Protein arginine methylation: Cellular functions and methods of analysis

Pahlich, Steffen; Zakaryan, Rouzanna P.; Gehring, Heinz

doi:10.1016/j.bbapap.2006.08.008

Cited by 217 publications

(247 citation statements)

References 136 publications

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“…Methylation of ICP27 was reduced by about 50 to 70% in the AdOx-treated samples (Fig. 1A, bottom panels), which is consistent with results reported previously (24).…”

supporting

confidence: 81%

“…Protein-arginine methylation is catalyzed by a family of enzymes known as protein arginine methyltransferases (PRMT), of which at least nine members have previously been identified (1). PRMT1 is the main methyltransferase in human cells (24), and this enzyme usually recognizes arginines within a glycine-argininerich region, which is a motif that is present in many RNA and DNA binding proteins. Arginine methylation has been shown to be important for modulating protein-protein interactions (3,14,21,32,33), for regulating export of shuttling proteins (11,20,28,35), and for regulating nuclear importation of several regulatory proteins in mammalian cells (9,15,25,29).…”

mentioning

confidence: 99%

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Arginine Methylation of the RGG Box Does Not Appear To Regulate ICP27 Import during Herpes Simplex Virus Infection

Souki

Hernandez

Sandri‐Goldin

2011

J Virol

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Arginine methylation can regulate protein import and export and can modulate protein interactions. Herpes simplex virus 1 (HSV-1) ICP27 is a shuttling protein involved in viral mRNA export. We previously reported that ICP27 is methylated on three arginines within its RGG box and that arginine methylation regulates ICP27 export and its interaction with SRPK1 and Aly/REF. Here, we report that ICP27 was efficiently imported into the nucleus when hypomethylated as determined by Fluorescence Recovery After Photobleaching (FRAP). Furthermore, coimmunoprecipitation of ICP27 with ␤-importin was not significantly affected by ICP27 hypomethylation. Thus, ICP27 import does not appear to be regulated by arginine methylation.

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“…Methylation of ICP27 was reduced by about 50 to 70% in the AdOx-treated samples (Fig. 1A, bottom panels), which is consistent with results reported previously (24).…”

supporting

confidence: 81%

mentioning

confidence: 99%

Arginine Methylation of the RGG Box Does Not Appear To Regulate ICP27 Import during Herpes Simplex Virus Infection

Souki

Hernandez

Sandri‐Goldin

2011

J Virol

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“…PRMT5 methylates components of the transcription complex, including the transcription elongation factor SPT5, altering its interaction with RNA polymerase II and potentially affecting global transcription rates (47). PRMT5 also interacts with Switch/Sucrose nonfermentable (SWI/SNF) chromatin remodeling complexes to act as a transcriptional coactivator (46).…”

Section: Discussionmentioning

confidence: 99%

Type II protein arginine methyltransferase 5 (PRMT5) is required for circadian period determination in Arabidopsis thaliana

Hong

Song

Lutz

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

122

118

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Posttranslational modification is an important element in circadian clock function from cyanobacteria through plants and mammals. For example, a number of key clock components are phosphorylated and thereby marked for subsequent ubiquitination and degradation. Through forward genetic analysis we demonstrate that protein arginine methyltransferase 5 (PRMT5; At4g31120) is a critical determinant of circadian period in Arabidopsis. PRMT5 is coregulated with a set of 1,253 genes that shows alterations in phase of expression in response to entrainment to thermocycles versus photocycles in constant temperature. PRMT5 encodes a type II protein arginine methyltransferase that catalyzes the symmetric dimethylation of arginine residues (Rsme2). Rsme2 modification has been observed in many taxa, and targets include histones, components of the transcription complex, and components of the spliceosome. Neither arginine methylation nor PRMT5 has been implicated previously in circadian clock function, but the period lengthening associated with mutational disruption of prmt5 indicates that Rsme2 is a decoration important for the Arabidopsis clock and possibly for clocks in general.circadian rhythms | circadian clock | luciferase

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“…25,26 Finally, arginine methylation reduces the interaction of hnRNP K with the tyrosine kinase c-Src, leading to inhibition of c-Src activation, 27 based on co-IP studies from cells, whereas methylated arginines in Sm proteins are ligands for binding of the Tudor family of proteins. 28 Arginine methylation could affect direct interactions of RGG motif proteins with RNAs or proteins by either the methyl group increasing the hydrophobicity of arginine residue to promote stacking interactions with mRNA, 29,30 reducing the number of hydrogen bonds the arginine residue can form, or by creating a steric hindrance for a specific interaction.…”

Section: Mrnps Poised For Re-entry To Translationmentioning

confidence: 99%