CRMP2 protein SUMOylation modulates NaV1.7 channel trafficking.

@article{Dustrude2013CRMP2PS,
  title={CRMP2 protein SUMOylation modulates NaV1.7 channel trafficking.},
  author={Erik Thomas Dustrude and Sarah M Wilson and Weina Ju and Yucheng Xiao and Rajesh Khanna},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 34},
  pages={24316-31}
}
Voltage-gated sodium channel (NaV) trafficking is incompletely understood. Post-translational modifications of NaVs and/or auxiliary subunits and protein-protein interactions have been posited as NaV-trafficking mechanisms. Here, we tested if modification of the axonal collapsin response mediator protein 2 (CRMP2) by a small ubiquitin-like modifier (SUMO) could affect NaV trafficking; CRMP2 alters the extent of NaV slow inactivation conferred by the anti-epileptic (R)-lacosamide, implying NaV… CONTINUE READING

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Hierarchical CRMP 2 posttranslational modifications control NaV 1 . 7 function

Erik T. Dustrudea, Aubin Moutala, +3 authors Rajesh Khannaa
2016
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Sodium Channel Trafficking.

Handbook of experimental pharmacology • 2018
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Hierarchical CRMP2 posttranslational modifications control NaV1.7 function.

Proceedings of the National Academy of Sciences of the United States of America • 2016

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