Tyrosine phosphorylation of HSP-90 during mammalian sperm capacitation
Date
2003
Authors
Ecroyd, Heath William
Jones, Russell C.
Aitken, R. John
Editors
Advisors
Journal Title
Journal ISSN
Volume Title
Type:
Journal article
Citation
Biology of Reproduction, 2003; 69 (6):1801-1807
Statement of Responsibility
Heath Ecroyd, Russell C. Jones, and R. John Aitken
Conference Name
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.
School/Discipline
School of Chemistry and Physics : Chemistry
Dissertation Note
Provenance
Description
© 2003 by the Society for the Study of Reproduction