A novel germ cell protein, SPIF (sperm PKA interacting factor), is essential for the formation of a PKA/TCP11 complex that undergoes conformational and phosphorylation changes upon capacitation. Issue 8 (22nd April 2016)
- Record Type:
- Journal Article
- Title:
- A novel germ cell protein, SPIF (sperm PKA interacting factor), is essential for the formation of a PKA/TCP11 complex that undergoes conformational and phosphorylation changes upon capacitation. Issue 8 (22nd April 2016)
- Main Title:
- A novel germ cell protein, SPIF (sperm PKA interacting factor), is essential for the formation of a PKA/TCP11 complex that undergoes conformational and phosphorylation changes upon capacitation
- Authors:
- Stanger, Simone J.
Law, Estelle A.
Jamsai, Duangporn
O'Bryan, Moira K.
Nixon, Brett
McLaughlin, Eileen A.
Aitken, R. John
Roman, Shaun D. - Abstract:
- ABSTRACT: Spermatozoa require the process of capacitation to enable them to fertilize an egg. PKA is crucial to capacitation and the development of hyperactivated motility. Sperm PKA is activated by cAMP generated by the germ cell‐enriched adenylyl cyclase encoded by Adcy10 . Male mice lacking Adcy10 are sterile, because their spermatozoa are immotile. The current study was designed to identify binding partners of the sperm‐specific (Cα2) catalytic subunit of PKA (PRKACA) by using it as the "bait" in a yeast 2‐hybrid system. This approach was used to identify a novel germ cell‐enriched protein, sperm PKA interacting factor (SPIF), in 25% of the positive clones. Homozygous Spif ‐null mice were embryonically lethal. SPIF was coexpressed and coregulated with PRKACA and with t‐complex protein (TCP)‐11, a protein associated with PKA signaling. We established that these 3 proteins form part of a novel complex in mouse spermatozoa. Upon capacitation, the SPIF protein becomes tyrosine phosphorylated in >95% of sperm. An apparent molecular rearrangement in the complex occurs, bringing PRKACA and TCP11 into proximity. Taken together, these results suggest a role for the novel complex of SPIF, PRKACA, and TCP11 during sperm capacitation, fertilization, and embryogenesis.—Stanger, S. J., Law, E. A., Jamsai, D., O'Bryan, M. K., Nixon, B., McLaughlin, E. A., Aitken, R. J., Roman, S. D. A novel germ cell protein, SPIF (sperm PKA interacting factor), is essential for the formation of aABSTRACT: Spermatozoa require the process of capacitation to enable them to fertilize an egg. PKA is crucial to capacitation and the development of hyperactivated motility. Sperm PKA is activated by cAMP generated by the germ cell‐enriched adenylyl cyclase encoded by Adcy10 . Male mice lacking Adcy10 are sterile, because their spermatozoa are immotile. The current study was designed to identify binding partners of the sperm‐specific (Cα2) catalytic subunit of PKA (PRKACA) by using it as the "bait" in a yeast 2‐hybrid system. This approach was used to identify a novel germ cell‐enriched protein, sperm PKA interacting factor (SPIF), in 25% of the positive clones. Homozygous Spif ‐null mice were embryonically lethal. SPIF was coexpressed and coregulated with PRKACA and with t‐complex protein (TCP)‐11, a protein associated with PKA signaling. We established that these 3 proteins form part of a novel complex in mouse spermatozoa. Upon capacitation, the SPIF protein becomes tyrosine phosphorylated in >95% of sperm. An apparent molecular rearrangement in the complex occurs, bringing PRKACA and TCP11 into proximity. Taken together, these results suggest a role for the novel complex of SPIF, PRKACA, and TCP11 during sperm capacitation, fertilization, and embryogenesis.—Stanger, S. J., Law, E. A., Jamsai, D., O'Bryan, M. K., Nixon, B., McLaughlin, E. A., Aitken, R. J., Roman, S. D. A novel germ cell protein, SPIF (sperm PKA interacting factor), is essential for the formation of a PKA/TCP11 complex that undergoes conformational and phosphorylation changes upon capacitation. FASEB J. 30, 2777‐2791 (2016). www.fasebj.org … (more)
- Is Part Of:
- FASEB journal. Volume 30:Issue 8(2016)
- Journal:
- FASEB journal
- Issue:
- Volume 30:Issue 8(2016)
- Issue Display:
- Volume 30, Issue 8 (2016)
- Year:
- 2016
- Volume:
- 30
- Issue:
- 8
- Issue Sort Value:
- 2016-0030-0008-0000
- Page Start:
- 2777
- Page End:
- 2791
- Publication Date:
- 2016-04-22
- Subjects:
- protein kinase A -- tyrosine kinase -- protein complex -- sperm capacitation
Biology -- Periodicals
Biology, Experimental -- Periodicals
570 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
- DOI:
- 10.1096/fj.201500136R ↗
- Languages:
- English
- ISSNs:
- 0892-6638
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 13314.xml