ArticleScientific reports2017
The inhibitory mechanism of Hal3 on the yeast Ppz1 phosphatase: A mutagenesis analysis.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Functional mapping of the N-terminal region of the yeast moonlighting protein Sis2/Hal3 reveals crucial residues for Ppz1 regulation.The FEBS journal · 2022Article
- Fungal Hal3 (and Its Close Relative Cab3) as Moonlighting Proteins.Journal of fungi (Basel, Switzerland) · 2022Review
- When Phosphatases Go Mad: The Molecular Basis for Toxicity of Yeast Ppz1.International journal of molecular sciences · 2022Review
- Comparative Analysis of Type 1 and Type Z Protein Phosphatases Reveals D615 as a Key Residue for Ppz1 Regulation.International journal of molecular sciences · 2022Article
- The N-Terminal Region of Yeast Protein Phosphatase Ppz1 Is a Determinant for Its Toxicity.International journal of molecular sciences · 2020Article
- Protein Phosphatase Ppz1 Is Not Regulated by a Hal3-Like Protein in Plant PathogenInternational journal of molecular sciences · 2019Article
- Ser/Thr protein phosphatases in fungi: structure, regulation and function.Microbial cell (Graz, Austria) · 2019Review
- Dissection of the regulatory role for the N-terminal domain in Candida albicans protein phosphatase Z1.PloS one · 2019Article
- Mutations at the hydrophobic core affect Hal3 trimer stability, reducing its Ppz1 inhibitory capacity but not its PPCDC moonlighting function.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Ser/Thr protein phosphatase (PPase) Ppz1 is an enzyme related to the ubiquitous type-1 PPases (PP1c) but found only in fungi. It is regulated by an inhibitory subunit, Hal3, which binds to its catalytic domain. Overexpression of Ppz1 is highly toxic for yeast cells, so its de-regulation has been proposed as a target for novel antifungal therapies. While modulation of PP1c by its many regulatory subunits has been extensively characterized, the manner by which Hal3 controls Ppz1 remains unknown. We have used error-prone PCR mutagenesis to construct a library of Ppz1 variants and developed a functional assay to identify mutations affecting the binding or/and the inhibitory capacity of Hal3. We have characterized diverse Ppz1 mutated versions in vivo and in vitro and found that, although they were clearly refractory to Hal3 inhibition, none of them exhibited significant reduction in Hal3 binding. Mapping the mutations strengthened the notion that Hal3 does not interact with Ppz1 through its RVxF-like motif (found in most PP1c regulators). In contrast, the most relevant mutations mapped to a conserved α-helix region used by mammalian Inhibitor-2 to regulate PP1c. Therefore, modulation of PP1c and Ppz1 by their subunits likely differs, but could share some structural features.
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