Evidence map›Paper›PMID 20708587›Full record

ArticleDevelopmental cell2010

CLASP promotes microtubule rescue by recruiting tubulin dimers to the microtubule.

Jawdat Al-Bassam, Hwajin Kim, Gary Brouhard, Antoine van Oijen, Stephen C Harrison, Fred Chang

Open access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.

0numbers the graph read from it
0cells of the map it votes in
128citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

128 citing papers in PubMed, 209 citations in OpenAlex.

  1. CLASP2 promotes repair of kinesin-1 damage to the microtubule lattice.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Review
  4. SSNA1 mechanically reinforces the damaged microtubule lattice.bioRxiv : the preprint server for biology · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Tubulin Complexity in Cancer and Metastasis.Advances in experimental medicine and biology · 2024
    Review
  10. Article
  11. Article
  12. Mechanical coupling coordinates microtubule growth.bioRxiv : the preprint server for biology · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Gcap14 is a microtubule plus-end-tracking protein coordinating microtubule-actin crosstalk during neurodevelopment.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  20. Article

68 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

6 authors at 2 institutions in 2 countries.

Jawdat Al-BassamDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA. jawdat@crystal.harvard.edu
Hwajin Kim
Gary Brouhard
Antoine van Oijen
Stephen C Harrison
Fred Chang
Harvard University · USMcGill University · CA

Funding

Nuclear Positioning and Microtubule OrganizationR01GM069670 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI CHANG, FRED · 2005 to 2012
$2.4M
Microtubule Polymerization and Depolymerization Mechanisms by Conserved ProteinsR00GM084292 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI AL-BASSAM, JAWDAT MH · 2011 to 2013
$715k
Microtubule Polymerization and Depolymerization Mechanisms by Conserved ProteinsK99GM084292 · NIGMS · HARVARD MEDICAL SCHOOL · PI AL-BASSAM, JAWDAT MH · 2008 to 2010
$217k
Howard Hughes Medical InstituteNIGMS NIH HHS GM069670NIGMS NIH HHS K99 GM084292NIGMS NIH HHS R00 GM084292NIGMS NIH HHS R01 GM069670PHS HHS GMO8429
6 · The paper itself

Abstract

Spatial regulation of microtubule (MT) dynamics contributes to cell polarity and cell division. MT rescue, in which a MT stops shrinking and reinitiates growth, is the least understood aspect of MT dynamics. Cytoplasmic Linker Associated Proteins (CLASPs) are a conserved class of MT-associated proteins that contribute to MT stabilization and rescue in vivo. We show here that the Schizosaccharomyces pombe CLASP, Cls1p, is a homodimer that binds an alphabeta-tubulin heterodimer through conserved TOG-like domains. In vitro, CLASP increases MT rescue frequency, decreases MT catastrophe frequency, and moderately decreases MT disassembly rate. CLASP binds stably to the MT lattice, recruits tubulin, and locally promotes rescues. Mutations in the CLASP TOG domains demonstrate that tubulin binding is critical for its rescue activity. We propose a mechanism for rescue in which CLASP-tubulin dimer complexes bind along the MT lattice and reverse MT depolymerization with their bound tubulin dimer.

Indexed as

Protein Structure, QuaternaryHumansMicrotubulesModels, MolecularNuclear ProteinsProtein BindingProtein MultimerizationProtein Structure, TertiaryRecombinant Fusion ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsTubulinNuclear ProteinsPeg1 protein, S pombeRecombinant Fusion ProteinsSchizosaccharomyces pombe ProteinsTubulin

Identifiers

PMID20708587
PMCPMC3156696
OpenAlexW2039737272

What OpenQuestion holds

Textmetadata
LicenceTDM
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.