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. 2021 Jul 28;163(4):753–764. doi: 10.1097/j.pain.0000000000002421

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Copyright © 2021 The Author(s). Published by Wolters Kluwer Health, Inc. on behalf of the International Association for the Study of Pain.

This is an open access article distributed under the terms of the Creative Commons Attribution-Non Commercial-No Derivatives License 4.0 (CCBY-NC-ND), where it is permissible to download and share the work provided it is properly cited. The work cannot be changed in any way or used commercially without permission from the journal.

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Figure 7. — Proposed working model of PRMT7-mediated Na_V1.9 trafficking and cellular excitability. The PRMT7 C-terminal domain interacts with residues 563 to 566 of hLoop1 and methylates arginine 519 (R519 me) in this loop using S-adenosyl-L-methionine (AdoMet) as a methyl donor to produce S-adenosylhomocysteine (AdoHcy). Human Na_V1.9; R519 me is involved in the regulation of Na_V1.9 trafficking to the cell surface through an undefined mechanism. Consequently, altered cell surface expression of Na_V1.9 increases sodium current density, leading to hyperexcitability of DRG neurons. DRG, dorsal root ganglion; PRMT7, protein arginine methyltransferase 7.