Evidence map›Paper›PMID 21998204›Full record

ArticleMolecular biology of the cell2011

Differential interactions of the formins INF2, mDia1, and mDia2 with microtubules.

Jeremie Gaillard, Vinay Ramabhadran, Emmanuelle Neumanne, Pinar Gurel, Laurent Blanchoin, Marylin Vantard, Henry N Higgs

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
4.4field-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

89 citing papers in PubMed, 126 citations in OpenAlex.

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  14. 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
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  20. The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022
    Review

29 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

7 authors at 2 institutions in 2 countries.

Jeremie GaillardCEA, iRTSV, Laboratoire Physiologie Cellulaire & Végétale, CNRS, UMR5168, Université Joseph Fourier-Grenoble I, F-38054 Grenoble, France.
Vinay Ramabhadran
Emmanuelle Neumanne
Pinar Gurel
Laurent Blanchoin
Marylin Vantard
Henry N Higgs
Centre National de la Recherche Scientifique · FRDartmouth College · US

Funding

INF2 in kidney function and dysfunctionR01DK088826 · NIDDK · BETH ISRAEL DEACONESS MEDICAL CENTER · PI HENRY N HIGGS, MARTIN R. POLLAK · 2010 to 2026
$6.3M
Comparative molecular physiology of mammalian forminsR01GM069818 · NIGMS · DARTMOUTH COLLEGE · PI HIGGS, HENRY N · 2004 to 2017
$4.3M
NIDDK NIH HHS DK088826NIDDK NIH HHS R01 DK088826NIGMS NIH HHS R01 GM069818
6 · The paper itself

Abstract

A number of cellular processes use both microtubules and actin filaments, but the molecular machinery linking these two cytoskeletal elements remains to be elucidated in detail. Formins are actin-binding proteins that have multiple effects on actin dynamics, and one formin, mDia2, has been shown to bind and stabilize microtubules through its formin homology 2 (FH2) domain. Here we show that three formins, INF2, mDia1, and mDia2, display important differences in their interactions with microtubules and actin. Constructs containing FH1, FH2, and C-terminal domains of all three formins bind microtubules with high affinity (K(d) < 100 nM). However, only mDia2 binds microtubules at 1:1 stoichiometry, with INF2 and mDia1 showing saturating binding at approximately 1:3 (formin dimer:tubulin dimer). INF2-FH1FH2C is a potent microtubule-bundling protein, an effect that results in a large reduction in catastrophe rate. In contrast, neither mDia1 nor mDia2 is a potent microtubule bundler. The C-termini of mDia2 and INF2 have different functions in microtubule interaction, with mDia2's C-terminus required for high-affinity binding and INF2's C-terminus required for bundling. mDia2's C-terminus directly binds microtubules with submicromolar affinity. These formins also differ in their abilities to bind actin and microtubules simultaneously. Microtubules strongly inhibit actin polymerization by mDia2, whereas they moderately inhibit mDia1 and have no effect on INF2. Conversely, actin monomers inhibit microtubule binding/bundling by INF2 but do not affect mDia1 or mDia2. These differences in interactions with microtubules and actin suggest differential function in cellular processes requiring both cytoskeletal elements.

Indexed as

Actin CytoskeletonActinsAnimalsCarrier ProteinsForminsHumansMiceMicrofilament ProteinsMicrotubule-Associated ProteinsMicrotubulesNADPH DehydrogenaseProtein Structure, TertiaryRabbitsRecombinant ProteinsActinsCarrier ProteinsDia2 protein, mouseDiap1 protein, mouseForminsINF2 protein, humanMicrofilament ProteinsMicrotubule-Associated ProteinsNADPH DehydrogenaseRecombinant Proteins

Identifiers

PMID21998204
PMCPMC3226476
OpenAlexW2040611486

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.