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The SUMO protease SENP7 is a critical component to ensure HP1 enrichment at pericentric heterochromatin

SUMOylation targets HP1α to pericentric heterochromatin, but the enzyme responsible for removing the SUMO molecule from HP1α has not been determined. SENP7 is now identified as the factor that deconjugates SUMO, promoting retention of HP1α at these domains.

Christèle Maison
Kelly Romeo
Geneviève Almouzni
Research04 Mar 2012
Nature Structural & Molecular Biology

Volume: 19, P: 458-460
The methyltransferase Suv39h1 links the SUMO pathway to HP1α marking at pericentric heterochromatin

The Suv39h histone methyltransferases promote trimethylation of histone H3 on lysine 9 (H3K9me3). Here, in the Suv39h1 paralog, the authors identify an enhancer of HP1a sumoylation activity that impacts heterochromatin.

Christèle Maison
Delphine Bailly
Geneviève Almouzni
ResearchOpen Access18 Jul 2016
Nature Communications

Volume: 7, P: 1-9
Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component

Christèle Maison
Delphine Bailly
Geneviève Almouzni
Research19 Feb 2002
Nature Genetics

Volume: 30, P: 329-334
Reversible disruption of pericentric heterochromatin and centromere function by inhibiting deacetylases

Angela Taddei
Christèle Maison
Geneviève Almouzni
Research04 Jan 2001
Nature Cell Biology

Volume: 3, P: 114-120
SUMOylation promotes de novo targeting of HP1α to pericentric heterochromatin

Geneviève Almouzni and colleagues report that SUMOylation promotes de novo targeting of HP1α to pericentric heterochromatin in mouse. They identify long nuclear non-coding transcripts at major satellite repeats and show that they specifically associate with SUMO-modified HP1 proteins.

Christèle Maison
Delphine Bailly
Geneviève Almouzni
Research13 Feb 2011
Nature Genetics

Volume: 43, P: 220-227
HP1 and the dynamics of heterochromatin maintenance

Christèle Maison
Geneviève Almouzni
Reviews01 Apr 2004
Nature Reviews Molecular Cell Biology

Volume: 5, P: 296-305
An epigenetic silencing pathway controlling T helper 2 cell lineage commitment

The histone modification H3K9me3, the histone methyltransferase SUV39H1 and the H3K9me3-binding protein HP1α participate in maintaining the silent state of the two canonical T helper 1 cell signature genes (which encode interferon-γ and T-bet), ensuring T helper 2 lineage stability in vitro and in vivo; targeting this pathway has the potential to reduce asthma-related pathology.

Rhys S. Allan
Elina Zueva
Sebastian Amigorena
Research04 Jul 2012
Nature

Volume: 487, P: 249-253
De novo SMARCA2 variants clustered outside the helicase domain cause a new recognizable syndrome with intellectual disability and blepharophimosis distinct from Nicolaides–Baraitser syndrome

Gerarda Cappuccio
Camille Sayou
Nicola Brunetti-Pierri
Research22 Jul 2020
Genetics in Medicine

Volume: 22, P: 1838-1850

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The SUMO protease SENP7 is a critical component to ensure HP1 enrichment at pericentric heterochromatin

The methyltransferase Suv39h1 links the SUMO pathway to HP1α marking at pericentric heterochromatin

Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component

Reversible disruption of pericentric heterochromatin and centromere function by inhibiting deacetylases

SUMOylation promotes de novo targeting of HP1α to pericentric heterochromatin

HP1 and the dynamics of heterochromatin maintenance

An epigenetic silencing pathway controlling T helper 2 cell lineage commitment

De novo SMARCA2 variants clustered outside the helicase domain cause a new recognizable syndrome with intellectual disability and blepharophimosis distinct from Nicolaides–Baraitser syndrome

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