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Free keywords:
Arginine/*metabolism
HeLa Cells
Humans
Methylation
Nerve Tissue Proteins/*metabolism
Protein Transport
Protein-Arginine N-Methyltransferases/*metabolism
Repressor Proteins/*metabolism
Tumor Cells, Cultured
Asymmetric arginine dimethylation
Ataxin-2-like
Protein arginine methyltransferase
Splicing speckles
Stress granules
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.
