Interaction modulation through arrays of clustered methyl-arginine protein modifications

Woodsmith, Jonathan; Casado‐Medrano, Victoria; Benlasfer, Nouhad; Eccles, Rebecca L; Hutten, Saskia; Heine, Christian L.; Thormann, Verena; Abou‐Ajram, Claudia; Rocks, Oliver; Dormann, Dorothee; Stelzl, Ulrich

doi:10.26508/lsa.201800178

Cited by 11 publications

(7 citation statements)

References 55 publications

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“…We show that ArgMet NMR enables detection of methylation patterns in purified proteins incubated with PRMT1. Methylation by PRMTs in the human proteome occurs preferentially (but not exclusively) within glycine-arginine-rich and proline-glycine-methionine-rich regions ( Cheng et al., 2007 ; Thandapani et al., 2013 ; Woodsmith et al., 2018 ), but specific consensus sequences targeted by most of the human PRMTs remain to be identified. Our approach provides a toolbox for fast and label-free screening for PRMT selectivity in purified proteins/peptides, complementary to peptide arrays ( Kusevic et al., 2016 ) and mass spectrometry ( Uhlmann et al., 2012 ).…”

Section: Discussionmentioning

confidence: 99%

Global analysis of protein arginine methylation

Zhang

Kerbl-Knapp

Colman

et al. 2021

Cell Reports Methods

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Section: Discussionmentioning

confidence: 99%

Global analysis of protein arginine methylation

Zhang

Kerbl-Knapp

Colman

et al. 2021

Cell Reports Methods

Self Cite

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“…Interestingly, many SARS-CoV-2 Ninteracting proteins (27 of 119, Figure 2B) contained multiple RGG/RG motifs including DEAD/DExH family of RNA helicases DDX21, DDX54, DHX30, DHX57, and heterogeneous nuclear ribonucleoproteins hnRNPA1, A3, D, DL, G (RBMX), R, U, UL1 and UL2 (Table 1). Many of these N-interacting proteins, such as G3BP1 [50], FAM98A [51], FXR1 [52], hnRNPA1 [53], hnRNPUL1 [54], SYNCRIP [55], ILF3 [56], and SERBP1 [57] are known PRMT1 substrates. N protein-interactome changed significantly by two proteins with MS023 treatment.…”

Section: The Sars-cov-2 N Interactome Defines a Complex Of Rgg/rg Proteins And Prmt1mentioning

confidence: 99%

Arginine methylation of SARS-Cov-2 nucleocapsid protein regulates RNA binding, its ability to suppress stress granule formation, and viral replication

Cai

Wang

et al. 2021

Journal of Biological Chemistry

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This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

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“…hnRNP R is involved in axonal RNA transport and processing, the expression of immunity factors, and transcription and degradation process of c-fos mRNA [11, 16, 23, 49], whilst hnRNP Q, also known as SYNCRIP, is implicated in the maintenance of circadian rhythms and be involved in the regulation of mRNAs responsible for neuronal morphogenesis [10, 25, 31]. Both proteins are known to interact with the survival motor neuron (SMN) protein [1] and be involved in pre-mRNA splicing as components of the spliceosome [9, 38, 51, 56]. Recent analysis of these proteins in a cellular model has found them to be important regulators of neuronal homeostasis and indicated that their disruption could impair distinct pathways in the central nervous system axis [8].…”

Section: Discussionmentioning

confidence: 99%

Heterogeneous nuclear ribonucleoproteins R and Q accumulate in pathological inclusions in FTLD-FUS

Gittings

Foti

Benson

et al. 2019

acta neuropathol commun

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Frontotemporal lobar degeneration (FTLD) is pathologically subdivided based on the presence of particular pathological proteins that are identified in inclusion bodies observed post-mortem. The FTLD-FUS subgroup is defined by the presence of the fused in sarcoma protein (FUS) in pathological inclusions. FUS is a heterogeneous nuclear ribonucleoprotein (hnRNP) protein and a member of the FET (FUS, EWS, TAF15) protein family. It shuttles between the nucleus and cytoplasm, and has been implicated in many cellular functions including translation, splicing, and RNA transport. EWS, TAF15 and the nuclear import receptor transportin have been shown to co-accumulate with FUS in neuronal inclusions specifically in FTLD-FUS, with transportin-positive inclusions most frequently observed. Here, we report the identification of hnRNP R and hnRNP Q in neuronal cytoplasmic and intranuclear inclusions in the frontal cortex and hippocampus of FTLD-FUS patients, as frequently as transportin. hnRNP R and hnRNP Q were not found in the characteristic pathological inclusions observed in FTLD-TDP (subtypes A-C). Additionally, we studied the expression of hnRNP R in the frontal and temporal cortices from patients with FTLD and found significantly increased expression of the heterogeneous nuclear ribonucleoprotein R in several FTLD disease groups. Our identification of the frequent presence of hnRNP R and hnRNP Q in FTLD-FUS inclusions suggests a potential role for these hnRNPs in FTLD-FUS pathogenesis and supports the role of dysfunctional RNA metabolism in FTLD.Electronic supplementary materialThe online version of this article (10.1186/s40478-019-0673-y) contains supplementary material, which is available to authorized users.

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Interaction modulation through arrays of clustered methyl-arginine protein modifications

Cited by 11 publications

References 55 publications

Global analysis of protein arginine methylation

Global analysis of protein arginine methylation

Arginine methylation of SARS-Cov-2 nucleocapsid protein regulates RNA binding, its ability to suppress stress granule formation, and viral replication

Heterogeneous nuclear ribonucleoproteins R and Q accumulate in pathological inclusions in FTLD-FUS

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