Evidence map›Paper›PMID 34642328›Full record

ArticleNature communications2021

Structural and functional consequences of NEDD8 phosphorylation.

Katrin Stuber, Tobias Schneider, Jill Werner, Michael Kovermann, Andreas Marx, Martin Scheffner

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 16% of its field
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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Protein neddylation and its role in health and diseases.Signal transduction and targeted therapy · 2024
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. PermaPhosbioRxiv : the preprint server for biology · 2021
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Katrin StuberDept. of Biology, University of Konstanz, Konstanz, Germany.
Tobias SchneiderDept. of Chemistry, University of Konstanz, Konstanz, Germany.
Jill WernerDept. of Biology, University of Konstanz, Konstanz, Germany.ORCID http://orcid.org/0000-0002-8088-7814
Michael KovermannDept. of Chemistry, University of Konstanz, Konstanz, Germany. michael.kovermann@uni-konstanz.de.ORCID http://orcid.org/0000-0002-3357-9843
Andreas MarxDept. of Chemistry, University of Konstanz, Konstanz, Germany. andreas.marx@uni-konstanz.de.ORCID http://orcid.org/0000-0002-6471-3689
Martin ScheffnerDept. of Biology, University of Konstanz, Konstanz, Germany. martin.scheffner@uni-konstanz.de.ORCID http://orcid.org/0000-0003-2229-0128
University of Konstanz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitin (Ub) and Ub-like proteins (Ubls) such as NEDD8 are best known for their function as covalent modifiers of other proteins but they are also themselves subject to post-translational modifications including phosphorylation. While functions of phosphorylated Ub (pUb) have been characterized, the consequences of Ubl phosphorylation remain unclear. Here we report that NEDD8 can be phosphorylated at S65 - the same site as Ub - and that S65 phosphorylation affects the structural dynamics of NEDD8 and Ub in a similar manner. While both pUb and phosphorylated NEDD8 (pNEDD8) can allosterically activate the Ub ligase Parkin, they have different protein interactomes that in turn are distinct from those of unmodified Ub and NEDD8. Among the preferential pNEDD8 interactors are HSP70 family members and we show that pNEDD8 stimulates HSP70 ATPase activity more pronouncedly than unmodified NEDD8. Our findings highlight the general importance of Ub/NEDD8 phosphorylation and support the notion that the function of pUb/pNEDD8 does not require their covalent attachment to other proteins.

Indexed as

Protein Processing, Post-TranslationalAllosteric RegulationAmino Acid SequenceCloning, MolecularEscherichia coliGene ExpressionGenetic VectorsHEK293 CellsHSP70 Heat-Shock ProteinsHumansKineticsNEDD8 ProteinPhosphorylationProtein BindingProtein Interaction MappingRecombinant ProteinsHSP70 Heat-Shock ProteinsNEDD8 ProteinNEDD8 protein, humanRecombinant ProteinsUbiquitin

Identifiers

PMID34642328
PMCPMC9020517
OpenAlexW3202310628

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.