Diverse and conserved roles of the protein Ssu72 in eukaryotes: from yeast to higher organisms

Liu, Changfu; Zhang, Weihao; Xing, Wenge

doi:10.1007/s00294-020-01132-5

Cited by 6 publications

(4 citation statements)

References 94 publications

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“…Examples of protein phosphatases within this group include the classical PTPs (PF00102), which are responsible for the dephosphorylation of tyrosine residues, and the CDC25 phosphatase (PF00581), which dephosphorylates tyrosine in cyclin‐dependent kinases (CDK) (Boutros et al., 2007 ). Additionally, dual specificity phosphatases (PF00782, DSP) dephosphorylate serine, threonine and tyrosine residues (Patterson et al., 2009 ), while the low molecular weight protein tyrosine phosphatase (PF01451, LMWPTP) (Hoekstra et al., 2015 ) and SSU72 (PF04722) target serine residues in the C‐terminal domain of RNA polymerase II (Liu et al., 2021 ). The Cys‐based group includes nonprotein phosphatases, such as Paladin (PF14566), Sac (PF02383) and Myotubularin (PF06602) (Figure S1 ), which act on lipid substrates (Courtney & Deiters, 2019 ).…”

Section: Discussionmentioning

confidence: 99%

Mining oomycete proteomes for phosphatome leads to the identification of specific expanded phosphatases in oomycetes

Qiu,

Sun,

et al. 2024

Molecular Plant Pathology

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Phosphatases are important regulators of protein phosphorylation and various cellular processes, and they serve as counterparts to kinases. In this study, our comprehensive analysis of oomycete complete proteomes unveiled the presence of approximately 3833 phosphatases, with most species estimated to have between 100 and 300 putative phosphatases. Further investigation of these phosphatases revealed a significant increase in protein serine/threonine phosphatases (PSP) within oomycetes. In particular, we extensively studied the metallo‐dependent protein phosphatase (PPM) within the PSP family in the model oomycete Phytophthora sojae. Our results showed notable differences in the expression patterns of PPMs throughout 10 life stages of P. sojae, indicating their vital roles in various stages of oomycete pathogens. Moreover, we identified 29 PPMs in P. sojae, and eight of them possessed accessory domains in addition to phosphate domains. We investigated the biological function of one PPM protein with an extra PH domain (PPM1); this protein exhibited high expression levels in both asexual developmental and infectious stages. Our analysis confirmed that PPM1 is indeed an active protein phosphatase, and its accessory domain does not affect its phosphatase activity. To delve further into its function, we generated knockout mutants of PPM1 and validated its essential roles in mycelial growth, sporangia and oospore production, as well as infectious stages. To the best of our knowledge, this study provides the first comprehensive inventory of phosphatases in oomycetes and identifies an important phosphatase within the expanded serine/threonine phosphatase group in oomycetes.

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Section: Discussionmentioning

confidence: 99%

Mining oomycete proteomes for phosphatome leads to the identification of specific expanded phosphatases in oomycetes

Qiu,

Sun,

et al. 2024

Molecular Plant Pathology

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“…Although Ssu72 was discovered in budding yeast, similar proteins have been reported in multiple eukaryotes on the basis of sequence homology (Pappas and Hampsey, 2000;St-Pierre et al, 2005;Liu et al, 2021). Orthologs of Ssu72 have been identified in mammals including humans and mice, fungi like Schizosaccharomyces pombe, Kluyveromyces lactis, Aspergillus flavus and Cryptococcus neoformans, insects like Drosophila melanogaster, plants like Arabidopsis thaliana and Caenorhabditis elegans to name a few (Pappas and Hampsey, 2000;Chen et al, 2015;Park et al, 2023).…”

Section: Evolutionary Implicationsmentioning

confidence: 96%

Ssu72: a versatile protein with functions in transcription and beyond

Fidler,

Dwyer,

Ansari

2024

Front. Mol. Biosci.

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Eukaryotic transcription is a complex process involving a vast network of protein and RNA factors that influence gene expression. The main player in transcription is the RNA polymerase that synthesizes the RNA from the DNA template. RNA polymerase II (RNAPII) transcribes all protein coding genes and some noncoding RNAs in eukaryotic cells. The polymerase is aided by interacting partners that shuttle it along the gene for initiation, elongation and termination of transcription. One of the many factors that assist RNAPII in transcription of genes is Ssu72. It is a carboxy-terminal-domain (CTD)-phosphatase that plays pleiotropic roles in the transcription cycle. It is essential for cell viability in Saccharomyces cerevisiae, the organism in which it was discovered. The homologues of Ssu72 have been identified in humans, mice, plants, flies, and fungi thereby suggesting the evolutionarily conserved nature of the protein. Recent studies have implicated the factor beyond the confines of transcription in homeostasis and diseases.

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“…The length of its repeat sequence differs between species, ranging from 26 repeats in budding yeast to 52 repeats in mammals. The sequence of the CTD undergoes dynamic structural changes through multiple post-translational modifications, including phosphorylation/dephosphorylation, cis–trans Pro isomerization, and O -GlcNAcylation [ 17 , 18 , 19 , 20 ]. Flexible interactions between the CTD and diverse factors at appropriate stages of the transcription process are critical for the regulation of multiple steps of the transcription cycle.…”

Section: Mechanism By Which Ssu72 Phosphatase Regulates Gene Exprementioning

confidence: 99%

Ssu72 Dual-Specific Protein Phosphatase: From Gene to Diseases

Hwang

Kim

Lee

2021

IJMS

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More than 70% of eukaryotic proteins are regulated by phosphorylation. However, the mechanism of dephosphorylation that counteracts phosphorylation is less studied. Phosphatases are classified into 104 distinct groups based on substrate-specific features and the sequence homologies in their catalytic domains. Among them, dual-specificity phosphatases (DUSPs) that dephosphorylate both phosphoserine/threonine and phosphotyrosine are important for cellular homeostasis. Ssu72 is a newly studied phosphatase with dual specificity that can dephosphorylate both phosphoserine/threonine and phosphotyrosine. It is important for cell-growth signaling, metabolism, and immune activation. Ssu72 was initially identified as a phosphatase for the Ser5 and Ser7 residues of the C-terminal domain of RNA polymerase II. It prefers the cis configuration of the serine–proline motif within its substrate and regulates Pin1, different from other phosphatases. It has recently been reported that Ssu72 can regulate sister chromatid cohesion and the separation of duplicated chromosomes during the cell cycle. Furthermore, Ssu72 appears to be involved in the regulation of T cell receptor signaling, telomere regulation, and even hepatocyte homeostasis in response to a variety of stress and damage signals. In this review, we aim to summarize various functions of the Ssu72 phosphatase, their implications in diseases, and potential therapeutic indications.

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Diverse and conserved roles of the protein Ssu72 in eukaryotes: from yeast to higher organisms

Cited by 6 publications

References 94 publications

Mining oomycete proteomes for phosphatome leads to the identification of specific expanded phosphatases in oomycetes

Mining oomycete proteomes for phosphatome leads to the identification of specific expanded phosphatases in oomycetes

Ssu72: a versatile protein with functions in transcription and beyond

Ssu72 Dual-Specific Protein Phosphatase: From Gene to Diseases

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