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首页> 外文期刊>Biochimica et biophysica acta. Molecular cell research >Nuclear translocation of the phosphoprotein Hop (Hsp70/Hsp90 organizing protein) occurs under heat shock, and its proposed nuclear localization signal is involved in Hsp90 binding.
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Nuclear translocation of the phosphoprotein Hop (Hsp70/Hsp90 organizing protein) occurs under heat shock, and its proposed nuclear localization signal is involved in Hsp90 binding.

机译：磷酸蛋白Hop（Hsp70 / Hsp90组织蛋白）在热激下发生核易位，其提议的核定位信号与Hsp90结合有关。

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摘要

The Hsp70-Hsp90 complex is implicated in the folding and regulation of numerous signaling proteins, and Hop, the Hsp70-Hsp90 Organizing Protein, facilitates the association of this multichaperone machinery. Phosphatase treatment of mouse cell extracts reduced the number of Hop isoforms compared to untreated extracts, providing the first direct evidence that Hop was phosphorylated in vivo. Furthermore, surface plasmon resonance (SPR) spectroscopy showed that a cdc2 kinase phosphorylation mimic of Hop had reduced affinity for Hsp90 binding. Hop was predominantly cytoplasmic, but translocated to the nucleus in response to heat shock. A putative bipartite nuclear localization signal (NLS) has been identified within the Hsp90-binding domain of Hop. Although substitution of residues within the major arm of this proposed NLS abolished Hop-Hsp90 interaction as determined by SPR, this was not sufficient to prevent the nuclear accumulation of Hop under leptomycin-B treatment and heat shock conditions. These results showed for the first time that the subcellular localization of Hop was stress regulated and that the major arm of the putative NLS was not directly important for nuclear translocation but was critical for Hop-Hsp90 association in vitro. We propose a model in which the association of Hop with Hsp90 and the phosphorylated status of Hop both play a role in the mechanism of nucleo-cytoplasmic shuttling of Hop.
机译：Hsp70-Hsp90复合物与多种信号蛋白的折叠和调控有关，Hop，Hsp70-Hsp90组织蛋白，促进了这种多分子伴侣机器的结合。与未处理的提取物相比，小鼠细胞提取物的磷酸酶处理减少了Hop异构体的数量，这提供了Hop体内磷酸化的第一个直接证据。此外，表面等离振子共振（SPR）光谱显示Hop的cdc2激酶磷酸化模拟物降低了对Hsp90结合的亲和力。啤酒花主要是胞质的，但响应热激而易位至细胞核。在Hop的Hsp90结合域内已鉴定出一个假定的两核定位信号（NLS）。尽管该取代的NLS主臂内的残基取代消除了由SPR确定的Hop-Hsp90相互作用，但这不足以防止在瘦霉素B处理和热休克条件下Hop的核积累。这些结果首次表明，Hop的亚细胞定位是受压力调节的，并且假定的NLS的主要臂对核易位不是直接重要，但对体外Hop-Hsp90结合至关重要。我们提出一个模型，其中Hop与Hsp90的关联和Hop的磷酸化状态均在Hop的核质穿梭机制中起作用。

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