REGULATION OF CAPZ, AN ACTIN CAPPING PROTEIN OF CHICKEN MUSCLE, BY ANIONIC PHOSPHOLIPIDS
REGULATION OF CAPZ, AN ACTIN CAPPING PROTEIN OF CHICKEN MUSCLE, BY ANIONIC PHOSPHOLIPIDS
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DOI：
10.1021/bi00100a006
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发表时间：
1991-09-10
期刊：
影响因子：
2.9
通讯作者：
COOPER, JA
中科院分区：
文献类型：
--
作者：
HEISS, SG;COOPER, JA
鸡肌肉CapZ是肌动蛋白结合蛋白的加帽蛋白家族的成员，与肌动蛋白丝的倒刺末端结合并使肌动蛋白聚合成核。尚未描述加帽蛋白家族的调节。我们报告说，胶束磷脂酰肌醇4，5-二磷酸（PIP 2）结合CapZ和完全抑制其影响肌动蛋白聚合的能力，通过几个独立的测定。较高浓度的其他阴离子磷脂也完全抑制CapZ的活性。中性磷脂没有影响。PIP 2与磷脂酰胆碱或磷脂酰乙醇胺的混合囊泡也抑制CapZ，但Triton X-100的加入既阻止又逆转了PIP 2对CapZ的抑制。
Chicken muscle CapZ, a member of the capping protein family of actin-binding proteins, binds to the barbed end of actin filaments and nucleates actin polymerization. No regulation of the capping protein family has been described. We report that micelles of phosphatidylinositol 4,5-bisphosphate (PIP2) bind to CapZ and completely inhibit its ability to affect actin polymerization as measured by several independent assays. Higher concentrations of other anionic phospholipids also completely inhibit the activity of CapZ. Neutral phospholipids have no effect. Mixed vesicles of PIP2 with phosphatidylcholine or phosphatidylethanolamine also inhibit CapZ, but addition of Triton X-100 both prevents and reverses PIP2's inhibition of CapZ.