Co-repressor activity of scaffold attachment factor B1 requires sumoylation.
Co-repressor activity of scaffold attachment factor B1 requires sumoylation.
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DOI：
10.1016/j.bbrc.2011.04.040
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发表时间：
2011-05-20
影响因子：
3.1
通讯作者：
Oesterreich S
中科院分区：
文献类型：
--
作者：
Garee JP;Meyer R;Oesterreich S
Sumoylation是一种新兴的修饰，与多种细胞过程相关，包括核受体及其协同调节因子的转录活性调节。由于SUMO修饰通常与转录抑制有关，我们研究了SUMO化是否参与了支架附着因子B1转录抑制活性的调节。在这里，我们发现SAFB1被SUMO1和SUMO2/3家族蛋白在赖氨酸的K231和K294上进行修饰。此外，我们证明SAFB1可以与PIAS1相互作用，PIAS1是一种介导SAFB1 SUMO E3连接酶。此外，SENP1被鉴定为使SAFB1脱氧的酶。SAFB1 sumo化位点的突变导致转录抑制的丧失，至少部分原因是与HDAC3（一种已知的转录抑制因子和SAFB1结合伙伴）的相互作用减少。综上所述，转录抑制因子SAFB1同时被SUMO1和SUMO2/3修饰，这种修饰是其充分抑制活性所必需的。
Sumoylation is an emerging modification associated with a variety of cellular processes including the regulation of transcriptional activities of nuclear receptors and their coregulators. As SUMO modifications are often associated with transcriptional repression, we examined if sumoylation was involved in modulation of the transcriptional repressive activity of scaffold attachment factor B1. Here we show that SAFB1 is modified by both the SUMO1 and SUMO2/3 family of proteins, on lysine’s K231 and K294. Further, we demonstrate that SAFB1 can interact with PIAS1, a SUMO E3 ligase which mediates SAFB1 sumoylation. Additionally, SENP1 was identified as the enzyme desumoylating SAFB1. Mutation of the SAFB1 sumoylation sites lead to a loss of transcriptional repression, at least in part due to decreased interaction with HDAC3, a known transcriptional repressor and SAFB1 binding partner. In summary, the transcriptional repressor SAFB1 is modified by both SUMO1 and SUMO2/3, and this modification is necessary for its full repressive activity.
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