Search Results
You are looking at 1 - 1 of 1 items for
- Author: Florenza A La Spina x
- Refine by access: Open Access content only x
Search for other papers by Martina Jabloñski in
Google Scholar
PubMed
Search for other papers by Florenza A La Spina in
Google Scholar
PubMed
Search for other papers by Liza J Schiavi-Ehrenhaus in
Google Scholar
PubMed
Search for other papers by Clara I Marín-Briggiler in
Google Scholar
PubMed
Search for other papers by Matias D Gomez-Elias in
Google Scholar
PubMed
Search for other papers by Dario Krapf in
Google Scholar
PubMed
Search for other papers by Pablo E Visconti in
Google Scholar
PubMed
Search for other papers by Diego Krapf in
Google Scholar
PubMed
Search for other papers by Guillermina M Luque in
Google Scholar
PubMed
Search for other papers by Mariano G Buffone in
Google Scholar
PubMed
Valosin-containing protein (VCP; aka p97), a member of the AAA (ATPases Associated with various cellular Activities) family, has been associated with a wide range of cellular functions. While previous evidence has shown its presence in mammalian sperm, our study unveils its function in mouse sperm. Notably, we found that mouse VCP does not undergo tyrosine phosphorylation during capacitation and exhibits distinct localization patterns. In the sperm head, it resides within the equatorial segment and, following acrosomal exocytosis, it is released and cleaved. In the flagellum, VCP is observed in the principal and midpiece. Furthermore, our research highlights a unique role for VCP in the cAMP/PKA pathway during capacitation. Pharmacological inhibition of sperm VCP led to reduced intracellular cAMP levels that resulted in decreased phosphorylation in PKA substrates and tyrosine residues and diminished fertilization competence. Our results show that in mouse sperm, VCP plays a pivotal role in regulating cAMP production, probably by the modulation of soluble adenylyl cyclase activity.
