Flagellar motility requires the cAMP-dependent phosphorylation of a heat-stable NP-40-soluble 56 kd protein, axokinin.
Flagellar motility requires the cAMP-dependent phosphorylation of a heat-stable NP-40-soluble 56 kd protein, axokinin.
复制标题
鞭毛运动需要热稳定的 NP-40 可溶性 56 kd 蛋白轴突蛋白的 cAMP 依赖性磷酸化。
DOI:
10.1016/0092-8674(84)90509-9
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发表时间:
1984
期刊:
影响因子:
64.5
通讯作者:
Means,AR
中科院分区:
文献类型:
--
作者:
Tash,JS;Kakar,SS;Means,AR
Using NP-40-treated dog sperm as a model, the stimulatory effect of CAMP upon reactivated flagellar motility has been shown to be dependent upon the CAMP-dependent phosphorylation of a heat-stable NPQO-soluble protein of 56 kd. Examination by twodimensional polyacrylamide gel electrophoresis of NP-40 extract proteins phosphorylated with Y-~* PATP revealed a major CAMP-dependent phosphopeptide at 56 kd. This is the only CAMP-dependent phosphoprotein common to NP-40 extracts of all tissues that show CAMP-dependent stimulation of flagellar motility. These cells and tissues include sea urchin, dog, and human sperm, as well as dog trachea and retina. Moreover, this phosphoprotein is absent in nonstimulatory extracts from tissues such as skeletal muscle, brain, and liver. We conclude that the CAMP-dependent phosphorylation of the 56 kd peptide represents a major regulatory component of not only sperm but other types of axonemal motility as well.