Evidence map›Paper›PMID 29947928›Full record

ReviewCellular and molecular life sciences : CMLS2018

Coordination of microtubule acetylation and the actin cytoskeleton by formins.

Jaime Fernández-Barrera, Miguel A Alonso

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Identification of an FMNL2 Interactome by Quantitative Mass Spectrometry.International journal of molecular sciences · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Role of formin INF2 in human diseases.Molecular biology reports · 2022
    Review
  16. Article
  17. Review
  18. Dysregulated Dynein-Mediated Trafficking of Nephrin Causes INF2-related Podocytopathy.Journal of the American Society of Nephrology : JASN · 2021
    Article
  19. The formin INF2 in disease: progress from 10 years of research.Cellular and molecular life sciences : CMLS · 2020
    Review
  20. 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

2 authors at 1 institution in 1 country.

Jaime Fernández-BarreraDepartment of Cell Biology and Immunology, Centro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Científicas and Universidad Autónoma, Madrid, Spain.ORCID http://orcid.org/0000-0002-4186-9533
Miguel A AlonsoDepartment of Cell Biology and Immunology, Centro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Científicas and Universidad Autónoma, Madrid, Spain. maalonso@cbm.csic.es.ORCID http://orcid.org/0000-0002-7001-8826
Consejo Superior de Investigaciones Científicas · ES

Funding

Ministerio de Economía y Competitividad (ES)/ Fondo Europeo de Desarrollo Regional BFU2015-67266R
6 · The paper itself

Abstract

The acetylation of the lysine 40 residue of α-tubulin was described more than 30 years ago and has been the subject of intense research ever since. Although the exact function of this covalent modification of tubulin in the cell remains unknown, it has been established that tubulin acetylation confers resilience to mechanical stress on the microtubules. Formins have a dual role in the fate of the actin and tubulin cytoskeletons. On the one hand, they catalyze the formation of actin filaments, and on the other, they bind microtubules, act on their stability, and regulate their acetylation and alignment with actin fibers. Recent evidence indicates that formins coordinate the actin cytoskeleton and tubulin acetylation by modulating the levels of free globular actin (G-actin). G-actin, in turn, controls the activity of the myocardin-related transcription factor-serum response factor transcriptional complex that regulates the expression of the α-tubulin acetyltransferase 1 (α-TAT1) gene, which encodes the main enzyme responsible for tubulin acetylation. The effect of formins on tubulin acetylation is the combined result of their ability to activate α-TAT1 gene transcription and of their capacity to regulate microtubule stabilization. The contribution of these two mechanisms in different formins is discussed, particularly with respect to INF2, a formin that is mutated in hereditary human renal and neurodegenerative disorders.

Indexed as

Models, BiologicalAcetylationActin CytoskeletonForminsHumansKidney DiseasesMicrofilament ProteinsMicrotubulesMutationNeurodegenerative DiseasesProtein BindingForminsINF2 protein, humanMicrofilament ProteinsActin homeostasisForminsINF2MicrotubulesMyocardin-related transcription factorSerum response factorTubulin acetylationα-Tubulin acetyltransferase 1

Identifiers

PMID29947928
PMCPMC11105221
OpenAlexW2808547046

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.