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Title: PRMT1-mediated arginine methylation controls ATXN2L localization

Abstract

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. - Highlights: • ATXN2L is asymmetrically dimethylated in vivo. • ATXN2L interacts with PRMT1 under normal and stress conditions. • PRMT1-mediated dimethylation of ATXN2L controls its nuclear localization. • ATXN2L localization to stress granules appears independent of its methylation state.

Authors:
; ; ;
Publication Date:
OSTI Identifier:
22462287
Resource Type:
Journal Article
Journal Name:
Experimental Cell Research
Additional Journal Information:
Journal Volume: 334; Journal Issue: 1; Other Information: Copyright (c) 2015 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0014-4827
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ARGININE; GLYCINE; IN VIVO; INHIBITION; MASS SPECTROSCOPY; METHYL TRANSFERASES; METHYLATION; MUTATIONS; SPLICING

Citation Formats

Kaehler, Christian, Guenther, Anika, Uhlich, Anja, and Krobitsch, Sylvia, E-mail: krobitsc@molgen.mpg.de. PRMT1-mediated arginine methylation controls ATXN2L localization. United States: N. p., 2015. Web. doi:10.1016/J.YEXCR.2015.02.022.
Kaehler, Christian, Guenther, Anika, Uhlich, Anja, & Krobitsch, Sylvia, E-mail: krobitsc@molgen.mpg.de. PRMT1-mediated arginine methylation controls ATXN2L localization. United States. doi:10.1016/J.YEXCR.2015.02.022.
Kaehler, Christian, Guenther, Anika, Uhlich, Anja, and Krobitsch, Sylvia, E-mail: krobitsc@molgen.mpg.de. Fri . "PRMT1-mediated arginine methylation controls ATXN2L localization". United States. doi:10.1016/J.YEXCR.2015.02.022.
@article{osti_22462287,
title = {PRMT1-mediated arginine methylation controls ATXN2L localization},
author = {Kaehler, Christian and Guenther, Anika and Uhlich, Anja and Krobitsch, Sylvia, E-mail: krobitsc@molgen.mpg.de},
abstractNote = {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. - Highlights: • ATXN2L is asymmetrically dimethylated in vivo. • ATXN2L interacts with PRMT1 under normal and stress conditions. • PRMT1-mediated dimethylation of ATXN2L controls its nuclear localization. • ATXN2L localization to stress granules appears independent of its methylation state.},
doi = {10.1016/J.YEXCR.2015.02.022},
journal = {Experimental Cell Research},
issn = {0014-4827},
number = 1,
volume = 334,
place = {United States},
year = {2015},
month = {5}
}