A novel germ cell protein SPIF (Sperm PKA Interacting Factor) forms a complex with PKA and TCP11 during capacitation resulting in tyrosine phosphorylation — ASN Events
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  3. A novel germ cell protein SPIF (Sperm PKA Interacting Factor) forms a complex with PKA and TCP11 during capacitation resulting in tyrosine phosphorylation

A novel germ cell protein SPIF (Sperm PKA Interacting Factor) forms a complex with PKA and TCP11 during capacitation resulting in tyrosine phosphorylation (#274)

Simone Stanger 1 2 3 , Duangporn Jamsai 4 , Moira O'Bryan 4 , Elieen McLaughlin 1 2 3 , John Aitken 2 3 , Shaun Roman 1 2 3
  1. Centre for Chemical Biology, University of Newcastle, Callaghan, NSW, Australia
  2. Priority Reseach Centre for Reproductive Science, University of Newcastle, Callaghan, NSW, A
  3. University of Newcastle, CALLAGHAN, NSW, Australia
  4. Anatomy and Cell Biology, University of Melbourne, Parkville, VIC, Australia

Spermatozoa require the complex process of capacitation to enable them to fertilise an oocyte. Protein Kinase A (PKA) is crucial to capacitation and is an attractive target for understanding germ cell signalling. The current study was designed to identify binding partners of the sperm specific (Cs) isoform of PKA by using it as the ‘bait’ in a yeast-two hybrid system. A novel germ cell specific protein, sperm PKA interacting factor (SPIF), was identified. Homozygous Spif null mice, generated by a special BAC based method, were embryonic lethal and heterozygous deletion lead to transmission ratio distortion. SPIF was co-expressed and co-regulated in later stage germ cells with PKA C and with Tcp11, another gene demonstrating transmission ratio distortion. These three proteins are part of a novel complex in mouse spermatozoa that is rearranged upon capacitation resulting in the tyrosine phosphorylation of the SPIF protein.  These results suggest a role for a complex of SPIF and its partners PKA C and TCP11 during capacitation.

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