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Heat shock protein 90 (Hsp90) signaling pathways participate in protein phosphorylation during sperm capacitation. However, the underlying mechanism is largely unknown.

The aim of this study was to explore the interaction between Hsp90 and its co‐chaperone protein, cell division cycle protein Cdc37 (Cdc37), in human spermatozoa.

We examined the effects of H‐89 (a protein kinase A [PKA] inhibitor) and Go6983 (a protein kinase C [PKC] inhibitor) on the phosphorylation of serine, threonine, and tyrosine residues in Hsp90; the effect of 17‐allylamino‐17‐demethoxygeldanamycin (17‐AAG, Hsp90 inhibitor) on Y416‐Src phosphorylation; and the effects of 17‐AAG and geldanamycin on threonine phosphorylation during human sperm capacitation.

Hsp90 co‐localized and interacted with Cdc37. During human sperm capacitation, Hsp90 phosphorylation …