Evidence map›Paper›PMID 26018074›Full record

ArticleThe Journal of biological chemistry2015

TPX2 Inhibits Eg5 by Interactions with Both Motor and Microtubule.

Sai K Balchand, Barbara J Mann, Janel Titus, Jennifer L Ross, Patricia Wadsworth

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

23 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Distinct regions of the kinesin-5 C-terminal tail are essential for mitotic spindle midzone localization and sliding force.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Review
  8. Article
  9. Article
  10. Acentrosomal spindle assembly and maintenance inMolecular biology of the cell · 2022
    Article
  11. Article
  12. Article
  13. Article
  14. Kif15 functions as an active mechanical ratchet.Molecular biology of the cell · 2018
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

5 authors at 1 institution in 1 country.

Sai K Balchandthe Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, Massachusetts 01003.
Barbara J Mannthe Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, Massachusetts 01003.
Janel Titusthe Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, Massachusetts 01003.
Jennifer L Rossthe Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, Massachusetts 01003 Physics and.
Patricia Wadsworththe Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, Massachusetts 01003 From the Departments of Biology and.
University of Massachusetts Amherst · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The microtubule-associated protein, TPX2, regulates the activity of the mitotic kinesin, Eg5, but the mechanism of regulation is not established. Using total internal reflection fluorescence microscopy, we observed that Eg5, in extracts of mammalian cells expressing Eg5-EGFP, moved processively toward the microtubule plus-end at an average velocity of 14 nm/s. TPX2 bound to microtubules with an apparent dissociation constant of ∼ 200 nm, and microtubule binding was not dependent on the C-terminal tails of tubulin. Using single molecule assays, we found that full-length TPX2 dramatically reduced Eg5 velocity, whereas truncated TPX2, which lacks the domain that is required for the interaction with Eg5, was a less effective inhibitor at the same concentration. To determine the region(s) of Eg5 that is required for interaction with TPX2, we performed microtubule gliding assays. Dimeric, but not monomeric, Eg5 was differentially inhibited by full-length and truncated TPX2, demonstrating that dimerization or residues in the neck region are important for the interaction of TPX2 with Eg5. These results show that both microtubule binding and interaction with Eg5 contribute to motor inhibition by TPX2 and demonstrate the utility of mammalian cell extracts for biophysical assays.

Indexed as

AnimalsCell Cycle ProteinsGreen Fluorescent ProteinsHumansKinesinsLLC-PK1 CellsMicroscopy, FluorescenceMicrotubule-Associated ProteinsMicrotubulesModels, BiologicalMolecular Motor ProteinsNuclear ProteinsPeptide FragmentsProtein BindingProtein Interaction Domains and MotifsProtein Structure, QuaternaryCell Cycle Proteinsenhanced green fluorescent proteinGreen Fluorescent ProteinsKIF11 protein, humanKinesinsMicrotubule-Associated ProteinsMolecular Motor ProteinsNuclear ProteinsPeptide FragmentsRecombinant Fusion ProteinsTPX2 protein, humanEg5kinesinmicrotubulemicrotubule-associated protein (MAP)mitosismitotic spindlespindleTPX2

Identifiers

PMID26018074
PMCPMC4498074
OpenAlexW1652328017

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.