Evidence map›Paper›PMID 19618964›Full record

ArticleBiochemistry2009

The amino acid motif L/IIxxFE defines a novel actin-binding sequence in PDZ-RhoGEF.

Jayashree Banerjee, Christopher C Fischer, Philip B Wedegaertner

Abstract readComparative Study
In one paragraph

Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

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  11. PLEKHG3 enhances polarized cell migration by activating actin filaments at the cell front.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
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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

3 authors at 1 institution in 1 country.

Jayashree BanerjeeDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.
Christopher C Fischer
Philip B Wedegaertner
Thomas Jefferson University · US

Funding

SIGNALING THROUGH RHO GTP/GDP EXCHANGE FACTORSR01GM062884 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI WEDEGAERTNER, PHILIP B · 2001 to 2013
$3.4M
NIGMS NIH HHS GM62884NIGMS NIH HHS R01 GM062884
6 · The paper itself

Abstract

PDZ-RhoGEF is a member of the regulator family of G protein signaling (RGS) domain-containing RhoGEFs (RGS-RhoGEFs) that link activated heterotrimeric G protein alpha subunits of the G12 family to activation of the small GTPase RhoA. Unique among the RGS-RhoGEFs, PDZ-RhoGEF contains a short sequence that localizes the protein to the actin cytoskeleton. In this report, we demonstrate that the actin-binding domain, located between amino acids 561 and 585, directly binds to F-actin in vitro. Extensive mutagenesis identifies isoleucine 568, isoleucine 569, phenylalanine 572, and glutamic acid 573 as being necessary for binding to actin and for colocalization with the actin cytoskeleton in cells. These results define a novel actin-binding sequence in PDZ-RhoGEF with a critical amino acid motif of IIxxFE. Moreover, sequence analysis identifies a similar actin-binding motif in the N-terminus of the RhoGEF frabin, and as with PDZ-RhoGEF, mutagenesis and actin interaction experiments demonstrate an LIxxFE motif, consisting of the key amino acids leucine 23, isoleucine 24, phenylalanine 27, and glutamic acid 28. Taken together, results with PDZ-RhoGEF and frabin identify a novel actin-binding sequence. Lastly, inducible dimerization of the actin-binding region of PDZ-RhoGEF revealed a dimerization-dependent actin bundling activity in vitro. PDZ-RhoGEF exists in cells as a dimer, raising the possibility that PDZ-RhoGEF could influence actin structure in a manner independent of its ability to activate RhoA.

Indexed as

ActinsAmino Acid MotifsAmino Acid SequenceAnimalsChlorocebus aethiopsConserved SequenceCOS CellsDimerizationGuanine Nucleotide Exchange FactorsMiceMicrofilament ProteinsMolecular Sequence DataMutagenesis, Site-DirectedrhoA GTP-Binding ProteinRho Guanine Nucleotide Exchange FactorsZebrafish ProteinsActinsARHGEF11 protein, humanFGD4 protein, humanGuanine Nucleotide Exchange FactorsMicrofilament ProteinsrhoA GTP-Binding ProteinRHOA protein, humanRho Guanine Nucleotide Exchange FactorsZebrafish Proteins

Identifiers

PMID19618964
PMCPMC2728795
OpenAlexW1992482702

What OpenQuestion holds

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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.