Phosphorylation of calmodulin by plasma-membrane-associated protein kinase(s).
Phosphorylation of calmodulin by plasma-membrane-associated protein kinase(s).
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钙调蛋白被质膜相关蛋白激酶磷酸化。
DOI：
10.1111/j.1432-1033.1995.050_c.x
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发表时间：
1995
期刊：
影响因子：
--
通讯作者：
Villalobo,A
中科院分区：
文献类型：
--
作者：
Benguría,A;Soriano,M;Joyal,JL;Sacks,DB;Villalobo,A
正常大鼠肝脏质膜相关蛋白激酶(S)在无钙离子和组蛋白或多聚L赖氨酸存在的情况下磷酸化外源性牛脑钙调蛋白。当聚(L-赖氨酸)/钙调素摩尔比为0.4时，钙调素磷酸化水平达到最大。磷酸氨基酸分析表明，钙调蛋白在丝氨酸、苏氨酸和酪氨酸残基上被磷酸化。在没有添加阳离子蛋白或多肽的情况下，内源性质膜相关钙调蛋白也被质膜相关蛋白激酶(S)磷酸化。用抗钙调素的特异性单抗进行免疫沉淀，证实了内源性磷酸钙调素的同源性。艾氏腹水瘤细胞质膜不含内源性钙调蛋白。然而，来自这些肿瘤细胞的膜相关蛋白激酶(S)在多聚L赖氨酸存在的情况下磷酸化牛脑钙调蛋白。这些数据表明，磷酸化钙调素存在于肝脏质膜上，并提示这种翻译后修饰可能在该位置具有生理作用。
Plasma‐membrane‐associated protein kinase(s) from normal rat liver phosphorylates exogenous bovine brain calmodulin in the absence of Ca2+and in the presence of histone or poly(l‐lysine). Maximum levels of calmodulin phosphorylation are obtained at a poly (l‐lysine)/calmodulin molar ratio of 0.4. Phosphoamino acid analysis revealed that calmodulin is phosphorylated on serine, threonine and tyrosine residues. Endogenous plasma‐membrane‐associated calmodulin was also phosphorylated by plasma‐membrane‐associated protein kinase(s) in the absence of added cationic protein or polypeptide. The identity of endogenous phosphocalmodulin was confirmed by immunoprecipitation with a specific anti‐calmodulin monoclonal antibody. Ehrlich ascites tumor cell plasma membranes do not contain endogenous calmodulin. However, membrane‐associated protein kinase(s) from these tumor cells phosphorylates bovine brain calmodulin in the presence of poly(l‐lysine). These data demonstrate that phosphocalmodulin is present in liver plasma membranes and suggest that this post‐translational modification could have a physiological role in this location.