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Deciphering the molecular mechanisms underlying the plasma membrane targeting of PRMT8
Sang-Won Park1, Yong-Woo Jun2, Ha-Eun Choi3, Jin-A Lee3, Deok-Jin Jang1,2,*
1Department of Applied Biology and 2Department of Ecological Science, College of Ecology and Environment, Kyungpook National University,
3Department of Biological Science and Biotechnology, College of Life Science and Nano Technology, Hannam University
Arginine methylation plays crucial roles in many cellular functions including signal transduction, RNA transcription, and regulation of gene expression. Protein arginine methyltransferase 8 (PRMT8), a unique brain-specific protein, is localized to the plasma membrane. However, the detailed molecular mechanisms underlying PRMT8 plasma membrane targeting remain unclear. Here, we demonstrate that the N-terminal 20 amino acids of PRMT8 are sufficient for plasma membrane localization and that oligomerization enhances membrane localization. The basic amino acids, combined with myristoylation within the N-terminal 20 amino acids of PRMT8, are critical for plasma membrane targeting. We also found that substituting Gly-2 with Ala [PRMT8(G2A)] or Cys-9 with Ser [PRMT8(C9S)] induces the formation of punctate structures in the cytosol or patch-like plasma membrane localization, respectively. Impairment of PRMT8 oligomerization/dimerization by C-terminal deletion induces PRMT8 mis-localization to the mitochondria, prevents the formation of punctate structures by PRMT8(G2A), and inhibits PRMT8(C9S) patch-like plasma membrane localization. Overall, these results suggest that oligomerization/dimerization plays several roles in inducing the efficient and specific plasma membrane localization of PRMT8.
Abstract, Accepted Manuscript(in press) [Submitted on November 29, 2018, Accepted on January 16, 2019]
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