Evidence map›Paper›PMID 26406596›Full record

ArticlePloS one2015

TOG Proteins Are Spatially Regulated by Rac-GSK3β to Control Interphase Microtubule Dynamics.

Kathryn P Trogden, Stephen L Rogers

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

9 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. The microtubule GTP-tubulin cap size is modulated during cell division.bioRxiv : the preprint server for biology · 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

2 authors at 1 institution in 1 country.

Kathryn P TrogdenDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, United States of America.
Stephen L RogersDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, United States of America; Carolina Center for Genome Sciences, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, United States of America; Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, United States of America.
University of North Carolina at Chapel Hill · US

Funding

Mechanisms of cytoskeletal crosstalk during cellular motilityR01GM081645 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ROGERS, STEPHEN · 2008 to 2012
$1.3M
Understanding the role of Ric-8 in Ga 12/13 signalingR03HD077523 · NICHD · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ROGERS, STEPHEN · 2013 to 2014
$150k
NICHD NIH HHS R03 HD077523NICHD NIH HHS R03HD077523NIGMS NIH HHS R01 GM081645NIGMS NIH HHS R01GM081645
6 · The paper itself

Abstract

Microtubules are regulated by a diverse set of proteins that localize to microtubule plus ends (+TIPs) where they regulate dynamic instability and mediate interactions with the cell cortex, actin filaments, and organelles. Although individual +TIPs have been studied in depth and we understand their basic contributions to microtubule dynamics, there is a growing body of evidence that these proteins exhibit cross-talk and likely function to collectively integrate microtubule behavior and upstream signaling pathways. In this study, we have identified a novel protein-protein interaction between the XMAP215 homologue in Drosophila, Mini spindles (Msps), and the CLASP homologue, Orbit. These proteins have been shown to promote and suppress microtubule dynamics, respectively. We show that microtubule dynamics are regionally controlled in cells by Rac acting to suppress GSK3β in the peripheral lamellae/lamellipodium. Phosphorylation of Orbit by GSK3β triggers a relocalization of Msps from the microtubule plus end to the lattice. Mutation of the Msps-Orbit binding site revealed that this interaction is required for regulating microtubule dynamic instability in the cell periphery. Based on our findings, we propose that Msps is a novel Rac effector that acts, in partnership with Orbit, to regionally regulate microtubule dynamics.

Indexed as

AnimalsBinding SitesCell LineDrosophila melanogasterDrosophila ProteinsGene Expression RegulationGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaInterphaseMicrotubule-Associated ProteinsMicrotubulesPhosphorylationrac GTP-Binding Proteinschb protein, DrosophilaDrosophila ProteinsGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaMicrotubule-Associated Proteinsmsps protein, Drosophilarac GTP-Binding Proteins

Identifiers

PMID26406596
PMCPMC4583408
OpenAlexW2220211909

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.