Autophosphorylation and protein kinase activity of p21-activated protein kinase gamma-PAK are differentially affected by magnesium and manganese.
Autophosphorylation and protein kinase activity of p21-activated protein kinase gamma-PAK are differentially affected by magnesium and manganese.
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p21 激活蛋白激酶 gamma-PAK 的自磷酸化和蛋白激酶活性受镁和锰的影响不同。
DOI：
10.1021/bi982103o
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发表时间：
1998
期刊：
影响因子：
2.9
通讯作者：
Traugh,JA
中科院分区：
文献类型：
--
作者：
Tuazon,PT;Chinwah,M;Traugh,JA
To examine the requirements for activation of the p21-activated protein kinase γ-PAK (Pak2, PAK I) from rabbit reticulocytes by Cdc42(GTPγS), autophosphorylation with ATP(Mg) or ATP(Mn) and its effects on protein kinase activity were examined. Autophosphorylation with ATP(Mg) alone was minimal with negligible protein kinase activity; the rate of autophosphorylation was increased 3−4-fold upon binding of Cdc42(GTPγS), resulting in a 3-fold stimulation of protein kinase activity with peptide and protein substrates. The rate of autophosphorylation with ATP(Mn) was 4.7-fold faster than with ATP(Mg) alone and was stimulated 2-fold by Cdc42(GTPγS). However, γ-PAK autophosphorylated with ATP(Mn) in the presence or absence of Cdc42(GTPγS) did not phosphorylate peptide or protein substrates in the presence of ATP(Mn), indicating that γ-PAK can utilize ATP(Mn) for autophosphorylation but not for phosphorylation of exogenous substrates. Tryptic phosphopeptide maps of γ-PAK autophosphorylated with ATP(Mg) alone showed 3 phosphopeptides, while with Cdc42(GTPγS) a total of 9 major phosphopeptides was observed. When γ-PAK was autophosphorylated with ATP(Mn) in the presence or absence of Cdc42(GTPγS), 7 major phosphopeptides were observed, which were identical to peptides obtained with Cdc42(GTPγS) and ATP(Mg). Utilizing a recombinant mutant of γ-PAK with alanine replacing threonine 402 in the catalytic region (T402A), it was determined that the two additional phosphopeptides observed in active PAK (peptides 7 and 8) were due to phosphorylation of threonine 402. These results show that Mn sustains autophosphorylation on serine but does not support autophosphorylation of threonine 402, which is required for activity toward exogenous substrates, or phosphorylation of these substrates.
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DOI：
10.1016/s0021-9258(18)53160-4
发表时间：
1993-04
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
R. Colbran
通讯作者：
R. Colbran
自磷酸化过程中 Ca/钙调蛋白依赖性蛋白激酶 II 的失活和自缔合 (*)
影响因子：
4.8
作者：
A. Hudmon;J. Aronowski;S. Kolb;Neal Waxham
通讯作者：
Neal Waxham
通过野生型酶的共表达体内激活重组cAPK催化亚基活性位点突变体，分子间共翻译磷酸化的证据
影响因子：
3.5
作者：
A. Girod;V. Kinzel;D. Bossemeyer
通讯作者：
D. Bossemeyer
通过自磷酸化自动激活钙调蛋白依赖性蛋白激酶 II。
DOI：
10.1016/s0021-9258(18)49951-6
发表时间：
1991
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
T. Katoh;H. Fujisawa
通讯作者：
H. Fujisawa
钙/钙调蛋白依赖性蛋白激酶 II 的钙/钙调蛋白非依赖性自磷酸化位点。
DOI：
--
发表时间：
1990
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Colbran,RJ;Soderling,TR
通讯作者：
Soderling,TR