Evidence map›Paper›PMID 28277940›Full record

ArticleChannels (Austin, Tex.)2017

A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function.

Erik Thomas Dustrude, Samantha Perez-Miller, Liberty François-Moutal, Aubin Moutal, May Khanna, Rajesh Khanna

Abstract read
In one paragraph

Article in Channels (Austin, Tex.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

32 citing papers in PubMed.

  1. Article
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  9. Review
  10. A peptidomimetic modulator of the CaProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Identification and targeting of a unique NaProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Review
  13. Article
  14. Article
  15. Non-SUMOylated CRMP2 decreases NaMolecular brain · 2021
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Erik Thomas Dustrudea Department of Pharmacology, College of Medicine , University of Arizona , Tucson , AZ , USA.ORCID http://orcid.org/0000-0002-1753-8603
Samantha Perez-Millera Department of Pharmacology, College of Medicine , University of Arizona , Tucson , AZ , USA.ORCID http://orcid.org/0000-0002-9034-3693
Liberty François-Moutala Department of Pharmacology, College of Medicine , University of Arizona , Tucson , AZ , USA.ORCID http://orcid.org/0000-0003-1277-660X
Aubin Moutala Department of Pharmacology, College of Medicine , University of Arizona , Tucson , AZ , USA.ORCID http://orcid.org/0000-0003-4268-1206
May Khannaa Department of Pharmacology, College of Medicine , University of Arizona , Tucson , AZ , USA.ORCID http://orcid.org/0000-0002-9989-6374
Rajesh Khannaa Department of Pharmacology, College of Medicine , University of Arizona , Tucson , AZ , USA.ORCID http://orcid.org/0000-0002-9066-2969

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The neuronal collapsin response mediator protein 2 (CRMP2) undergoes several posttranslational modifications that codify its functions. Most recently, CRMP2 SUMOylation (addition of small ubiquitin like modifier (SUMO)) was identified as a key regulatory step within a modification program that codes for CRMP2 interaction with, and trafficking of, voltage-gated sodium channel NaV1.7. In this paper, we illustrate the utility of combining sequence alignment within protein families with structural analysis to identify, from several putative SUMOylation sites, those that are most likely to be biologically relevant. Co-opting this principle to CRMP2, we demonstrate that, of 3 sites predicted to be SUMOylated in CRMP2, only the lysine 374 site is a SUMOylation client. A reduction in NaV1.7 currents was the corollary of the loss of CRMP2 SUMOylation at this site. A 1.78-Å-resolution crystal structure of mouse CRMP2 was solved using X-ray crystallography, revealing lysine 374 as buried within the CRMP2 tetramer interface but exposed in the monomer. Since CRMP2 SUMOylation is dependent on phosphorylation, we postulate that this state forces CRMP2 toward a monomer, exposing the SUMO site and consequently, resulting in constitutive regulation of NaV1.7.

Indexed as

AnimalsCatalytic DomainCell LineCrystallography, X-RayIntercellular Signaling Peptides and ProteinsMiceModels, MolecularNAV1.7 Voltage-Gated Sodium ChannelNerve Tissue ProteinsPhosphorylationProtein ConformationProtein TransportSmall Ubiquitin-Related Modifier ProteinsSumoylationcollapsin response mediator protein-2Intercellular Signaling Peptides and ProteinsNAV1.7 Voltage-Gated Sodium ChannelNerve Tissue ProteinsSmall Ubiquitin-Related Modifier ProteinsCRMP2NaV1.7post-translational modificationsSUMOylationtraffickingX-ray crystallography

Identifiers

PMID28277940
PMCPMC5555265

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.