Differential activation of two protease-activated protein kinases from reticulocytes by a Ca2+-stimulated protease and identification of phosphorylated translational components.

Differential activation of two protease-activated protein kinases from reticulocytes by a Ca2+-stimulated protease and identification of phosphorylated translational components.
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Ca2 刺激的蛋白酶对网织红细胞中两种蛋白酶激活的蛋白激酶的差异激活以及磷酸化翻译成分的鉴定。

DOI:
10.1111/j.1432-1033.1982.tb06793.x
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发表时间:
1982
期刊:
European journal of biochemistry
影响因子:
--
通讯作者:
Traugh,JA
Traugh,JA
中科院分区:
--
文献类型:
--
作者:
Tahara,SM;Traugh,JA

文献摘要

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从兔网织红细胞中部分纯化了两种蛋白激酶,并显示它们可被胰蛋白酶有限的蛋白水解激活[S. M.田原和J. A. Traugh(1981)J.Biol.Chem.256,11558-11564; P.T. Tuazon,W. C.梅里克和J. A. Traugh(1980)J.Biol.Chem.255,10954-10958]。用网织红细胞裂解液检测了可能参与体内蛋白激酶激活的蛋白酶活性,鉴定并部分纯化了两种被Fe ~(2+)和Ca ~(2+)差异激活的中性蛋白酶。Ca 2+刺激的蛋白酶特异性激活蛋白酶活化激酶II;未观察到对蛋白酶活化激酶I的影响。Fe 2+刺激的蛋白酶对两种蛋白激酶都没有活性。使用起始因子(eIF)和40-S核糖体亚基作为底物检查蛋白酶激活激酶。蛋白酶活化激酶I磷酸化eIF-3(Mr 130000)、eIF-4 B和40-S核糖体蛋白S10的一个亚基。蛋白酶活化激酶II修饰eIF-2的β亚基(Mr,53000)和40-S核糖体蛋白S6。与来自网织红细胞的其他cAMP依赖性和cAMP非依赖性蛋白激酶相比,底物特异性是独特的。
Two protein kinases have been partially purified from rabbit reticulocytes and shown to be activated by limited proteolysis with trypsin [S. M. Tahara and J. A. Traugh (1981)J. Biol. Chem. 256, 11558–11564; P. T. Tuazon, W. C. Merrick, and J. A. Traugh (1980)J. Biol. Chem. 255, 10954–10958]. Reticulocyte lysate was examined for protease activities which might be involved in activation of the protein kinasesin vivo.Two neutral proteases, differentially activated by Fe2+and Ca2+, were identified and partially purified. The Ca2+‐stimulated protease specifically activated protease‐activated kinase II; no effect was observed on protease‐activated kinase I. The Fe2+‐stimulated protease was not active on either protein kinase. The protease‐activated kinases were examined using initiation factors (eIF) and 40‐S ribosomal subunits as substrate. Protease‐activated kinase I phosphorylated one subunit of eIF‐3 (Mr130000), eIF‐4B and 40‐S ribosomal protein S10. Protease‐activated kinase II modified the β subunit of eIF‐2 (Mr, 53000) and 40‐S ribosomal protein S6. The substrate specificities are unique when compared with other cAMP‐dependent and cAMP‐independent protein kinases from reticulocytes.
原位和体外磷酸化兔网织红细胞核糖体蛋白的比较。
DOI: 10.1021/bi00648a025
发表时间: 1976
期刊: Biochemistry
影响因子: 2.9
作者:
J. Traugh;G. G. Porter
通讯作者: G. G. Porter
内源性 CA2 依赖性蛋白酶激活和解离天然高分子量形式的兔骨骼肌磷酸化酶磷酸酶。
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发表时间: 1979
期刊: The Journal of biological chemistry
影响因子: --
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影响因子: 4.8
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