ArticleScientific reports2015
Complex stability and dynamic subunit interchange modulates the disparate activities of the yeast moonlighting proteins Hal3 and Vhs3.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- 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
- Yeast Ppz1 protein phosphatase toxicity involves the alteration of multiple cellular targets.Scientific reports · 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
- Methionine triggers Ppz-mediated dephosphorylation of Art1 to promote cargo-specific endocytosis.The Journal of cell biology · 2019Article
- Mutations at the hydrophobic core affect Hal3 trimer stability, reducing its Ppz1 inhibitory capacity but not its PPCDC moonlighting function.Scientific reports · 2018Article
- The inhibitory mechanism of Hal3 on the yeast Ppz1 phosphatase: A mutagenesis analysis.Scientific reports · 2017Article
- The Expanding Landscape of Moonlighting Proteins in Yeasts.Microbiology and molecular biology reviews : MMBR · 2016Review
- Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Saccharomyces cerevisiae Hal3 and Vhs3 are moonlighting proteins, acting both as inhibitors of the serine/threonine protein phosphatase Ppz1 and as subunits (together with Cab3) of the unique heterotrimeric phosphopantothenoylcysteine decarboxylase (PPCDC) enzyme of Hemiascomycetous yeast. Both these roles are essential: PPCDC catalyses the third step of coenzyme A biosynthesis, while Ppz1 inhibition is required for regulation of monovalent cation homeostasis. However, the mechanisms by which these proteins' disparate activities are regulated are not well understood. The PPCDC domains (PDs) of Hal3, Vhs3 and Cab3 constitute the minimum requirement for these proteins to show both PPCDC activity and, in the case of Hal3 and Vhs3, to bind to Ppz1. Using these PD proteins as a model system to study the possibility of dynamic interchange between these roles, we provide evidence that Hal3 binds Ppz1 as a monomer (1:1 stoichiometry), requiring it to de-oligomerize from its usual homo- and heterotrimeric states (the latter having PPCDC activity). This de-oligomerization is made possible by structural features that set Hal3 apart from Vhs3, increasing its ability to undergo monomer exchange. These findings suggest that oligomer interchange may be a significant factor in the functional regulation of these proteins and their various unrelated (moonlighting) functions.
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