The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
HP1: Heterochromatin binding proteins working the genome
Open accessAbstract
Heterochromatin Protein 1 (HP1) is a transcriptional repressor that directly binds to the methylated lysine 9 residue of histone H3 (H3K9me), which is a hallmark histone modification for transcriptionally silenced heterochromatin. Studies of homologs in different organisms have provided significant insight into the function of HP1 and the role of H3K9me. Initially discovered to be a major constituent of heterochromatin important for gene silencing, HP1 is now known to be a dynamic protein that also functions in transcriptional elongation, centromeric sister chromatid cohesion, telomere maintenance and DNA repair. Furthermore, recent studies have begun to uncover functional differences between HP1 variants and their H3K9me-independent mode of action. As our understanding of HP1 expands, however, conflicting data has also been reported that requires further reconciliation. Here we focus on some of the recent findings and controversies concerning HP1 functions in mammalian cells in comparison to studies in other organisms.
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Citations
Cites
Chromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883
Role of Histone H3 Lysine 27 Methylation in Polycomb-Group Silencing
Cao, R., Wang, L., Wang, H., Xia, L., Erdjument-Bromage, H., Tempst, P., Jones, R. S., & Zhang, Y. (2002) · Science · doi:10.1126/science.1076997 · Cited by 3,775
Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
Lachner, M., O'Carroll, D., Rea, S., Mechtler, K., & Jenuwein, T. (2001) · Nature · doi:10.1038/35065132 · Cited by 2,868
Schultz, D. C., Ayyanathan, K., Negorev, D., Maul, G. G., & Rauscher, F. J. (2002) · Genes & Development · doi:10.1101/gad.973302 · Cited by 1,313
ATM Signaling Facilitates Repair of DNA Double-Strand Breaks Associated with Heterochromatin
Goodarzi, A. A., Noon, A. T., Deckbar, D., Ziv, Y., Shiloh, Y., Löbrich, M., & Jeggo, P. A. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.05.017 · Cited by 836
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Murr, R., Loizou, J. I., Yang, Y.-G., Cuenin, C., Li, H., Wang, Z.-Q., & Herceg, Z. (2006) · Nature Cell Biology · doi:10.1038/ncb1343 · Cited by 613
Heterochromatin protein 1 is recruited to various types of DNA damage
Luijsterburg, M. S., Dinant, C., Lans, H., Stap, J., Wiernasz, E., Lagerwerf, S., Warmerdam, D. O., Lindh, M., Brink, M. C., Dobrucki, J. W., et al. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200810035 · Cited by 264
Recruitment of Mec1 and Ddc1 Checkpoint Proteins to Double-Strand Breaks Through Distinct Mechanisms
Kondo, T., Wakayama, T., Naiki, T., Matsumoto, K., & Sugimoto, K. (2001) · Science · doi:10.1126/science.1063827 · Cited by 258
Mobilization and recruitment of HP1β: A bimodal response to DNA breakage
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Cited by
Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases
Cargnello, M., & Roux, P. P. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00031-10 · Cited by 3,274
Genome Architecture: Domain Organization of Interphase Chromosomes
Bickmore, W. A., & van Steensel, B. (2013) · Cell · doi:10.1016/j.cell.2013.02.001 · Cited by 725
Crosstalk between chromatin state and DNA damage response in cellular senescence and cancer.
Sulli, G., Di Micco, R., & di Fagagna, F. D. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3344 · Cited by 238
RNA polymerase II speed: a key player in controlling and adapting transcriptome composition
Muniz, L., Nicolas, E., & Trouche, D. (2021) · The EMBO Journal · doi:10.15252/embj.2020105740 · Cited by 198
“HP1 proteins bind to di-and trimethylated H3K9, as well as to other proteins involved in various epigenetic functions, such as histone methyltransferases (HMTs) (Zeng et al , 2010).”
Zinc finger protein SALL4 functions through an AT-rich motif to regulate gene expression
Kong, N. R., Bassal, M. A., Tan, H. K., Kurland, J. V., Yong, K. J., Young, J. J., Yang, Y., Li, F., Lee, J. D., Liu, Y., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2020.108574 · Cited by 56
Metadata
- Authors
- Zeng, W., Ball Jr, A. R., & Yokomori, K.
- Venue
- Epigenetics
- Publisher
- Informa UK Limited
- Published
- 2010-05-16
- Volume
- 5
- Issue
- 4
- Pages
- 287-292
- ISSN
- 1559-2294 (ISSN-L)
- 1559-2308
- OpenAlex
- W1993758267
- Cited by
- 162
- References
- 10
- FWCI
- 4.61
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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