Evidence map›Paper›PMID 28204846›Full record

ReviewCellular and molecular life sciences : CMLS2017

Regulation of end-binding protein EB1 in the control of microtubule dynamics.

Anne Nehlig, Angie Molina, Sylvie Rodrigues-Ferreira, Stéphane Honoré, Clara Nahmias

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

78 citing papers in PubMed, 138 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. The endocytic fission protein EHD1 interacts with tubulin and regulates microtubule function.Biochimica et biophysica acta. Molecular cell research · 2026
    Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. EB-SUN, a new microtubule plus-end tracking protein inMolecular biology of the cell · 2024
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

18 more citing papers are in PubMed but not listed here.

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

5 authors at 3 institutions in 1 country.

Anne NehligInserm U981, Institut Gustave Roussy, 114 rue Edouard Vaillant, 94800, Villejuif, France.
Angie MolinaInserm U981, Institut Gustave Roussy, 114 rue Edouard Vaillant, 94800, Villejuif, France.
Sylvie Rodrigues-FerreiraInserm U981, Institut Gustave Roussy, 114 rue Edouard Vaillant, 94800, Villejuif, France.
Stéphane HonoréAix Marseille University, Inserm U-911, CRO2, Marseille, France.
Clara NahmiasInserm U981, Institut Gustave Roussy, 114 rue Edouard Vaillant, 94800, Villejuif, France. clara.nahmias@inserm.fr.
Institut Gustave Roussy · FRUniversité Paris-Saclay · FRAix-Marseille Université · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The regulation of microtubule dynamics is critical to ensure essential cell functions, such as proper segregation of chromosomes during mitosis or cell polarity and migration. End-binding protein 1 (EB1) is a plus-end-tracking protein (+TIP) that accumulates at growing microtubule ends and plays a pivotal role in the regulation of microtubule dynamics. EB1 autonomously binds an extended tubulin-GTP/GDP-Pi structure at growing microtubule ends and acts as a molecular scaffold that recruits a large number of regulatory +TIPs through interaction with CAP-Gly or SxIP motifs. While extensive studies have focused on the structure of EB1-interacting site at microtubule ends and its role as a molecular platform, the mechanisms involved in the negative regulation of EB1 have only started to emerge and remain poorly understood. In this review, we summarize recent studies showing that EB1 association with MT ends is regulated by post-translational modifications and affected by microtubule-targeting agents. We also present recent findings that structural MAPs, that have no tip-tracking activity, physically interact with EB1 to prevent its accumulation at microtubule plus ends. These observations point out a novel concept of "endogenous EB1 antagonists" and emphasize the importance of finely regulating EB1 function at growing microtubule ends.

Indexed as

AnimalsBinding SitesGuanosine TriphosphateHumansMicrotubule-Associated ProteinsMicrotubulesModels, BiologicalProtein Processing, Post-TranslationalEB1 microtubule binding proteinsGuanosine TriphosphateMicrotubule-Associated ProteinsEB1EB3MAPsMicrotubule-targeting agentsPhosphorylation+TIP

Identifiers

PMID28204846
PMCPMC11107513
OpenAlexW2588345357

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.