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首页> 外文期刊>Cell motility and the cytoskeleton >Microtubule sliding movement in tilapia sperm flagella axoneme is regulated by Ca2+/calmodulin-dependent protein phosphorylation.
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Microtubule sliding movement in tilapia sperm flagella axoneme is regulated by Ca2+/calmodulin-dependent protein phosphorylation.

机译：罗非鱼精子鞭毛轴突中的微管滑动运动受Ca2 + /钙调蛋白依赖性蛋白磷酸化的调节。

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摘要

Demembranated euryhaline tilapia Oreochromis mossambicus sperm were reactivated in the presence of concentrations in excess of 10(-6) M Ca(2+). Motility features changed when Ca(2+) concentrations were increased from 10(-6) to 10(-5) M. Although the beat frequency did not increase, the shear angle and wave amplitude of flagellar beating increased, suggesting that the sliding velocity of microtubules in the axoneme, which represents dynein activity, rises with an increase in Ca(2+). Thus, it is possible that Ca(2+) binds to flagellar proteins to activate flagellar motility as a result of the enhanced dynein activity. One Ca(2+)-binding protein (18 kDa, pI 4.0), calmodulin (CaM), was detected by (45)Ca overlay assay and immunologically. A CaM antagonist, W-7, suppressed the reactivation ratio and swimming speed, suggesting that the 18 kDa Ca(2+)-binding protein is CaM and that CaM regulates flagellar motility. CaMKIV was detected immunologically as a single 48 kDa band in both the fraction of low ion extract of the axoneme and the remnant of the axoneme, suggesting that CaMKIV binds to distinct positions in the axoneme. It is possible that CaMKIV phosphorylates the axonemal proteins in a Ca(2+)/CaM-dependent manner for regulating the dynein activity. A (32)P-uptake in the axoneme showed that 48, 75, 120, 200, 250, 380, and 400 kDa proteins were phosphorylated in a Ca(2+)/CaM kinase-dependent manner. Proteins (380 kDa) were phosphorylated in the presence of 10(-5) M Ca(2+). It is possible that an increase in Ca(2+) induces Ca(2+)/CaM kinase-dependent regulation, including protein phosphorylation for activation/regulation of dynein activity in flagellar axoneme.
机译：在超过10（-6）M Ca（2+）浓度的情况下，去膜的去核的欧亚罗非鱼Oreochromis mossambicus精子被重新激活。当Ca（2+）浓度从10（-6）增加到10（-5）M时，运动功能发生变化。尽管搏动频率没有增加，但鞭毛搏动的剪切角和波幅却增加了，表明滑动速度代表动力蛋白活性的轴突中的微管数量随Ca（2+）的增加而增加。因此，有可能是Ca（2+）与鞭毛蛋白结合，从而由于增强的达因活性而激活鞭毛运动。一种钙（2 +）结合蛋白（18 kDa，pI 4.0），钙调蛋白（CaM），通过（45）Ca覆盖检测和免疫学检测。 CaM拮抗剂，W-7，抑制了再激活率和游泳速度，表明18 kDa Ca（2+）结合蛋白是CaM，并且CaM调节鞭毛运动。 CaMKIV在轴突的低离子提取物部分和轴突的残基中均以一条48 kDa的免疫条带被检测到，这表明CaMKIV结合在轴突的不同位置。 CaMKIV可能以Ca（2 +）/ CaM依赖性方式磷酸化轴索蛋白，以调节动力蛋白的活性。轴突中的（32）P吸收显示48、75、120、200、250、380和400 kDa蛋白质以Ca（2 +）/ CaM激酶依赖性方式被磷酸化。蛋白质（380 kDa）在10（-5）M Ca（2+）存在下被磷酸化。 Ca（2+）的增加可能诱导Ca（2 +）/ CaM激酶依赖性调节，包括蛋白质磷酸化，以激活/调节鞭毛轴突中的达因活性。

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