Protein arginine methylation of SERBP1 by protein arginine methyltransferase 1 affects cytoplasmic/nuclear distribution

Lee, Yu–Jen; Hsieh, Wan-Yu; Chen, Lingyun; Li, Chuan

doi:10.1002/jcb.24151

Cited by 42 publications

(60 citation statements)

References 22 publications

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“…In our previous study, we observed the interaction of SERBP1 with asymmetric N G ,N G -dimethylarginine-containing proteins by co-immunoprecipitation [2]. As many SGincorporated proteins are RNA-binding proteins and may be arginine-methylated [10], we analyzed whether SERBP1 interacts with these proteins.…”

Section: Resultsmentioning

confidence: 98%

“…We have shown that SERBP1 is arginine-methylated in the central RG and C-terminal RGG regions [2]. Protein arginine methylation of some SG-incorporated RNA-binding proteins has been shown to be critical for their cellular distribution, and may further affect their sorting to SGs [10].…”

Section: Discussionmentioning

confidence: 94%

“…These results indicate that SERBP1 interacts with some RNA-binding proteins through RNA under normal conditions without stress. The central RG segment, which is important for SERBP1 nuclear localization [2], is not required or sufficient for the interaction, because RG deletion proteins interacted with hnRNPA1 and FMRP, but only very weak interaction was detected for the central segment (151-270) containing the RG sequences (Fig. S1).…”

Section: Resultsmentioning

confidence: 99%

“…It contains a central arginine and glycine (RG)-rich domain and a C-terminal arginine-and glycine-rich motif (RGG box) domain that are methylated by protein arginine N-methyltransferases (PRMTs). We have demonstrated protein arginine methylation in these regions of SERBP1, and the effect of methylation on the subcellular localization of SERBP1 [2]. Hypomethylation by the treatment with the indirect methyltransferase inhibitor adenosine periodate (AdOx) or PRMT1 siRNA results in an increased nuclear distribution of SERBP compared with the otherwise pre-dominant cytoplasmic localization.…”

Section: Introductionmentioning

confidence: 93%

“…Analyzes of various deletions indicated that the central RG region is important for the nuclear localization, while both the N-and C-termini are required for nuclear export to the cytoplasm. Low methylation of the C-terminal RGG region also favors nuclear localization [2].…”

Section: Introductionmentioning

confidence: 99%

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Localization of SERBP1 in stress granules and nucleoli

et al. 2013

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SERPINE1 mRNA-binding protein 1 (SERBP1) is an arginine-methylated RNA-binding protein whose modification affects protein interaction and intracellular localization. In the present study, we show that, under normal growth conditions without stress, SERBP1 interacts with arginine-methylated and stress granule-associated proteins such as heterogeneous nuclear ribonucleoprotein A1, fragile X mental retardation protein and fragile X mental retardation syndrome-related protein 1 in an RNA-dependent manner. We also show that, after arsenite treatment, a proportion of full-length SERBP1 protein co-localizes with the typical stress granule marker T-cell intracellular antigen-1 in the cytoplasmic stress granules. Truncated SERBP1 with an Nterminal, central RG or C-terminal deletion, or single-domain segments comprising the N-terminal, central or C-terminal region, were recruited to stress granules upon arsenite treatment but with reduced efficiency. In addition, upon arsenite treatment, the localization of SERBP1 changed from a diffuse cytoplasmic localization to nuclear-dominant (concentrated in the nucleolus) A similar distribution was observed when cells were treated with the methylation inhibitor adenosine periodate, and was also detected for N-or C-terminal domain deletions and all three single-domain fragments even without stress induction. We further demonstrate that adenosine periodate treatment delays the association/dissociation of SERBP1 with stress granules. Hypomethylation retains SERBP1 in the nucleus/nucleolus regardless of arsenite treatment. Our study indicates that arginine methylation is correlated with recruitment of SERBP to stress granules and nucleoli and its retention therein. To our knowledge, this is the first report of an RNA-binding protein that is shifted simultaneously to cytoplasmic stress granules and nucleoli, two ribonucleoprotein-enriched subcellular compartments, upon stress.

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Section: Resultsmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 94%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

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Localization of SERBP1 in stress granules and nucleoli

et al. 2013

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Emerging Implications of Phase Separation in Cancer

et al. 2022

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In eukaryotic cells, biological activities are executed in distinct cellular compartments or organelles. Canonical organelles with membrane‐bound structures are well understood. Cells also inherently contain versatile membrane‐less organelles (MLOs) that feature liquid or gel‐like bodies. A biophysical process termed liquid–liquid phase separation (LLPS) elucidates how MLOs form through dynamic biomolecule assembly. LLPS‐related molecules often have multivalency, which is essential for low‐affinity inter‐ or intra‐molecule interactions to trigger phase separation. Accumulating evidence shows that LLPS concentrates and organizes desired molecules or segregates unneeded molecules in cells. Thus, MLOs have tunable functional specificity in response to environmental stimuli and metabolic processes. Aberrant LLPS is widely associated with several hallmarks of cancer, including sustained proliferative signaling, growth suppressor evasion, cell death resistance, telomere maintenance, DNA damage repair, etc. Insights into the molecular mechanisms of LLPS provide new insights into cancer therapeutics. Here, the current understanding of the emerging concepts of LLPS and its involvement in cancer are comprehensively reviewed.

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The mRNA‐binding protein Serbp1 as an auxiliary protein associated with mammalian cytoplasmic ribosomes

Muto

Sugihara

Shibakawa

et al. 2018

Cell Biochemistry & Function

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In mammalian cells, the final protein output of their genetic program is determined not only by controlling transcription but also by regulating the posttranscriptional events. Although mRNA-binding proteins and the cytoplasmic ribosome have long been recognized as central players in the posttranscriptional regulation, their physical and functional interactions are still far from a complete understanding. Here, we describe the intracellular localization of Serbp1, an mRNA-binding protein, and the inclusion of this protein in actively translating ribosomes in normal and cancer cells. These findings shed a new light into molecular mechanisms underlying Serbp1 action in translational gene regulation and tumour progression.

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Protein arginine methylation of SERBP1 by protein arginine methyltransferase 1 affects cytoplasmic/nuclear distribution

Cited by 42 publications

References 22 publications

Localization of SERBP1 in stress granules and nucleoli

Localization of SERBP1 in stress granules and nucleoli

Emerging Implications of Phase Separation in Cancer

The mRNA‐binding protein Serbp1 as an auxiliary protein associated with mammalian cytoplasmic ribosomes

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