Identification of the human testis protein phosphatase 1 interactome

Margarida Fardilha (Lead / Corresponding author), Sara L. C. Esteves, Luis Korrodi-Gregório, Ana Paula Vintém, Sara C. Domingues, Sandra Rebelo, Nick Morrice, Patricia T. W. Cohen, Odette A. B. da cruz e silva, Edgar F. da cruz e silva

    Research output: Contribution to journalArticlepeer-review

    62 Citations (Scopus)


    Protein phosphorylation is a critical regulatory mechanism in cellular signalling. To this end, PP1 is a major eukaryotic serine/threonine-specific phosphatase whose cellular functions, in turn, depend on complexes it forms with PP1 interacting proteins - PIPs. The importance of the testis/sperm-enriched variant, PP1?2, 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 human testis cDNA library using as baits the different PP1 isoforms and also a proteomic approach aimed at identifying PP1?2 binding proteins. To the best of our knowledge this is the largest data set of the human testis PP1 interactome. We report the identification of 77 proteins in human testis and 7 proteins in human sperm that bind PP1. The data obtained increased the known PP1 interactome by reporting 72 novel interactions. Confirmation of the interaction of PP1 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 PP1 regulators makes them excellent targets for pharmacological intervention.
    Original languageEnglish
    Pages (from-to)1403-1415
    Number of pages13
    JournalBiochemical Pharmacology
    Issue number10
    Publication statusPublished - 2011


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