SUMO-1 promotes association of SNURF (RNF4) with PML nuclear bodies
SUMO-1 promotes association of SNURF (RNF4) with PML nuclear bodies
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DOI：
10.1016/j.yexcr.2004.10.029
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发表时间：
2005-03-10
影响因子：
3.7
通讯作者：
Palvimo, JJ
中科院分区：
文献类型：
--
作者：
Häkli, M;Karvonen, U;Palvimo, JJ
小核无名指蛋白SNURF （RNF4）参与转录和细胞生长调控。我们在这里表明，内源性SNURF的很大一部分定位于与内源性早幼粒细胞白血病（PML）蛋白和小泛素样修饰因子-1 （SUMO-1）结构域重叠或邻近的核小体（NBs）。在生化分析中，SNURF以非共价方式有效结合SUMO-1。SNURF在非一致附着位点也被SUMO-1共价修饰。SUMO-1的异位表达明显增强了PML3 （PML IV）和SNURF之间的相互作用，但SUMO-1不需要与这两种蛋白的共价附着。此外，在转激活实验中，PML3而非PML- l （PML III）的过表达会消除SNURF的共激活功能，这与PML3将SNURF招募到核小体的能力相似。总之，我们已经确定了SNURF是PML小体中的一个新成分，并表明sumo -1促进了SNURF在这些核结构域的隔离，从而调节了SNURF的转录活性。(C) 2004爱思唯尔公司版权所有。
Small nuclear RING finger protein SNURF (RNF4) is involved in transcriptional and cell growth regulation. We show here that a significant portion of endogenous SNURF localizes to nuclear bodies (NBs) that overlap with or are adjacent to domains containing endogenous promyelocytic leukemia (PML) protein and small ubiquitin-like modifier-1 (SUMO-1). In biochemical assays, SNURF efficiently binds SUMO-1 in a noncovalent fashion. SNURF is also covalently modified by SUMO-1 at nonconsensus attachment sites. Ectopic expression of SUMO-1 markedly enhances the interaction between PML3 (PML IV) and SNURF, but covalent attachment of SUMO-1 to neither protein is required. Moreover, overexpression of PML3, but not PML-L (PML III), abolishes the coactivation function of SNURF in transactivation assays, which parallels the ability of PML3 to recruit SNURF to nuclear bodies. In sum, we have identified SNURF as a novel component in PML bodies and suggest that SUMO-1-facilitated sequestration into these nuclear domains regulates the transcriptional activity of SNURF. (C) 2004 Elsevier Inc. All rights reserved.