Tyrosine phosphorylation of HSP-90 during mammalian sperm capacitation

被引:76
作者
Ecroyd, H
Jones, RC
Aitken, RJ [1 ]
机构
[1] Univ Newcastle, Reprod Sci Grp, Newcastle, NSW 2308, Australia
[2] Univ Newcastle, Sch Environm & Life Sci, Newcastle, NSW 2308, Australia
[3] Univ Newcastle, ARC Ctr Excellence Biotechnol & Dev, Newcastle, NSW 2308, Australia
关键词
gamete biology; signal transduction; sperm capacitation;
D O I
10.1095/biolreprod.103.017350
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:1801 / 1807
页数:7
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