PML induces compaction, TRF2 depletion and DNA damage signaling at telomeres and promotes their alternative lengthening
Abstract
The alternative lengthening of telomeres (ALT) mechanism allows cancer cells to escape senescence and apoptosis in the absence of active telomerase. A characteristic feature of this pathway is the assembly of ALT-associated promyelocytic leukemia (PML) nuclear bodies (APBs) at telomeres. Here, we dissected the role of APBs in a human ALT cell line by performing an RNA interference screen using an automated 3D fluorescence microscopy platform and advanced 3D image analysis. We identified 29 proteins that affected APB formation, which included proteins involved in telomere and chromatin organization, protein sumoylation and DNA repair. By integrating and extending these findings, we found that APB formation induced clustering of telomere repeats, telomere compaction and concomitant depletion of the shelterin protein TRF2 (also known as TERF2). These APB-dependent changes correlated with the induction of a DNA damage response at telomeres in APBs as evident by a strong enrichment of the phosphorylated form of the ataxia telangiectasia mutated (ATM) kinase. Accordingly, we propose that APBs promote telomere maintenance by inducing a DNA damage response in ALT-positive tumor cells through changing the telomeric chromatin state to trigger ATM phosphorylation.
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ALT-associated PML bodies have an essential role in telomere-lengthening in ALT+ cells by bringing chromosome ends together with recombination proteins.
“These ALT-associated PML bodies have an essential role in telomere-lengthening in ALT+ cells, by bringing chromosome ends together with the recombination proteins that mediate their lengthening (Draskovic et al., 2009; Osterwald et al., 2015).”
From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Osterwald et al., 2015
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“These ALT-associated PML bodies have an essential role in telomere-lengthening in ALT+ cells, by bringing chromosome ends together with the recombination proteins that mediate their lengthening (Draskovic et al., 2009; Osterwald et al., 2015).”
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- Authors
- Osterwald, S., Deeg, K. I., Chung, I., Parisotto, D., Wörz, S., Rohr, K., Erfle, H., & Rippe, K.
- Affiliations
- German Cancer Research Center (DE)
- Heidelberg University (DE)
- Corresponding author
- Rippe, Karsten
- ORCID
- Rippe, Karsten
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2015-05-15
- Volume
- 128
- Issue
- 10
- Pages
- 1887-1900
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2099254632
- Semantic Scholar
- 766c087cec70c08d0fa78733ded10518f2c28199
- Cited by
- 92
- References
- 78
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 9 · 2023: 8 · 2022: 8 · 2021: 11 · 2020: 16 · 2019: 9 · 2018: 6 · 2017: 10 · 2016: 7 · 2015: 1
- FWCI
- 5.90
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Cell Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Telomeres, Telomerase, and Senescence
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- alternative lengthening of telomeres, PML nuclear bodies, shelterin, DNA damage response, telomere maintenance, SUMOylation, chromatin organization, senescence escape, RNAi screen
- MeSH terms
- Promyelocytic Leukemia Protein, DNA Damage, DNA Repair, Humans, Nuclear Proteins, Transcription Factors, Signal Transduction, Leukemia, Promyelocytic, Acute, Telomere, Tumor Suppressor Proteins, Telomeric Repeat Binding Protein 2, Cell Line, Tumor
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