Tyrosine phosphorylation of HSP-90 during mammalian sperm capacitation
Tyrosine phosphorylation of HSP-90 during mammalian sperm capacitation
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DOI：
10.1095/biolreprod.103.017350
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发表时间：
2003-12-01
影响因子：
3.6
通讯作者：
Aitken, RJ
中科院分区：
文献类型：
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作者：
Ecroyd, H;Jones, RC;Aitken, RJ
精子获能的过程与导致蛋白酪氨酸磷酸化的信号转导途径的激活相关。而磷酸酪氨酸的表达是受精的一个必要的先决条件，在获能过程中被磷酸化的蛋白质尚未被确定。在本研究中，我们观察到该信号通路的一个主要靶点是分子伴侣蛋白，热休克蛋白（HSP）-86，HSP-90家族的成员。我们使用交叉免疫沉淀实验来证实HSP-86的酪氨酸磷酸化，这是一个不被安莎霉素抗生素格尔德霉素抑制的过程。这些发现的一般意义得到了研究的证实，其中HSP-90也被发现是酪氨酸磷酸化的人类和大鼠精子培养条件下，支持获能。据我们所知，这些结果代表的蛋白质，在小鼠精子获能过程中经历酪氨酸磷酸化的第一次报告和第一次研究牵连分子伴侣的过程中，哺乳动物精子获得受精的卵母细胞的能力。
The process of sperm capacitation is correlated with activation of a signal transduction pathway leading to protein tyrosine phosphorylation. Whereas phosphotyrosine expression is an essential prerequisite for fertilization, the proteins that are phosphorylated during capacitation have not yet been identified. In the present study, we observed that a major target of this signaling pathway is the molecular chaperone protein, heat shock protein (HSP)-86, a member of the HSP-90 family of HSPs. We used cross-immunoprecipitation experiments to confirm the tyrosine phosphorylation of HSP-86, a process that is not inhibited by the ansamycin antibiotic, geldanamycin. The general significance of these findings was confirmed by studies in which HSP-90 was also found to be tyrosine phosphorylated in human and rat spermatozoa when incubated under conditions that support capacitation. To our knowledge, these results represent the first report of a protein that undergoes tyrosine phosphorylation during mouse sperm capacitation and the first study implicating molecular chaperones in the processes by which mammalian spermatozoa gain the ability to fertilize the oocyte.