Identification of the XXXX testis protein phosphatase 1 interactome.

@entity1 @entity1889 @entity27863 @entity563
Protein phosphorylation is a critical regulatory mechanism in cellular signalling. To this end, @entity27863 is a major eukaryotic @entity563 / @entity1889 -specific phosphatase whose cellular functions, in turn, depend on complexes it forms with @entity27863 interacting proteins-PIPs. The importance of the testis/sperm-enriched variant, PP1y2, in sperm motility and spermatogenesis has previously been shown. Given the key role of PIPs, it is imperative to identify the physiologically relevant PIPs in testis and sperm. Hence, we performed Yeast Two-Hybrid screens of a @entity1 testis cDNA library using as baits the different @entity27863 isoforms and also a proteomic approach aimed at identifying PP1y2 binding proteins. To the best of our knowledge this is the largest data set of the @entity1 testis @entity27863 interactome. We report the identification of 77 proteins in @entity1 testis and 7 proteins in @entity1 sperm that bind @entity27863 . The data obtained increased the known @entity27863 interactome by reporting 72 novel interactions. Confirmation of the interaction of @entity27863 with 5 different proteins was also further validated by co-immunoprecipitation or protein overlays. The data here presented provides important insights towards the function of these proteins and opens new possibilities for future research. In fact, such diversity in @entity27863 regulators makes them excellent targets for pharmacological intervention.
