Tyrosine Phosphorylation of HSP-90 During Mammalian Sperm Capacitation1

2003/12/01 by Heath Ecroyd, Russell C. Jones, R. John Aitken · 103 citations
Agricultural and Biological Sciences · Biochemistry, Genetics and Molecular Biology · Medicine · #Bee Products Chemical Analysis #Biochemistry #Biology #Capacitation #Cell biology #Geldanamycin #Genetics #Heat shock protein #Heat shock proteins research #Hsp90 #Immunoprecipitation #Phosphorylation #Phosphorylation cascade #Protein kinase A #Protein phosphorylation #Signal transduction #Sperm #Sperm and Testicular Function #Tyrosine #Tyrosine phosphorylation

paper · pdf · doi:10.1095/biolreprod.103.017350

published in Biology of Reproduction 69(6), 1801-1807 (Oxford University Press)

openalex publication_date 2003/12/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/15

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.

Cited by

• Role of tyrosine phosphorylation in sperm capacitation / acrosome reaction. [europepmc]
• Heat shock proteins on the human sperm surface. [europepmc]
• The Australian saltwater crocodile (Crocodylus porosus) provides evidence that the capacitation of spermatozoa may extend beyond the mammalian lineage. [europepmc]
• Progesterone requires heat shock protein 90 (HSP90) in human sperm to regulate motility and acrosome reaction. [europepmc]
• Relationship between HSP90a, NPC2 and L-PGDS proteins to boar semen freezability. [europepmc]
• Sperm Proteome after Interaction with Reproductive Fluids in Porcine: From the Ejaculation to the Fertilization Site. [europepmc]
• ACRBP (Sp32) is involved in priming sperm for the acrosome reaction and the binding of sperm to the zona pellucida in a porcine model. [europepmc]
• GIV/Girdin, a non-receptor modulator for Gαi/s, regulates spatiotemporal signaling during sperm capacitation and is required for male fertility. [europepmc]
• Heat shock protein family D member 1 in boar spermatozoa is strongly related to the litter size of inseminated sows. [europepmc]
• Targeted Analysis of HSP70 Isoforms in Human Spermatozoa in the Context of Capacitation and Motility. [europepmc]
• Heat stress and stallion fertility. [europepmc]
• The proteomic landscape of sperm surface deciphers its maturational and functional aspects in buffalo. [europepmc]
• Higher abundance of DLD protein in buffalo bull spermatozoa causes elevated ROS production leading to early sperm capacitation and reduction in fertilizing ability. [europepmc]

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