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Type: Journal article
Title: Tyrosine phosphorylation of HSP-90 during mammalian sperm capacitation
Author: Ecroyd, Heath William
Jones, Russell C.
Aitken, R. John
Citation: Biology of Reproduction, 2003; 69 (6):1801-1807
Publisher: Society Study Reproduction
Issue Date: 2003
ISSN: 0006-3363
School/Discipline: School of Chemistry and Physics : Chemistry
Statement of
Heath Ecroyd, Russell C. Jones, and R. John Aitken
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.
Keywords: gamete biology, signal transduction, sperm capacitation
Description: © 2003 by the Society for the Study of Reproduction
DOI: 10.1095/biolreprod.103.017350
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Appears in Collections:Chemistry and Physics publications

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