Evidence map›Paper›PMID 26003921›Full record

ArticleJournal of molecular biology2015

CLASP2 Has Two Distinct TOG Domains That Contribute Differently to Microtubule Dynamics.

Takahisa Maki, Ashley D Grimaldi, Sotaro Fuchigami, Irina Kaverina, Ikuko Hayashi

Abstract read
In one paragraph

Article in Journal of molecular biology, 2015. 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
1.6field-weighted citation impact, top 19% 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

24 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. The Link between Oxygen and Basement Membranes.Reviews of physiology, biochemistry and pharmacology · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. A cryptic tubulin-binding domain links MEKK1 to curved tubulin protomers.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Article
  13. CLASPs at a glance.Journal of cell science · 2020
    Review
  14. Article
  15. The Journal of biological chemistry · 2019
    Article
  16. Article
  17. Review
  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

5 authors at 2 institutions in 2 countries.

Takahisa MakiDepartment of Medical Life Science, Yokohama City University, 1-7-29 Suehiro, Tsurumi, Yokohama, Kanagawa 230-0045, Japan.
Ashley D GrimaldiDepartment of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
Sotaro FuchigamiDepartment of Medical Life Science, Yokohama City University, 1-7-29 Suehiro, Tsurumi, Yokohama, Kanagawa 230-0045, Japan.
Irina KaverinaDepartment of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
Ikuko HayashiDepartment of Medical Life Science, Yokohama City University, 1-7-29 Suehiro, Tsurumi, Yokohama, Kanagawa 230-0045, Japan. Electronic address: ihay@tsurumi.yokohama-cu.ac.jp.
Vanderbilt University Medical Center · USYokohama City University · JP

Funding

Spatial Regulation of Cytoskeletal AsymmetryR01GM078373 · NIGMS · VANDERBILT UNIVERSITY · PI KAVERINA, IRINA · 2008 to 2017
$3.2M
NIGMS NIH HHS GM078373NIGMS NIH HHS R01 GM078373
6 · The paper itself

Abstract

CLIP-associated proteins CLASPs are mammalian microtubule (MT) plus-end tracking proteins (+TIPs) that promote MT rescue in vivo. Their plus-end localization is dependent on other +TIPs, EB1 and CLIP-170, but in the leading edge of the cell, CLASPs display lattice-binding activity. MT association of CLASPs is suggested to be regulated by multiple TOG (tumor overexpressed gene) domains and by the serine-arginine (SR)-rich region, which contains binding sites for EB1. Here, we report the crystal structures of the two TOG domains of CLASP2. Both domains consist of six HEAT repeats, which are similar to the canonical paddle-like tubulin-binding TOG domains, but have arched conformations. The degrees and directions of curvature are different between the two TOG domains, implying that they have distinct roles in MT binding. Using biochemical, molecular modeling and cell biological analyses, we have investigated the interactions between the TOG domains and αβ-tubulin and found that each domain associates differently with αβ-tubulin. Our findings suggest that, by varying the degrees of domain curvature, the TOG domains may distinguish the structural conformation of the tubulin dimer, discriminate between different states of MT dynamic instability and thereby function differentially as stabilizers of MTs.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCells, CulturedCrystallography, X-RayHEK293 CellsHumansMiceMicrotubule-Associated ProteinsMicrotubulesModels, MolecularMolecular Sequence DataProtein BindingProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiaryCLASP2 protein, humanCLASP2 protein, mouseMicrotubule-Associated Proteinscrystal structuremicrotubulemicrotubule-associated protein (MAP)molecular modeling+TIPs

Identifiers

PMID26003921
PMCPMC4646087
OpenAlexW225539739

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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.