Evidence map›Paper›PMID 21965297›Full record

ArticleMolecular biology of the cell2011

The microtubule lattice and plus-end association of Drosophila Mini spindles is spatially regulated to fine-tune microtubule dynamics.

Joshua D Currie, Shannon Stewman, Gregory Schimizzi, Kevin C Slep, Ao Ma, Stephen L Rogers

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. The dynamic duo of microtubule polymerase Mini spindles/XMAP215 and cytoplasmic dynein is essential for maintainingProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. bioRxiv : the preprint server for biology · 2023
    Article
  6. MAPping tubulin mutations.Frontiers in cell and developmental biology · 2023
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

6 authors.

Joshua D CurrieDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Shannon Stewman
Gregory Schimizzi
Kevin C Slep
Ao Ma
Stephen L Rogers

Funding

Determining the spindle dynamics regulatory network with an integrated approachR01GM086536 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI MA, AO · 2010 to 2014
$1.5M
Mechanisms of cytoskeletal crosstalk during cellular motilityR01GM081645 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ROGERS, STEPHEN · 2008 to 2012
$1.3M
NIGMS NIH HHS R01 GM081645NIGMS NIH HHS R01GM081645NIGMS NIH HHS R01 GM086536NIGMS NIH HHS R01GM086536
6 · The paper itself

Abstract

Individual microtubules (MTs) exhibit dynamic instability, a behavior in which they cycle between phases of growth and shrinkage while the total amount of MT polymer remains constant. Dynamic instability is promoted by the conserved XMAP215/Dis1 family of microtubule-associated proteins (MAPs). In this study, we conducted an in vivo structure-function analysis of the Drosophila homologue Mini spindles (Msps). Msps exhibits EB1-dependent and spatially regulated MT localization, targeting to microtubule plus ends in the cell interior and decorating the lattice of growing and shrinking microtubules in the cell periphery. RNA interference rescue experiments revealed that the NH(2)-terminal four TOG domains of Msps function as paired units and were sufficient to promote microtubule dynamics and EB1 comet formation. We also identified TOG5 and novel inter-TOG linker motifs that are required for targeting Msps to the microtubule lattice. These novel microtubule contact sites are necessary for the interplay between the conserved TOG domains and inter-TOG MT binding that underlies the ability of Msps to promote MT dynamic instability.

Indexed as

Amino Acid MotifsAnimalsCell LineDrosophilaDrosophila ProteinsMicrofilament ProteinsMicrotubule-Associated ProteinsMicrotubulesProtein BindingProtein Structure, TertiaryRNA InterferenceSpindle ApparatusDrosophila ProteinsEB1 microtubule binding proteinsMicrofilament ProteinsMicrotubule-Associated Proteinsmsps protein, Drosophila

Identifiers

PMID21965297
PMCPMC3216660

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.