Abstract
Type 2C Ser/Thr phosphatases are a remarkable class of protein phosphatases, which are conserved in eukaryotes and involved in a large variety of functional processes. Unlike in other Ser/Thr phosphatases, the catalytic polypeptide is not usually associated with regulatory subunits, and functional specificity is achieved by encoding multiple isoforms. For fungi, most information comes from the study of type 2C protein phosphatase (PP2C) enzymes in Saccharomyces cerevisiae, where seven PP2C-encoding genes (PTC1 to -7) with diverse functions can be found. More recently, data on several Candida albicans PP2C proteins became available, suggesting that some of them can be involved in virulence. In this work we review the available literature on fungal PP2Cs and explore sequence databases to provide a comprehensive overview of these enzymes in fungi.
Highlights
Reversible phosphorylation of proteins is a major mechanism regulating many biological processes such as metabolism, gene transcription, or cell cycle
Type 2C Ser/Thr phosphatases are a remarkable class of protein phosphatases, which are conserved in eukaryotes and involved in a large variety of functional processes
An additional link between type 2C phosphatases and the cell wall integrity (CWI) pathway regulation was established when Takada and coworkers reported that Ptc1 and Ptc3 modulate Pmk1 phosphorylation levels induced by the cell wall-damaging agent micafungin [97]
Summary
Reversible phosphorylation of proteins is a major mechanism regulating many biological processes such as metabolism, gene transcription, or cell cycle. These authors showed that in cells lacking PTC1 intracellular glycerol levels are higher than in the wild type and that this phenotype is suppressed by the deletion of PBS2, suggesting that the ptc1 mutation may increase the activity of the HOG pathway (Fig. 2a).
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
