Deciphering the molecular mechanisms underlying the plasma membrane targeting of PRMT8
Autor: | Yong-Woo Jun, Jin-A Lee, Sang-Won Park, Ha-Eun Choi, Deok-Jin Jang |
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Rok vydání: | 2019 |
Předmět: |
Protein-Arginine N-Methyltransferases
Myristoylation Protein Sorting Signals Mitochondrion Biochemistry Mice 03 medical and health sciences Protein Domains Oligomerization Animals Humans Molecular Biology Protein arginine methyltransferase 8 Regulation of gene expression chemistry.chemical_classification 0303 health sciences Chemistry Cell Membrane 030302 biochemistry & molecular biology Membrane Proteins Articles General Medicine Cell biology Amino acid Cytosol HEK293 Cells Membrane Signal transduction Dimerization PRMT8 Plasma membrane |
Zdroj: | BMB Reports |
ISSN: | 1976-670X |
DOI: | 10.5483/bmbrep.2019.52.10.272 |
Popis: | 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 Cterminal 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. [BMB Reports 2019; 52(10): 601-606]. |
Databáze: | OpenAIRE |
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