Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae.
Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae.
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DOI：
10.1083/jcb.201106037
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发表时间：
2011-11-14
期刊：
影响因子：
--
通讯作者：
Bukau B
中科院分区：
文献类型：
--
作者：
Specht S;Miller SB;Mogk A;Bukau B
萌芽酵母热休克蛋白Hsp42与错误折叠的蛋白质共聚集，并可能将这些聚集与进一步的分选因素联系起来。蛋白质在细胞内的聚集是一个具有细胞保护功能的有组织的过程。在酿酒酵母中，聚集的蛋白质在空间上被隔离在核旁或外围位置，这些位置针对不同的质量控制途径进行折叠和降解。将错误折叠的蛋白质隔离到这些位置的细胞机制尚不清楚。在这篇文章中，我们证明了酵母的两个小的热休克蛋白之一，Hsp42，在生理性热应激过程中对于外周聚集体的形成是必不可少的。HSP42优先定位于周围聚集体，但在核旁聚集体中大部分缺失，核旁聚集体仍在HSP42Δ细胞中形成。将Hsp42的氨基末端结构域转移到不参与聚集体排序的Hsp26上，使Hsp26能够取代Hsp42的功能。我们的数据表明，Hsp42通过其氨基末端结构域与错误折叠的蛋白质共同聚集，并可能将这些复合体与进一步的分选因子联系起来。
The budding yeast heat shock protein Hsp42 coaggregates with misfolded proteins and may link those aggregates to further sorting factors. The aggregation of proteins inside cells is an organized process with cytoprotective function. In Saccharomyces cerevisiae, aggregating proteins are spatially sequestered to either juxtanuclear or peripheral sites, which target distinct quality control pathways for refolding and degradation. The cellular machinery driving the sequestration of misfolded proteins to these sites is unknown. In this paper, we show that one of the two small heat shock proteins of yeast, Hsp42, is essential for the formation of peripheral aggregates during physiological heat stress. Hsp42 preferentially localizes to peripheral aggregates but is largely absent from juxtanuclear aggregates, which still form in hsp42Δ cells. Transferring the amino-terminal domain of Hsp42 to Hsp26, which does not participate in aggregate sorting, enables Hsp26 to replace Hsp42 function. Our data suggest that Hsp42 acts via its amino-terminal domain to coaggregate with misfolded proteins and perhaps link such complexes to further sorting factors.
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影响因子：
64.5
作者：
Kawaguchi, Y;Kovacs, JJ;Yao, TP
通讯作者：
Yao, TP
DOI：
10.1083/jcb.143.7.1883
发表时间：
1998-12-28
期刊：
The Journal of cell biology
影响因子：
--
作者：
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作者：
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11.4
作者：
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