Evidence map›Paper›PMID 24362037›Full record

ArticleThe Journal of biological chemistry2014

Interaction between microtubules and the Drosophila formin Cappuccino and its effect on actin assembly.

Elizabeth A Roth-Johnson, Christina L Vizcarra, Justin S Bois, Margot E Quinlan

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Article
  2. Review
  3. Antagonistic Activities of Fmn2 and ADF Regulate Axonal F-Actin Patch Dynamics and the Initiation of Collateral Branching.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. New twists in actin-microtubule interactions.Molecular biology of the cell · 2021
    Review
  9. Epithelial morphogenesis, tubulogenesis and forces in organogenesis.Current topics in developmental biology · 2021
    Review
  10. Article
  11. Article
  12. Profilin choreographs actin and microtubules in cells and cancer.International review of cell and molecular biology · 2020
    Article
  13. Article
  14. Actin-microtubule crosstalk in cell biology.Nature reviews. Molecular cell biology · 2019
    Review
  15. Review
  16. The Journal of biological chemistry · 2018
    Article
  17. Article
  18. Article
  19. Dynamic microtubules regulate cellular contractility during T-cell activation.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  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

4 authors.

Elizabeth A Roth-JohnsonFrom the Molecular Biology Interdepartmental PhD Program.
Christina L Vizcarra
Justin S Bois
Margot E Quinlan

Funding

UCLA NIGMS T32 Program AssessmentT32GM007185 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORRES, JORGE · 1985 to 2020
$21.7M
Collaboration between actin nucleators - Spire and CappuccinoR01GM096133 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI QUINLAN, MARGOT E · 2011 to 2024
$4.1M
Understanding actin nucleation by and regulation of the Spire/Cappuccino complexF32GM087857 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI VIZCARRA, CHRISTINA LUISA · 2009 to 2011
$151k
NIGMS NIH HHS F32 GM087857NIGMS NIH HHS F32GM087857NIGMS NIH HHS GM007185NIGMS NIH HHS R01 GM096133NIGMS NIH HHS T32 GM007185
6 · The paper itself

Abstract

Formin family actin nucleators are potential coordinators of the actin and microtubule cytoskeletons, as they can both nucleate actin filaments and bind microtubules in vitro. To gain a more detailed mechanistic understanding of formin-microtubule interactions and formin-mediated actin-microtubule cross-talk, we studied microtubule binding by Cappuccino (Capu), a formin involved in regulating actin and microtubule organization during Drosophila oogenesis. We found that two distinct domains within Capu, FH2 and tail, work together to promote high-affinity microtubule binding. The tail domain appears to bind microtubules through nonspecific charge-based interactions. In contrast, distinct residues within the FH2 domain are important for microtubule binding. We also report the first visualization of a formin polymerizing actin filaments in the presence of microtubules. Interestingly, microtubules are potent inhibitors of the actin nucleation activity of Capu but appear to have little effect on Capu once it is bound to the barbed end of an elongating filament. Because Capu does not simultaneously bind microtubules and assemble actin filaments in vitro, its actin assembly and microtubule binding activities likely require spatial and/or temporal regulation within the Drosophila oocyte.

Indexed as

Actin CytoskeletonActinsAnimalsDrosophila melanogasterDrosophila ProteinsFemaleMaleMicrofilament ProteinsMicrotubulesOocytesOogenesisProtein MultimerizationProtein Structure, TertiaryActinscapu protein, DrosophilaDrosophila ProteinsMicrofilament ProteinsActinCapuCell PolarityCytoskeletonForminMicrotubulesOocyteTIRF

Identifiers

PMID24362037
PMCPMC3924302

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.