Evidence map›Paper›PMID 26719334›Full record

ArticleThe Journal of biological chemistry2016

Structural and Mechanistic Insights into the Regulation of the Fundamental Rho Regulator RhoGDIα by Lysine Acetylation.

Nora Kuhlmann, Sarah Wroblowski, Philipp Knyphausen, Susanne de Boor, Julian Brenig, Anke Y Zienert, Katrin Meyer-Teschendorf, Gerrit J K Praefcke, Hendrik Nolte, Marcus Krüger and 5 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

34 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
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  8. A direct interaction between RhoGDIα/Tau alleviates hyperphosphorylation of Tau in Alzheimer's disease and vascular dementia.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2023
    Article
  9. Review
  10. Article
  11. Review
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  13. Electrostatic Forces Mediate the Specificity of RHO GTPase-GDI Interactions.International journal of molecular sciences · 2021
    Article
  14. Article
  15. Article
  16. Article
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  18. Review
  19. A Molecular Perspective on Sirtuin Activity.International journal of molecular sciences · 2020
    Review
  20. Critical review of non-histone human substrates of metal-dependent lysine deacetylases.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Review
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

15 authors at 2 institutions in 2 countries.

Nora KuhlmannFrom the Institute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-associated Diseases (CECAD), Joseph-Stelzmann-Strasse 26, University of Cologne, 50931 Cologne, Germany.
Sarah WroblowskiFrom the Institute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-associated Diseases (CECAD), Joseph-Stelzmann-Strasse 26, University of Cologne, 50931 Cologne, Germany.
Philipp KnyphausenFrom the Institute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-associated Diseases (CECAD), Joseph-Stelzmann-Strasse 26, University of Cologne, 50931 Cologne, Germany.
Susanne de BoorFrom the Institute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-associated Diseases (CECAD), Joseph-Stelzmann-Strasse 26, University of Cologne, 50931 Cologne, Germany.
Julian BrenigFrom the Institute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-associated Diseases (CECAD), Joseph-Stelzmann-Strasse 26, University of Cologne, 50931 Cologne, Germany.
Anke Y Zienertthe Institute for Genetics, Zülpicher Strasse 47a, University of Cologne, 50674 Cologne, Germany.
Katrin Meyer-Teschendorfthe Institute for Genetics, Zülpicher Strasse 47a, University of Cologne, 50674 Cologne, Germany.
Gerrit J K Praefckethe Institute for Genetics, Zülpicher Strasse 47a, University of Cologne, 50674 Cologne, Germany,; the Paul-Ehrlich-Institute, Paul-Ehrlich-Strasse 51-59, 63225 Langen, Germany, and.
Hendrik NolteFrom the Institute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-associated Diseases (CECAD), Joseph-Stelzmann-Strasse 26, University of Cologne, 50931 Cologne, Germany.
Marcus KrügerFrom the Institute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-associated Diseases (CECAD), Joseph-Stelzmann-Strasse 26, University of Cologne, 50931 Cologne, Germany.
Magdalena Schacherlthe Institute for Biochemistry, Zülpicher Strasse 47, University of Cologne, 50674 Cologne, Germany.
Ulrich Baumannthe Institute for Biochemistry, Zülpicher Strasse 47, University of Cologne, 50674 Cologne, Germany.
Leo C Jamesthe Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge CB2 0QH, United Kingdom.
Jason W Chinthe Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge CB2 0QH, United Kingdom.
Michael LammersFrom the Institute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-associated Diseases (CECAD), Joseph-Stelzmann-Strasse 26, University of Cologne, 50931 Cologne, Germany,. Electronic address: michael.lammers@uni-koeln.de.
University of Cologne · DEMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105181009Medical Research Council MC_U105181010
6 · The paper itself

Abstract

Rho proteins are small GTP/GDP-binding proteins primarily involved in cytoskeleton regulation. Their GTP/GDP cycle is often tightly connected to a membrane/cytosol cycle regulated by the Rho guanine nucleotide dissociation inhibitor α (RhoGDIα). RhoGDIα has been regarded as a housekeeping regulator essential to control homeostasis of Rho proteins. Recent proteomic screens showed that RhoGDIα is extensively lysine-acetylated. Here, we present the first comprehensive structural and mechanistic study to show how RhoGDIα function is regulated by lysine acetylation. We discover that lysine acetylation impairs Rho protein binding and increases guanine nucleotide exchange factor-catalyzed nucleotide exchange on RhoA, these two functions being prerequisites to constitute a bona fide GDI displacement factor. RhoGDIα acetylation interferes with Rho signaling, resulting in alteration of cellular filamentous actin. Finally, we discover that RhoGDIα is endogenously acetylated in mammalian cells, and we identify CBP, p300, and pCAF as RhoGDIα-acetyltransferases and Sirt2 and HDAC6 as specific deacetylases, showing the biological significance of this post-translational modification.

Indexed as

AcetylationActin CytoskeletonCrystallography, X-RayGuanine NucleotidesHEK293 CellsHeLa CellsHistone Deacetylase 6Histone DeacetylasesHumansLysineModels, MolecularrhoA GTP-Binding Proteinrho Guanine Nucleotide Dissociation Inhibitor alphaSirtuin 2SumoylationGuanine NucleotidesHDAC6 protein, humanHistone Deacetylase 6Histone DeacetylasesLysinerhoA GTP-Binding Proteinrho Guanine Nucleotide Dissociation Inhibitor alphaSIRT2 protein, humanSirtuin 2acetylationacetyltransferaseguanine-nucleotide-dissociation inhibitor alphahistone deacetylase (HDAC)lysine acetylationlysine acetyltransferasepost-translational modification (PTM)Ras homolog gene family, member A (RhoA)Rho (Rho GTPase)sirtuin

Identifiers

PMID26719334
PMCPMC4786691
OpenAlexW2201488213

What OpenQuestion holds

Textmetadata
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.