Association of a myristoylated protein with a biological membrane and its increased phosphorylation by protein kinase C
Association of a myristoylated protein with a biological membrane and its increased phosphorylation by protein kinase C
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肉豆蔻酰化蛋白与生物膜的关联及其通过蛋白激酶 C 增加的磷酸化
DOI：
10.1016/0014-5793(88)80215-1
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发表时间：
1988
期刊：
影响因子：
3.5
通讯作者：
K. Utsumi
中科院分区：
文献类型：
--
作者：
T. Utsumi;K. Yoshinaga;D. Koga;A. Ide;K. Nobori;E. Okimasu;Shigeo Terada;K. Utsumi
用N-羟基琥珀酰亚胺肉豆蔻酸酯在体外对溶菌酶进行了肉豆蔻酰化，并通过CM-纤维素阳离子交换柱层析分离得到了单肉豆蔻酰化溶菌酶。单肉豆蔻酰化的溶菌酶与磷脂囊泡，而协会的天然溶菌酶是可以忽略不计的。膜相关的monomyristoylated溶菌酶磷酸化与部分纯化的大鼠脑钙和磷脂依赖性蛋白激酶（蛋白激酶C）的存在下，钙，磷脂酰丝氨酸和phorbolmyristate醋酸。因此，豆蔻酰化的溶菌酶通过其与膜的疏水缔合而成为蛋白激酶C的底物。本研究结果表明，胞质蛋白的豆蔻酰化可能在信号转导中起重要作用。
A hydrophilic enzyme, lysozyme, was myristoylated in vitro by theN-hydroxysuccinimide ester of myristic acid, and the monomyristoylated lysozyme was isolated by CM-cellulose cation-exchange column chromatography. The monomyristoylated lysozyme associated with phospholipid vesicles, whereas the association of native lysozyme was negligible. The membrane-associated monomyristoylated lysozyme was phosphorylated with partially purified rat brain Ca2+- and phospholipid-dependent protein kinase (protein kinase C) in the presence of Ca2+, phosphatidylserine and phorbolmyristate acetate. Thus, the myristoylated lysozyme became a substrate of protein kinase C through its hydrophobic association with the membrane. The present results suggest that the myristoylation of cytoplasmic proteins may have an important role in signal transduction.
DOI：
10.1073/pnas.82.14.4625
发表时间：
1985-01-01
影响因子：
11.1
作者：
KAMPS, MP;BUSS, JE;SEFTON, BM
通讯作者：
SEFTON, BM