SMALL HEAT-SHOCK PROTEINS OF DROSOPHILA ASSOCIATE WITH THE CYTOSKELETON
SMALL HEAT-SHOCK PROTEINS OF DROSOPHILA ASSOCIATE WITH THE CYTOSKELETON
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DOI：
10.1073/pnas.83.1.90
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发表时间：
1986-01-01
影响因子：
11.1
通讯作者：
BONNER, JJ
中科院分区：
文献类型：
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作者：
LEICHT, BG;BIESSMANN, H;BONNER, JJ
热休克的果蝇Kc细胞的分级显示，小的热休克蛋白（HSP 28，-26，-23，和-22）和波形蛋白样中间丝蛋白（IFPs）丰富的核部分。IFPs与核的分离是由于热休克时IFP网络对核的崩溃，提高了小hsps的共分离是通过类似机制的可能性。间接免疫荧光支持这种可能性。在唾液腺中，无论是热休克蛋白和IFPs是细胞质后，轻度至中度的热休克，只有进入细胞核后，严重的，甚至致死性休克。施耐德线2细胞的双标记实验表明，IFPs和小热休克蛋白共定位于相同的核周聚集体中的70%的细胞检查。因此，小的热休克蛋白与细胞骨架，而不是与核结构。
Fractionation of heat-shocked Drosophila melanogaster Kc cells reveals that both the small heat shock proteins (hsp28, -26, -23, and -22) and vimentin-like intermediate filament proteins (IFPs) are abundantly represented in the nuclear fraction. Cofractionation of the IFPs with nuclei is due to the collapse of the IFP network against the nucleus upon heat shock, raising the possibility that cofractionation of the small hsps is by a similar mechanism. Indirect, immunofluorescence supports this possibility. In salivary glands, both the hsps and IFPs are cytoplasmic after mild-to-moderate heat shocks and only enter the nucleus upon severe-indeed, lethal-shocks. Double-label experiments with Schneider line 2 cells show that the IFPs and small hsps colocalize to the same perinuclear aggregates in 70% of the cells examined. Thus, the small hsps are associated with the cytoskeleton rather than with nuclear structures.