Evidence map›Paper›PMID 25117684›Full record

ArticleDevelopmental cell2014

CLASPs are required for proper microtubule localization of end-binding proteins.

Ashley D Grimaldi, Takahisa Maki, Benjamin P Fitton, Daniel Roth, Dmitry Yampolsky, Michael W Davidson, Tatyana Svitkina, Anne Straube, Ikuko Hayashi, Irina Kaverina

Open access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.0field-weighted citation impact, top 16% 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

27 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Tubulin flux at spastin-induced nanodamage sites regulates microtubule rescue frequency and EB1 lifetimes.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

10 authors at 5 institutions in 3 countries.

Ashley D GrimaldiDepartment of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
Takahisa MakiDepartment of Medical Life Science, Yokohama City University, 1-7-29 Suehiro, Tsurumi, Yokohama 230-0045, Japan.
Benjamin P FittonCentre for Mechanochemical Cell Biology, Warwick Medical School, University of Warwick, Coventry CV4 7AL, UK.
Daniel RothCentre for Mechanochemical Cell Biology, Warwick Medical School, University of Warwick, Coventry CV4 7AL, UK.
Dmitry YampolskyDepartment of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
Michael W DavidsonNational High Magnetic Field Laboratory and Department of Biological Science, Florida State University, Tallahassee, FL 32310, USA.
Tatyana SvitkinaDepartment of Biology, University of Pennsylvania, Philadelphia, PA 19104, USA.
Anne StraubeCentre for Mechanochemical Cell Biology, Warwick Medical School, University of Warwick, Coventry CV4 7AL, UK.
Ikuko HayashiDepartment of Medical Life Science, Yokohama City University, 1-7-29 Suehiro, Tsurumi, Yokohama 230-0045, Japan.
Irina KaverinaDepartment of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37232, USA. Electronic address: irina.kaverina@vanderbilt.edu.
University of Warwick · GBVanderbilt University Medical Center · USYokohama City University · JPNational High Magnetic Field Laboratory · USUniversity of Pennsylvania · US

Funding

Spatial Regulation of Cytoskeletal AsymmetryR01GM078373 · NIGMS · VANDERBILT UNIVERSITY · PI KAVERINA, IRINA · 2008 to 2017
$3.2M
Multifaceted roles of nonmuscle myosin II in cell adhesion and migrationR01GM095977 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI SVITKINA, TATYANA · 2013 to 2020
$2.7M
British Heart Foundation FS/13/42/30377NIGMS NIH HHS GM078373NIGMS NIH HHS R01 GM078373NIGMS NIH HHS R01 GM095977
6 · The paper itself

Abstract

Microtubule (MT) plus-end tracking proteins (+TIPs) preferentially localize to MT plus ends. End-binding proteins (EBs) are master regulators of the +TIP complex; however, it is unknown whether EBs are regulated by other +TIPs. Here, we show that cytoplasmic linker-associated proteins (CLASPs) modulate EB localization at MTs. In CLASP-depleted cells, EBs localized along the MT lattice in addition to plus ends. The MT-binding region of CLASP was sufficient for restoring normal EB localization, whereas neither EB-CLASP interactions nor EB tail-binding proteins are involved. In vitro assays revealed that CLASP directly functions to remove EB from MTs. Importantly, this effect occurs specifically during MT polymerization, but not at preformed MTs. Increased GTP-tubulin content within MTs in CLASP-depleted cells suggests that CLASPs facilitate GTP hydrolysis to reduce EB lattice binding. Together, these findings suggest that CLASPs influence the MT lattice itself to regulate EB and determine exclusive plus-end localization of EBs in cells.

Indexed as

AnimalsCarrier ProteinsCell LineCytoplasmHumansMicrotubule-Associated ProteinsMicrotubulesProtein BindingRatsTubulinCarrier ProteinsMicrotubule-Associated ProteinsTubulin

Identifiers

PMID25117684
PMCPMC4133696
OpenAlexW1966245475

What OpenQuestion holds

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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.