Regulation of ribosomal protein S6 phosphorylation in heat-shocked HeLa cells.
Regulation of ribosomal protein S6 phosphorylation in heat-shocked HeLa cells.
复制标题
热休克 HeLa 细胞中核糖体蛋白 S6 磷酸化的调节。
DOI:
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发表时间:
1987
期刊:
影响因子:
--
通讯作者:
O. Martini
中科院分区:
文献类型:
--
作者:
P. Tas;O. Martini
Decreases in energy charge, ribosomal protein phosphorylation and rate of protein synthesis are well-documented facets of the cellular response to hyperthermia in non-vertebrates. We have tried to reproduce this response pattern in 32P-labelled HeLa cells in order to investigate the hypothetical causal relationship between these effects. In HeLa cells shifted from 36 degrees C to 42 degrees C, dephosphorylation of S6 and inhibition of protein synthesis, owing to a decreased initiation rate, were observed, but could not have been mediated by changes in the cells' general energy charge since the ATP and GTP levels were not reduced. In addition, we found that the hyperthermic translation block developed faster than the overall dephosphorylation of S6, showing that S6 dephosphorylation cannot be responsible for the translation block unless site-specific effects play a critical role.
DOI:
10.1111/j.1432-1033.1984.tb08088.x
发表时间:
1984
期刊:
European journal of biochemistry
影响因子:
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作者:
Panniers,R;Henshaw,EC
通讯作者:
Henshaw,EC
DOI:
10.1073/pnas.79.9.2937
发表时间:
1982
影响因子:
11.1
作者:
Nielsen,PJ;Thomas,G;Maller,JL
通讯作者:
Maller,JL
DOI:
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发表时间:
1985
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Panniers,R;Stewart,EB;Merrick,WC;Henshaw,EC
通讯作者:
Henshaw,EC