Mammalian HP1 Isoforms Have Specific Roles in Heterochromatin Structure and Organization

Laia Bosch-Presegué, Helena Raurell-Vila, Joshua K Thackray, Jessica González, Carmen Casal, Noriko Kane-Goldsmith, Miguel Vizoso, Jeremy P Brown, Antonio Gómez, Juan Ausió, Timo Zimmermann, Manel Esteller, Gunnar Schotta, Prim B Singh, Lourdes Serrano, Alejandro Vaquero

Research output: Contribution to journalArticle

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Abstract

HP1 is a structural component of heterochromatin. Mammalian HP1 isoforms HP1α, HP1β, and HP1γ play different roles in genome stability, but their precise role in heterochromatin structure is unclear. Analysis of Hp1α-/-, Hp1β-/-, and Hp1γ-/- MEFs show that HP1 proteins have both redundant and unique functions within pericentric heterochromatin (PCH) and also act globally throughout the genome. HP1α confines H4K20me3 and H3K27me3 to regions within PCH, while its absence results in a global hyper-compaction of chromatin associated with a specific pattern of mitotic defects. In contrast, HP1β is functionally associated with Suv4-20h2 and H4K20me3, and its loss induces global chromatin decompaction and an abnormal enrichment of CTCF in PCH and other genomic regions. Our work provides insight into the roles of HP1 proteins in heterochromatin structure and genome stability.

Original languageEnglish
Pages (from-to)2048-2057
Number of pages10
JournalCell Reports
Volume21
Issue number8
DOIs
Publication statusPublished - Nov 21 2017
Externally publishedYes

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Heterochromatin
Protein Isoforms
Genes
Chromatin
Genomic Instability
Proteins
Compaction
Defects
Genome

Keywords

  • Journal Article

Cite this

Bosch-Presegué, L., Raurell-Vila, H., Thackray, J. K., González, J., Casal, C., Kane-Goldsmith, N., ... Vaquero, A. (2017). Mammalian HP1 Isoforms Have Specific Roles in Heterochromatin Structure and Organization. Cell Reports, 21(8), 2048-2057. https://doi.org/10.1016/j.celrep.2017.10.092

Mammalian HP1 Isoforms Have Specific Roles in Heterochromatin Structure and Organization. / Bosch-Presegué, Laia; Raurell-Vila, Helena; Thackray, Joshua K; González, Jessica; Casal, Carmen; Kane-Goldsmith, Noriko; Vizoso, Miguel; Brown, Jeremy P; Gómez, Antonio; Ausió, Juan; Zimmermann, Timo; Esteller, Manel; Schotta, Gunnar; Singh, Prim B; Serrano, Lourdes; Vaquero, Alejandro.

In: Cell Reports, Vol. 21, No. 8, 21.11.2017, p. 2048-2057.

Research output: Contribution to journalArticle

Bosch-Presegué, L, Raurell-Vila, H, Thackray, JK, González, J, Casal, C, Kane-Goldsmith, N, Vizoso, M, Brown, JP, Gómez, A, Ausió, J, Zimmermann, T, Esteller, M, Schotta, G, Singh, PB, Serrano, L & Vaquero, A 2017, 'Mammalian HP1 Isoforms Have Specific Roles in Heterochromatin Structure and Organization', Cell Reports, vol. 21, no. 8, pp. 2048-2057. https://doi.org/10.1016/j.celrep.2017.10.092
Bosch-Presegué L, Raurell-Vila H, Thackray JK, González J, Casal C, Kane-Goldsmith N et al. Mammalian HP1 Isoforms Have Specific Roles in Heterochromatin Structure and Organization. Cell Reports. 2017 Nov 21;21(8):2048-2057. https://doi.org/10.1016/j.celrep.2017.10.092
Bosch-Presegué, Laia ; Raurell-Vila, Helena ; Thackray, Joshua K ; González, Jessica ; Casal, Carmen ; Kane-Goldsmith, Noriko ; Vizoso, Miguel ; Brown, Jeremy P ; Gómez, Antonio ; Ausió, Juan ; Zimmermann, Timo ; Esteller, Manel ; Schotta, Gunnar ; Singh, Prim B ; Serrano, Lourdes ; Vaquero, Alejandro. / Mammalian HP1 Isoforms Have Specific Roles in Heterochromatin Structure and Organization. In: Cell Reports. 2017 ; Vol. 21, No. 8. pp. 2048-2057.
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AU - Raurell-Vila, Helena

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AU - González, Jessica

AU - Casal, Carmen

AU - Kane-Goldsmith, Noriko

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AU - Brown, Jeremy P

AU - Gómez, Antonio

AU - Ausió, Juan

AU - Zimmermann, Timo

AU - Esteller, Manel

AU - Schotta, Gunnar

AU - Singh, Prim B

AU - Serrano, Lourdes

AU - Vaquero, Alejandro

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N2 - HP1 is a structural component of heterochromatin. Mammalian HP1 isoforms HP1α, HP1β, and HP1γ play different roles in genome stability, but their precise role in heterochromatin structure is unclear. Analysis of Hp1α-/-, Hp1β-/-, and Hp1γ-/- MEFs show that HP1 proteins have both redundant and unique functions within pericentric heterochromatin (PCH) and also act globally throughout the genome. HP1α confines H4K20me3 and H3K27me3 to regions within PCH, while its absence results in a global hyper-compaction of chromatin associated with a specific pattern of mitotic defects. In contrast, HP1β is functionally associated with Suv4-20h2 and H4K20me3, and its loss induces global chromatin decompaction and an abnormal enrichment of CTCF in PCH and other genomic regions. Our work provides insight into the roles of HP1 proteins in heterochromatin structure and genome stability.

AB - HP1 is a structural component of heterochromatin. Mammalian HP1 isoforms HP1α, HP1β, and HP1γ play different roles in genome stability, but their precise role in heterochromatin structure is unclear. Analysis of Hp1α-/-, Hp1β-/-, and Hp1γ-/- MEFs show that HP1 proteins have both redundant and unique functions within pericentric heterochromatin (PCH) and also act globally throughout the genome. HP1α confines H4K20me3 and H3K27me3 to regions within PCH, while its absence results in a global hyper-compaction of chromatin associated with a specific pattern of mitotic defects. In contrast, HP1β is functionally associated with Suv4-20h2 and H4K20me3, and its loss induces global chromatin decompaction and an abnormal enrichment of CTCF in PCH and other genomic regions. Our work provides insight into the roles of HP1 proteins in heterochromatin structure and genome stability.

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