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      Ser/Thr protein phosphatases in fungi: structure, regulation and function

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      Author(s): 1 , * , 1 , 1
      Publication date (Electronic, pub):
      Publication date (Electronic, collection):
      Journal: Microbial Cell
      Publisher: Shared Science Publishers OG
      Keywords: protein phosphorylation, protein phosphatases, cell signaling, S. cerevisiae, fungi

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          Abstract

          Reversible phospho-dephosphorylation of proteins is a major mechanism for the control of cellular functions. By large, Ser and Thr are the most frequently residues phosphorylated in eukar-yotes. Removal of phosphate from these amino acids is catalyzed by a large family of well-conserved enzymes, collectively called Ser/Thr protein phosphatases. The activity of these enzymes has an enormous impact on cellular functioning. In this work we pre-sent the members of this family in S. cerevisiae and other fungal species, and review the most recent findings concerning their regu-lation and the roles they play in the most diverse aspects of cell biology.

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          A comprehensive two-hybrid analysis to explore the yeast protein interactome.

          T Ito, T Chiba, R Ozawa … (2001)
          Protein-protein interactions play crucial roles in the execution of various biological functions. Accordingly, their comprehensive description would contribute considerably to the functional interpretation of fully sequenced genomes, which are flooded with novel genes of unpredictable functions. We previously developed a system to examine two-hybrid interactions in all possible combinations between the approximately 6,000 proteins of the budding yeast Saccharomyces cerevisiae. Here we have completed the comprehensive analysis using this system to identify 4,549 two-hybrid interactions among 3,278 proteins. Unexpectedly, these data do not largely overlap with those obtained by the other project [Uetz, P., et al. (2000) Nature (London) 403, 623-627] and hence have substantially expanded our knowledge on the protein interaction space or interactome of the yeast. Cumulative connection of these binary interactions generates a single huge network linking the vast majority of the proteins. Bioinformatics-aided selection of biologically relevant interactions highlights various intriguing subnetworks. They include, for instance, the one that had successfully foreseen the involvement of a novel protein in spindle pole body function as well as the one that may uncover a hitherto unidentified multiprotein complex potentially participating in the process of vesicular transport. Our data would thus significantly expand and improve the protein interaction map for the exploration of genome functions that eventually leads to thorough understanding of the cell as a molecular system.
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            Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.

            Liam Holt, Brian B. Tuch, Judit Villén … (2009)
            To explore the mechanisms and evolution of cell-cycle control, we analyzed the position and conservation of large numbers of phosphorylation sites for the cyclin-dependent kinase Cdk1 in the budding yeast Saccharomyces cerevisiae. We combined specific chemical inhibition of Cdk1 with quantitative mass spectrometry to identify the positions of 547 phosphorylation sites on 308 Cdk1 substrates in vivo. Comparisons of these substrates with orthologs throughout the ascomycete lineage revealed that the position of most phosphorylation sites is not conserved in evolution; instead, clusters of sites shift position in rapidly evolving disordered regions. We propose that the regulation of protein function by phosphorylation often depends on simple nonspecific mechanisms that disrupt or enhance protein-protein interactions. The gain or loss of phosphorylation sites in rapidly evolving regions could facilitate the evolution of kinase-signaling circuits.
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              Ultradeep human phosphoproteome reveals a distinct regulatory nature of Tyr and Ser/Thr-based signaling.

              Kirti Sharma, Stefka Tyanova, Christoph Schaab … (2014)
              Regulatory protein phosphorylation controls normal and pathophysiological signaling in eukaryotic cells. Despite great advances in mass-spectrometry-based proteomics, the extent, localization, and site-specific stoichiometry of this posttranslational modification (PTM) are unknown. Here, we develop a stringent experimental and computational workflow, capable of mapping more than 50,000 distinct phosphorylated peptides in a single human cancer cell line. We detected more than three-quarters of cellular proteins as phosphoproteins and determined very high stoichiometries in mitosis or growth factor signaling by label-free quantitation. The proportion of phospho-Tyr drastically decreases as coverage of the phosphoproteome increases, whereas Ser/Thr sites saturate only for technical reasons. Tyrosine phosphorylation is maintained at especially low stoichiometric levels in the absence of specific signaling events. Unexpectedly, it is enriched on higher-abundance proteins, and this correlates with the substrate KM values of tyrosine kinases. Our data suggest that P-Tyr should be considered a functionally separate PTM of eukaryotic proteomes. Copyright © 2014 The Authors. Published by Elsevier Inc. All rights reserved.
              Article 0 comments Cited 341 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): Microb Cell
                Journal ID (iso-abbrev): Microb Cell
                Journal ID (pmc): Microb Cell
                Journal ID (publisher-id): Microb Cell
                Title: Microbial Cell
                Publisher: Shared Science Publishers OG
                ISSN (Electronic): 2311-2638
                Publication date (Electronic, pub): 24 April 2019
                Publication date (Electronic, collection): 06 May 2019
                Volume: 6
                Issue: 5
                Pages: 217-256
                Affiliations
                [1 ]Departament de Bioquímica i Biologia Molecular and Institut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, Cerdanyola del Vallès, Barcelona, Spain.
                Author notes
                * Corresponding Author: Dr. Joaquín Ariño, Institut de Biotecnologia i Biomedicina (Ed. IBB), Universitat Autònoma de Barcelona, Cerdanyola del Vallès, 08193, Barcelona, Spain; Phone: 34-93-5811315; E-mail: Joaquin.Arino@ 123456uab.es

                The authors wish to state that, due to constriction in the number of allowed references, many relevant publications could not be explicitly cited.

                Conflict of interest: The authors declare no conflict of interest.

                Please cite this article as: Joaquín Ariño, Diego Velázquez and Antonio Casamayor ( 2019). Ser/Thr protein phosphatases in fungi: structure, regulation and function. Microbial Cell 6(5): 217-256. doi: 10.15698/mic2019.05.677

                Article
                Publisher ID: MIC0179E111
                DOI: 10.15698/mic2019.05.677
                PMC ID: 6506691
                PubMed ID: 31114794
                SO-VID: e198efe7-006a-4f7e-a293-ebaa9f906754
                Copyright statement: Copyright @ 2019
                License:

                This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged.

                History
                Date received : 01 February 2019
                Date revision received : 19 March 2019
                Date accepted : 21 March 2019
                Funding
                Work in the author's laboratory has been supported by grants BFU2014-54591-C2-1-P (Ministerio de Economía y Competitividad, Spain) and BFU2017-82574-P (Ministerio de Ciencia, Innovación y Universidades, Spain). DV has been recipient of a UAB-PIF fellowship. We thank Dr. Ethel Queralt (IDIBELL, Barcelona), for critical review and suggestions.
                Categories
                Subject: Review
                Subject: Protein Phosphorylation
                Subject: Protein Phosphatases
                Subject: Cell Signaling
                Subject: S. Cerevisiae
                Subject: Fungi

                Keywords: protein phosphorylation,protein phosphatases,cell signaling,s. cerevisiae,fungi
                Data availability:
                Keywords: protein phosphorylation, protein phosphatases, cell signaling, s. cerevisiae, fungi

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