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BOR - Papers in Press, published online ahead of print July 30, 2003.
Biol Reprod 2003, 10.1095/biolreprod.103.017350
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Submitted March 20, 2003
Returned for revision April 8, 2003
Accepted July 8, 2003

Gamete Biology


Tyrosine Phosphorylation of HSP-90 During Mammalian Sperm Capacitation

Heath Ecroyd , Russell C. Jones , and R. John Aitken *

* To whom correspondence should be addressed. E-mail: jaitken{at}mail.newcastle.edu.au.

Abstract
This process of sperm capacitation is correlated with the activation of a signal transduction pathway leading to protein tyrosine phosphorylation. While phosphotyrosine expression is an essential prerequisite for fertilization, the identity of the proteins phosphorylated during capacitation still awaits resolution. In this study we have observed that a major target of this signaling pathway is the molecular chaperone protein, heat shock protein 86 (HSP-86), a member of the HSP-90 family of heat shock proteins. 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 in studies in which HSP-90 was also found to be tyrosine phosphorylated in human and rat spermatozoa when incubated under conditions that support capacitation. 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.

Key words: Gamete Biology • Signal transduction • Sperm capacitation


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