PIAS1,2-1 SUMOylate deacetylated HIC1 at lysine-333 (lysine ...

created [InstanceEdit:4090291] May, B, 2013-08-13
dbId 4090383
displayName PIAS1,2-1 SUMOylate deacetylated HIC1 at lysine-333 (lysine ...
modified [InstanceEdit:8955685] May, Bruce, 2017-01-12
schemaClass Summation
text PIAS1,2-1 SUMOylate deacetylated HIC1 at lysine-333 (lysine 314 of HIC1 isoform 2) with SUMO1 (Stankovic-Valentin et al. 2007). Acetylation of HIC1 at lysine-333 inhibits SUMOylation. SUMOylation increases transcription repression by HIC1 (Stankovic-Valentin et al. 2007) and favors the interaction of HIC1 with MTA1 (Van Rechem et al., Mol Cell Biol, 2010) and MTA3 (Paget et al. 2016) notably during the DNA damage response (DDR) to non-repairable double strand breaks (DSBs).(Dehennaut et al. 2013). This increase of HIC1 SUMOylation during the DDR to DSBs is strictly dependent on the ATM kinase (Paget et al. 2016). SUMOylation of HIC1 is dispensable for DNA repair since the non-SUMOylatable point mutant E316A is as efficient as wt HIC1 in Comet assays which measure the repair of DSBs (Paget et al. 2016).
Cite Us!