Analysis of the Physiological Activities of Scd6 through Its Interaction with Hmt1

Lien, Pham Thi Kim; Izumikawa, Keiichi; Muroi, Kei; Irie, Kaoru; Suda, Yuji; Irie, Kenji

doi:10.1371/journal.pone.0164773

Cited by 12 publications

(14 citation statements)

References 38 publications

(66 reference statements)

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“…This is consistent with the role of Hmt1 as a predominant methyltransferases in yeast. It is also consistent with the role of Hmt1 in methylating RNA-binding proteins in general including another RGG-motif protein Scd6 [25,29]. Our current results are based on usage of antibody specific for mono-methyl arginine.…”

Section: Discussionsupporting

confidence: 89%

Arginine methylation augments Sbp1 function in translation repression and decapping

et al. 2019

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The fate of messenger RNA in cytoplasm plays a crucial role in various cellular processes. However, the mechanisms that decide whether mRNA will be translated, degraded or stored remain unclear. Single stranded nucleic acid binding protein (Sbp1), an Arginine‐Glycine‐Glycine (RGG‐motif) protein, is known to promote transition of mRNA into a repressed state by binding eukaryotic translation initiation factor 4G1 (eIF4G1) and to promote mRNA decapping, perhaps by modulation of Dcp1/2 activity. Sbp1 is known to be methylated on arginine residues in RGG‐motif; however, the functional relevance of this modification in vivo remains unknown. Here, we report that Sbp1 is arginine‐methylated in an hnRNP methyl transferase (Hmt1)‐dependent manner and that methylation is enhanced upon glucose deprivation. Characterization of an arginine‐methylation‐defective (AMD) mutant provided evidence that methylation affects Sbp1 function in vivo. The AMD mutant is compromised in causing growth defect upon overexpression, and the mutant is defective in both localizing to and inducing granule formation. Importantly, the Sbp1‐eIF4G1 interaction is compromised both for the AMD mutant and in the absence of Hmt1. Upon overexpression, wild‐type Sbp1 increases localization of another RGG motif containing protein, Scd6 (suppressor of clathrin deficiency) to granules; however, this property of Sbp1 is compromised in the AMD mutant and in the absence of Hmt1, indicating that Sbp1 repression activity could involve other RGG‐motif translation repressors. Additionally, the AMD mutant fails to increase localization of the decapping activator DEAD box helicase homolog to foci and fails to rescue the decapping defect of a dcp1‐2Δski8 strain, highlighting the role of Sbp1 methylation in decapping. Taken together, these results suggest that arginine methylation modulates Sbp1 role in mRNA fate determination.

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Section: Discussionsupporting

confidence: 89%

Arginine methylation augments Sbp1 function in translation repression and decapping

et al. 2019

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“…SCD6 function is modulated by HMT1/PRMT1 in yeast and mammals, and in T. brucei SCD6 strongly interacts with Tb PRMT1 and is methylated on three arginine residues (35, 58 – 61). Unlike SCD6 in other organisms, Tb SCD6 does not seem to be necessary for formation of mRNA-containing granules under starvation conditions (35).…”

Section: Discussionmentioning

confidence: 99%

Trypanosoma brucei PRMT1 Is a Nucleic Acid Binding Protein with a Role in Energy Metabolism and the Starvation Stress Response

Kafková

Pazzo

et al. 2018

mBio

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Trypanosoma brucei infection causes human African trypanosomiasis, also known as sleeping sickness, a disease with a nearly 100% fatality rate when untreated. Current drugs are expensive, toxic, and highly impractical to administer, prompting the community to explore various unique aspects of T. brucei biology in search of better treatments. In this study, we identified the protein arginine methyltransferase (PRMT), TbPRMT1, as a factor that modulates numerous aspects of T. brucei biology. These include glycolysis and life cycle progression signaling, both of which are being intensely researched toward identification of potential drug targets. Our data will aid research in those fields. Furthermore, we demonstrate for the first time a direct association of a PRMT with nucleic acids, a finding we believe could translate to other organisms, including humans, thereby impacting research in fields as distant as human cancer biology and immune response modulation.

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“…Several phenotypes related to Scd6 have been reported. First, overexpression of Scd6 induces P-bodies and stress granules under nonstress conditions ( Lien et al, 2016 ; Rajyaguru et al, 2012 ). Second, Scd6 stimulates the formation of P-bodies under glucose starvation conditions ( Rajyaguru et al, 2012 ).…”

Section: Resultsmentioning

confidence: 99%

Analysis of the TORC1 interactome reveals a spatially distinct function of TORC1 in mRNP complexes

Chang

Lim

Huh

2021

Journal of Cell Biology

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The target of rapamycin complex 1 (TORC1) is mainly localized to the vacuolar membrane and regulates eukaryotic cell growth in response to nutrient availability. To obtain deeper insights into the functional roles of TORC1, we performed a genome-wide analysis of the TORC1 interactome in yeast using the bimolecular fluorescence complementation (BiFC) assay. We found that while most of the BiFC signals are observed at the vacuolar membrane, a fraction of them are detected at cytoplasmic messenger ribonucleoprotein (mRNP) granules. Moreover, mRNA-binding proteins are enriched in the TORC1 interactome, suggesting a functional relationship between TORC1 and mRNA metabolism. We show that a portion of TORC1 is consistently associated with mRNP complexes and interacts with a specific subset of mRNAs. We also demonstrate that TORC1 directly targets a translational repressor Scd6 and that the activity of Scd6 is inhibited by TORC1-dependent phosphorylation. Collectively, our data suggest that TORC1 plays a novel role in posttranscriptional regulation by controlling the activity of Scd6.

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Analysis of the Physiological Activities of Scd6 through Its Interaction with Hmt1

Cited by 12 publications

References 38 publications

Arginine methylation augments Sbp1 function in translation repression and decapping

Arginine methylation augments Sbp1 function in translation repression and decapping

Trypanosoma brucei PRMT1 Is a Nucleic Acid Binding Protein with a Role in Energy Metabolism and the Starvation Stress Response

Analysis of the TORC1 interactome reveals a spatially distinct function of TORC1 in mRNP complexes

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