Protein Methylation and Stress Granules: Posttranslational Remodeler or Innocent Bystander?

Xie, Wen; Denman, Robert B.

doi:10.4061/2011/137459

Cited by 28 publications

(27 citation statements)

References 69 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. We first showed that hnRNPA1 co-immunoprecipitated with FLAGtagged SERBP1 (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…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]. We are interested in whether arginine methylation of SERBP1 is related to its SG localization.…”

Section: Discussionmentioning

confidence: 99%

“…Protein arginine methylation of the RG-rich motif of some RNA-binding proteins is critical for the subcellular distribution of the proteins, and may further affect their sorting to SGs [10]. For example, mutations in the proline/tyrosine nuclear localization signal of fused in sarcoma (FUS) impair the normal nuclear localization of FUS.…”

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: 99%

Section: Discussionmentioning

confidence: 99%

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Localization of SERBP1 in stress granules and nucleoli

et al. 2013

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“…However, we cannot discard the possibility that R-CRT, when present in SGs, regulate particular mRNA's encoding key antiapoptotic factors, thus either preventing its degradation necessary for the survival response or sequestering mRNA of proapoptotic proteins, inhibiting its translation. This is not the only case where a post-translational modification is involved in the assembly and remodeling of SGs (50). Other examples include the histone deacetylase 6 activity in SG formation (47), the inhibition of the ubiquitin proteasome system in SG disassembly (51), and the demonstration that SGs contain methylarginine proteins (52).…”

Section: Discussionmentioning

confidence: 99%

Arginylated Calreticulin at Plasma Membrane Increases Susceptibility of Cells to Apoptosis

Sambrooks¹,

Carpio²,

Hallak

2012

Journal of Biological Chemistry

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Background: Calreticulin retrotranslocated from the endoplasmic reticulum to the cytoplasm is post-translationally arginylated associates to stress granules following stress that decrease Ca 2ϩ . Results: Arginylated calreticulin reaches the plasma membrane as a response to stress. Conclusion: Arginylation confers to calreticulin a function as one of the preapoptotic signals of the cells. Significance: Arginylated calreticulin is a novel factor involved in stress-induced apoptosis.

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“…phosphorylation and glycosylation, of several SG components that are involved in the primary nucleation step play a significant role in the regulation of SG assembly/disassembly and function [20]. Moreover, several RNA-binding proteins, representing SG components, have been found to be asymmetrically and symmetrically dimethylated, suggesting that arginine modification is important in the process of SG formation as well [21]. The recruitment of FMRP to SGs is reduced under methylation inhibition [17].…”

Section: Introductionmentioning

confidence: 98%

PRMT1-mediated arginine methylation controls ATXN2L localization

Kaehler

Guenther

Uhlich

et al. 2015

Experimental Cell Research

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Arginine methylation is a posttranslational modification that is of importance in diverse cellular processes. Recent proteomic mass spectrometry studies reported arginine methylation of ataxin-2-like (ATXN2L), the paralog of ataxin-2, a protein that is implicated in the neurodegenerative disorder spinocerebellar ataxia type 2. Here, we investigated the methylation state of ATXN2L and its significance for ATXN2L localization. We first confirmed that ATXN2L is asymmetrically dimethylated in vivo, and observed that the nuclear localization of ATXN2L is altered under methylation inhibition. We further discovered that ATXN2L associates with the protein arginine-N-methyltransferase 1 (PRMT1). Finally, we showed that neither mutation of the arginine-glycine-rich motifs of ATXN2L nor methylation inhibition alters ATXN2L localization to stress granules, suggesting that methylation of ATXN2L is probably not mandatory.

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Protein Methylation and Stress Granules: Posttranslational Remodeler or Innocent Bystander?

Cited by 28 publications

References 69 publications

Localization of SERBP1 in stress granules and nucleoli

Localization of SERBP1 in stress granules and nucleoli

Arginylated Calreticulin at Plasma Membrane Increases Susceptibility of Cells to Apoptosis

PRMT1-mediated arginine methylation controls ATXN2L localization

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