Baranova L A, Grits A N, Volotovskiĭ I D
Biofizika. 1996 Nov-Dec;41(6):1258-63.
The protein composition of microtubular structures of bovine retinal rod axoneme and phosphorylation of its proteins were studied. The axoneme was shown to consist of proteins of 25, 43, 51, 112, 145 and 240 kDa molecular mass. It was demonstrated that 32P is mainly incorporated into the 25, 43 and 51 kDa proteins. cGMP was found to enhance 32P. Incorporation into these proteins. In the presence of Ca(2+)-calmodulin the phosphorylation of the 43 and 51 kDa proteins was increased. The phosphoinositides were shown to be phosphorylated in axoneme. Phosphatidylinositol 4-monophosphate was found to be a principal substrate for phosphatidylinositol kinases to form phosphatidylinositol 4,5-bisphosphate. Ca2+, neomycin and colchicine inhibited 32P incorporation into phosphatidylinositol 4,5-bisphosphate indicating the dependence of phosphatidylinositol 4-monophosphate phosphorylation on structural state of axoneme. Phosphatidylinositol was found to diminish the axoneme ability for the polymerization of microtubules. Data was showed that kinases responsible for protein and phosphoinositides phosphorylation were tightly bound to axoneme structures.
对牛视网膜视杆轴丝微管结构的蛋白质组成及其蛋白质磷酸化进行了研究。结果表明，轴丝由分子量为25、43、51、112、145和240 kDa的蛋白质组成。已证明32P主要掺入25、43和51 kDa的蛋白质中。发现cGMP可增强32P掺入这些蛋白质中。在Ca(2+)-钙调蛋白存在下，43和51 kDa蛋白质的磷酸化增加。已表明轴丝中的磷酸肌醇会发生磷酸化。发现磷脂酰肌醇4-单磷酸是磷脂酰肌醇激酶形成磷脂酰肌醇4,5-二磷酸的主要底物。Ca2+、新霉素和秋水仙碱抑制32P掺入磷脂酰肌醇4,5-二磷酸，表明磷脂酰肌醇4-单磷酸的磷酸化依赖于轴丝的结构状态。发现磷脂酰肌醇会降低轴丝微管聚合的能力。数据表明，负责蛋白质和磷酸肌醇磷酸化的激酶与轴丝结构紧密结合。
