作者: Margarida Fardilha , Sara L.C. Esteves , Luís Korrodi-Gregório , Ana Paula Vintém , Sara C. Domingues
DOI: 10.1016/J.BCP.2011.02.018
关键词:
摘要: Protein phosphorylation is a critical regulatory mechanism in cellular signalling. To this end, PP1 major eukaryotic serine/threonine-specific phosphatase whose functions, turn, depend on complexes it forms with interacting proteins-PIPs. The importance of the testis/sperm-enriched variant, PP1γ2, sperm motility and spermatogenesis has previously been shown. Given key role PIPs, imperative to identify physiologically relevant PIPs testis sperm. Hence, we performed Yeast Two-Hybrid screens human cDNA library using as baits different isoforms also proteomic approach aimed at identifying PP1γ2 binding proteins. best our knowledge largest data set interactome. We report identification 77 proteins 7 that bind PP1. obtained increased known interactome by reporting 72 novel interactions. Confirmation interaction 5 was further validated co-immunoprecipitation or protein overlays. here presented provides important insights towards function these opens new possibilities for future research. In fact, such diversity regulators makes them excellent targets pharmacological intervention.