF2 silencing. In conclusion, our data highlighted a novel mechanism through which TERF2 modulates the autophagic process, thus demonstrating the key role of the telomeric protein in regulating a process that is fundamental, under both physiological and pathological conditions, in defining the fate of the cells.

Indexed as

HMGB1 ProteinAutophagyDNA DamageNuclear ProteinsTelomereHMGB1 ProteinNuclear ProteinsAutophagycancercell biologyHMGB1oxidative stressROSTERF2/TRF2

Identifiers

PMID36310382
PMCPMC10240986
OpenAlexW4307746769

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.