Translator Disclaimer
1 December 2003 Tyrosine Phosphorylation of HSP-90 During Mammalian Sperm Capacitation
Author Affiliations +
Abstract

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.

Heath Ecroyd, Russell C. Jones, and R. John Aitken "Tyrosine Phosphorylation of HSP-90 During Mammalian Sperm Capacitation," Biology of Reproduction 69(6), 1801-1807, (1 December 2003). https://doi.org/10.1095/biolreprod.103.017350
Received: 20 March 2003; Accepted: 1 July 2003; Published: 1 December 2003
JOURNAL ARTICLE
7 PAGES

This article is only available to subscribers.
It is not available for individual sale.
+ SAVE TO MY LIBRARY

SHARE
ARTICLE IMPACT
RIGHTS & PERMISSIONS
Get copyright permission
Back to Top