Journal
BIOCHEMICAL PHARMACOLOGY
Volume 82, Issue 10, Pages 1403-1415Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bcp.2011.02.018
Keywords
PP1; Human testis; Yeast Two-Hybrid; PP1 interacting proteins
Categories
Funding
- Centre for Cell Biology of the University of Aveiro
- Fundacao para a Ciencia e Tecnologia of the Portuguese Ministry of Science and Higher Education [(SFRH/BPD/16132/2004), (SFRH/BD/41751/2007), (SFRH/BD/42334/2007), (SFRH/BPD/45611/2008), (SFRH/BD/21559/2005), (POCI/SAU-OBS/57394/2004, PPCDT/SAU-OBS/57394/2004]
- [E-92/08
- B-32/09]
- Fundação para a Ciência e a Tecnologia [SFRH/BD/42334/2007, SFRH/BD/41751/2007, SFRH/BD/21559/2005, POCI/SAU-OBS/57394/2004, SFRH/BPD/16132/2004] Funding Source: FCT
Ask authors/readers for more resources
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 gamma 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 gamma 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. (C) 2011 Elsevier Inc. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available