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Histone H3.3 and its proteolytically processed form drive a cellular senescence programme

Duarte, Luis F., Young, Andrew R. J., Wang, Zichen, Wu, Hsan-Au, Panda, Taniya, Kou, Yan, Kapoor, Avnish, Hasson, Dan, Mills, Nicholas R., Ma’ayan, Avi, Narita, Masashi, Bernstein, Emily·2014·Nature Communications
DOI 10.1038/ncomms6210PMC PMC4235654
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  1. Hayflick, L. & Moorhead, P. S. The serial cultivation of human diploid cell strains. Exp. Cell Res. 25, 585–621 (1961). · DOI · Paper page
  2. Hemann, M. T. & Narita, M. Oncogenes and senescence: breaking down in the fast lane. Genes Dev. 21, 1–5 (2007). · DOI
  3. Voorhoeve, P. M. & Agami, R. The tumor-suppressive functions of the human INK4A locus. Cancer Cell 4, 311–319 (2003). · DOI · Paper page
  4. Chicas, A. et al. Dissecting the unique role of the retinoblastoma tumor suppressor during cellular senescence. Cancer Cell 17, 376–387 (2010). · DOI · Paper page
  5. Rai, T. S. & Adams, P. D. Lessons from senescence: chromatin maintenance in non-proliferating cells. Biochim. Biophys. Acta 1819, 322–331 (2011). · DOI
  6. Zhang, R. et al. Formation of MacroH2A-containing senescence-associated heterochromatin foci and senescence driven by ASF1a and HIRA. Dev. Cell 8, 19–30 (2005). · DOI · Paper page
  7. Chandra, T. et al. Independence of repressive histone marks and chromatin compaction during senescent heterochromatic layer formation. Mol. Cell 47, 203–214 (2012). · DOI · Paper page
  8. Chicas, A. et al. H3K4 demethylation by Jarid1a and Jarid1b contributes to retinoblastoma-mediated gene silencing during cellular senescence. Proc. Natl Acad. Sci. USA 109, 8971–8976 (2012). · DOI
  9. Bannister, A. J. & Kouzarides, T. Histone methylation: recognizing the methyl mark. Methods Enzymol. 376, 269–288 (2004). · DOI
  10. Allis, C. D., Bowen, J. K., Abraham, G. N., Glover, C. V. & Gorovsky, M. A. Proteolytic processing of histone H3 in chromatin: a physiologically regulated event in Tetrahymena micronuclei. Cell 20, 55–64 (1980). · DOI
  11. Duncan, E. M. et al. Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation. Cell 135, 284–294 (2008). · DOI
  12. Hiwasa, T. & Sakiyama, S. Nuclear localization of procathepsin L/MEP in ras-transformed mouse fibroblasts. Cancer Lett. 99, 87–91 (1996). · DOI
  13. Goulet, B. et al. A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor. Mol. Cell 14, 207–219 (2004). · DOI
  14. Ishidoh, K. et al. Multiple processing of procathepsin L to cathepsin L in vivo. Biochem. Biophys. Res. Commun. 252, 202–207 (1998). · DOI
  15. Galvani, A. et al. In vivo study of the nucleosome assembly functions of ASF1 histone chaperones in human cells. Mol. Cell. Biol. 28, 3672–3685 (2008). · DOI
  16. Adams-Cioaba, M. A., Krupa, J. C., Xu, C., Mort, J. S. & Min, J. Structural basis for the recognition and cleavage of histone H3 by cathepsin L. Nat. Commun. 2, 197 (2011). · DOI
  17. Corpet, A., Olbrich, T., Gwerder, M., Fink, D. & Stucki, M. Dynamics of histone H3.3 deposition in proliferating and senescent cells reveals a DAXX-dependent targeting to PML-NBs important for pericentromeric heterochromatin organization. Cell Cycle 13, 249–267 (2014). · DOI
  18. Ahmad, K. & Henikoff, S. The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly. Mol. Cell 9, 1191–1200 (2002). · DOI
  19. Goldberg, A. D. et al. Distinct factors control histone variant H3.3 localization at specific genomic regions. Cell 140, 678–691 (2010). · DOI
  20. Drané, P., Ouararhni, K., Depaux, A., Shuaib, M. & Hamiche, A. The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3. Genes Dev. 24, 1253–1265 (2010). · DOI
  21. Lewis, P. W., Elsaesser, S. J., Noh, K.-M., Stadler, S. C. & Allis, C. D. Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres. Proc. Natl Acad. Sci. USA 107, 14075–14080 (2010). · DOI
  22. Lachmann, A. et al. ChEA: transcription factor regulation inferred from integrating genome-wide ChIP-X experiments. Bioinformatics 26, 2438–2444 (2010). · DOI
  23. Coppe, J. P., Desprez, P. Y., Krtolica, A. & Campisi, J. The senescence-associated secretory phenotype: the dark side of tumor suppression. Annu. Rev. Pathol. 5, 99–118 (2010). · DOI · Paper page
  24. Bartkova, J. et al. Oncogene-induced senescence is part of the tumorigenesis barrier imposed by DNA damage checkpoints. Nature 444, 633–637 (2006). · DOI · Paper page
  25. Ivanov, A. et al. Lysosome-mediated processing of chromatin in senescence. J. Cell Biol. 202, 129–143 (2013). · DOI · Paper page
  26. Goulet, B. et al. Increased expression and activity of nuclear cathepsin L in cancer cells suggests a novel mechanism of cell transformation. Mol. Cancer Res. 5, 899–907 (2007). · DOI
  27. Lacoste, N. et al. Mislocalization of the centromeric histone variant CenH3/CENP-A in human cells depends on the chaperone DAXX. Mol. Cell 53, 631–644 (2014). · DOI
  28. Bernstein, E. et al. Mouse polycomb proteins bind differentially to methylated histone H3 and RNA and are enriched in facultative heterochromatin. Mol. Cell. Biol. 26, 2560–2569 (2006). · DOI
  29. Kapoor, A. et al. The histone variant macroH2A suppresses melanoma progression through regulation of CDK8. Nature 468, 1105–1109 (2010). · DOI
  30. Hasson, D. et al. The octamer is the major form of CENP-A nucleosomes at human centromeres. Nat. Struct. Mol. Biol. 20, 687–695 (2013). · DOI
  31. Hayashi-Takanaka, Y. et al. Tracking epigenetic histone modifications in single cells using Fab-based live endogenous modification labeling. Nucleic Acids Res. 39, 6475–6488 (2011). · DOI
  32. Trapnell, C., Pachter, L. & Salzberg, S. L. TopHat: discovering splice junctions with RNA-Seq. Bioinformatics 25, 1105–1111 (2009). · DOI
  33. Langmead, B. & Salzberg, S. L. Fast gapped-read alignment with Bowtie 2. Nat. Methods 9, 357–359 (2012). · DOI · Paper page
  34. Trapnell, C. et al. Transcript assembly and quantification by RNA-Seq reveals unannotated transcripts and isoform switching during cell differentiation. Nat. Biotechnol. 28, 511–515 (2010). · DOI · Paper page
  35. Huang da, W., Sherman, B. T. & Lempicki, R. A. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat. Protoc. 4, 44–57 (2009). · DOI · Paper page

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Metadata

Authors
Duarte, L. F., Young, A. R. J., Wang, Z., Wu, H.-A., Panda, T., Kou, Y., Kapoor, A., Hasson, D., Mills, N. R., Ma’ayan, A., Narita, M., & Bernstein, E.
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2014-11-14
Volume
5
Issue
1
ISSN
2041-1723
DOI
10.1038/ncomms6210
PMC
PMC4235654
Cited by
152
References
13
Language
en
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CoChat. (2026). Citation check: Histone H3.3 and its proteolytically processed form drive a cellular senescence programme. https://app.cochat.ai/papers/10.1038/ncomms6210
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Duarte, L. F., Young, A. R. J., Wang, Z., Wu, H.-A., Panda, T., Kou, Y., Kapoor, A., Hasson, D., Mills, N. R., Ma’ayan, A., Narita, M., & Bernstein, E. (2014). Histone H3.3 and its proteolytically processed form drive a cellular senescence programme. Nature Communications. https://doi.org/10.1038/ncomms6210