Evidence map›Paper›PMID 19696020›Full record

ArticleThe Journal of biological chemistry2009

The ubiquitin-like protein LC3 regulates the Rho-GEF activity of AKAP-Lbc.

Laurent Baisamy, Sabrina Cavin, Nathalie Jurisch, Dario Diviani

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 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
1.3field-weighted citation impact, top 20% 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, 27 citations in OpenAlex.

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  12. Streamlined embedding of cell monolayers on gridded glass-bottom imaging dishes for correlative light and electron microscopy.Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2010
    Article
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  14. Conserved role for autophagy in Rho1-mediated cortical remodeling and blood cell recruitment.Proceedings of the National Academy of Sciences of the United States of America · 2010
    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

4 authors at 1 institution in 1 country.

Laurent BaisamyDépartement de Pharmacologie et de Toxicologie, Faculté de Biologie et de Médecine, Rue du Bugnon 27, Lausanne 1005, Switzerland.
Sabrina CavinDépartement de Pharmacologie et de Toxicologie, Faculté de Biologie et de Médecine, Rue du Bugnon 27, Lausanne 1005, Switzerland.
Nathalie JurischDépartement de Pharmacologie et de Toxicologie, Faculté de Biologie et de Médecine, Rue du Bugnon 27, Lausanne 1005, Switzerland.
Dario DivianiDépartement de Pharmacologie et de Toxicologie, Faculté de Biologie et de Médecine, Rue du Bugnon 27, Lausanne 1005, Switzerland. Electronic address: Dario.diviani@unil.ch.
University of Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AKAP-Lbc is a member of the A-kinase anchoring protein (AKAP) family that has been recently associated with the development of pathologies, such as cardiac hypertrophy and cancer. We have previously demonstrated that, at the molecular level, AKAP-Lbc functions as a guanine nucleotide exchange factor (GEF) that promotes the specific activation of RhoA. In the present study, we identified the ubiquitin-like protein LC3 as a novel regulatory protein interacting with AKAP-Lbc. Mutagenesis studies revealed that LC3, through its NH(2)-terminal alpha-helical domain, interacts with two binding sites located within the NH(2)-terminal regulatory region of AKAP-Lbc. Interestingly, LC3 overexpression strongly reduced the ability of AKAP-Lbc to interact with RhoA, profoundly impairing the Rho-GEF activity of the anchoring protein and, as a consequence, its ability to promote cytoskeletal rearrangements associated with the formation of actin stress fibers. Moreover, AKAP-Lbc mutants that fail to interact with LC3 show a higher basal Rho-GEF activity as compared with the wild type protein and become refractory to the inhibitory effect of LC3. This suggests that LC3 binding maintains AKAP-Lbc in an inactive state that displays a reduced ability to promote downstream signaling. Collectively, these findings provide evidence for a previously uncharacterized role of LC3 in the regulation of Rho signaling and in the reorganization of the actin cytoskeleton.

Indexed as

A Kinase Anchor ProteinsAnimalsCell LineGuanine Nucleotide Exchange FactorsHumansMiceMicrotubule-Associated ProteinsMinor Histocompatibility AntigensModels, MolecularNIH 3T3 CellsProto-Oncogene ProteinsRecombinant Fusion ProteinsRho Guanine Nucleotide Exchange FactorsSignal TransductionTwo-Hybrid System TechniquesAKAP13 protein, humanA Kinase Anchor ProteinsGuanine Nucleotide Exchange FactorsMAP1LC3A protein, humanMicrotubule-Associated ProteinsMinor Histocompatibility AntigensProto-Oncogene ProteinsRecombinant Fusion ProteinsRho Guanine Nucleotide Exchange Factors

Identifiers

PMID19696020
PMCPMC2788875
OpenAlexW2088100199

What OpenQuestion holds

Textmetadata
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.