Molecular cloning of a protein kinase whose phosphorylation is regulated by genetic adhesion during Chlamydomonas fertilization.
Molecular cloning of a protein kinase whose phosphorylation is regulated by genetic adhesion during Chlamydomonas fertilization.
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一种蛋白激酶的分子克隆，其磷酸化在衣藻受精过程中受到遗传粘附的调节。
DOI：
10.1073/pnas.93.1.39
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发表时间：
1996
影响因子：
11.1
通讯作者：
Snell,WJ
中科院分区：
文献类型：
--
作者：
Kurvari,V;Zhang,Y;Luo,Y;Snell,WJ
衣藻的受精是由相反交配类型的配子之间通过称为凝集素的鞭毛糖蛋白进行的粘附性相互作用而启动的。这些细胞黏附分子之间的相互作用通过蛋白激酶的相互作用来激活腺苷环化酶，最终导致二倍体受精卵的形成。粘连诱导的信号转导过程中的早期事件之一是鞭毛蛋白激酶的快速失活，它使鞭毛中的48 kDa蛋白磷酸化。我们报道了48 kDa蛋白的生化和分子特征。利用细菌表达的融合蛋白进行的实验表明，48 kDa蛋白能够在丝氨酸和酪氨酸上自动磷酸化，并能使牛β-酪蛋白在丝氨酸上磷酸化，证实了48 kDa蛋白本身具有蛋白激酶活性。这种蛋白激酶与真核蛋白激酶超家族成员的同源性有限，可能是受精信号通路中的一个重要元件。
Fertilization in Chlamydomonas is initiated by adhesive interactions between gametes of opposite mating types through flagellar glycoproteins called agglutinins. Interactions between these cell adhesion molecules signal for the activation of adenylyl cyclase through an interplay of protein kinases and ultimately result in formation of a diploid zygote. One of the early events during adhesion-induced signal transduction is the rapid inactivation of a flagellar protein kinase that phosphorylates a 48-kDa protein in the flagella. We report the biochemical and molecular characterization of the 48-kDa protein. Experiments using a bacterially expressed fusion protein show that the 48-kDa protein is capable of autophosphorylation on serine and tyrosine and phosphorylation of bovine beta-casein on serine, confirming that the 48-kDa protein itself has protein kinase activity. This protein kinase exhibits limited homology to members of the eukaryotic protein kinase superfamily and may be an important element in a signaling pathway in fertilization.
DOI：
--
发表时间：
1994
期刊：
影响因子：
--
作者：
A. Harwood
通讯作者：
A. Harwood