ArticleBMC cell biology2013
Identification and characterization of two distinct PPP1R2 isoforms in human spermatozoa.
Article in BMC cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Glycerol Kinase 2 as a Metabolic Sentinel for Human Sperm Motility and Male Fertility.Biomolecules · 2025Review
- PP1, PP2A and PP2B Interplay in the Regulation of Sperm Motility: Lessons from Protein Phosphatase Inhibitors.International journal of molecular sciences · 2022Review
- First Insights on the Presence of the Unfolded Protein Response in Human Spermatozoa.International journal of molecular sciences · 2019Article
- Regulators of the protein phosphatase PP1γ2, PPP1R2, PPP1R7, and PPP1R11 are involved in epididymal sperm maturation.Journal of cellular physiology · 2019Article
- The protein phosphatase isoform PP1γ1 substitutes for PP1γ2 to support spermatogenesis but not normal sperm function and fertility†.Biology of reproduction · 2019Article
- Signaling mechanisms in mammalian sperm motility.Biology of reproduction · 2017Review
- Characterization of the functions and proteomes associated with membrane rafts in chicken sperm.PloS one · 2017Article
- Identification of Candidate Casein Kinase 2 Substrates in Mitosis by Quantitative Phosphoproteomics.Frontiers in cell and developmental biology · 2017Article
- Synphilin-1A is a phosphoprotein phosphatase 1-interacting protein and affects PPP1 sorting to subcellular compartments.Journal of molecular neuroscience : MN · 2015Article
- Identification of a novel human LAP1 isoform that is regulated by protein phosphorylation.PloS one · 2014Article
- Not so pseudo: the evolutionary history of protein phosphatase 1 regulatory subunit 2 and related pseudogenes.BMC evolutionary biology · 2013Article
- Protein phosphatases decrease their activity during capacitation: a new requirement for this event.PloS one · 2013Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 3 countries.
Funding
Abstract
backgroundProtein Ser/Thr Phosphatase PPP1CC2 is an alternatively spliced isoform of PPP1C that is highly enriched in testis and selectively expressed in sperm. Addition of the phosphatase inhibitor toxins okadaic acid or calyculin A to caput and caudal sperm triggers and stimulates motility, respectively. Thus, the endogenous mechanisms of phosphatase inhibition are fundamental for controlling sperm function and should be characterized. Preliminary results have shown a protein phosphatase inhibitor activity resembling PPP1R2 in bovine and primate spermatozoa.
resultsHere we show conclusively, for the first time, that PPP1R2 is present in sperm. In addition, we have also identified a novel protein, PPP1R2P3. The latter was previously thought to be an intron-less pseudogene. We show that the protein corresponding to the pseudogene is expressed. It has PPP1 inhibitory potency similar to PPP1R2. The potential phosphosites in PPP1R2 are substituted by non-phosphorylable residues, T73P and S87R, in PPP1R2P3. We also confirm that PPP1R2/PPP1R2P3 are phosphorylated at Ser121 and Ser122, and report a novel phosphorylation site, Ser127. Subfractionation of sperm structures show that PPP1CC2, PPP1R2/PPP1R2P3 are located in the head and tail structures.
conclusionsThe conclusive identification and localization of sperm PPP1R2 and PPP1R2P3 lays the basis for future studies on their roles in acrosome reaction, sperm motility and hyperactivation. An intriguing possibility is that a switch in PPP1CC2 inhibitory subunits could be the trigger for sperm motility in the epididymis and/or sperm hyperactivation in the female reproductive tract.
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