Evidence map›Paper›PMID 25588829›Full record

ArticleJournal of cell science2015

Acetylation of the RhoA GEF Net1A controls its subcellular localization and activity.

Eun Hyeon Song, Wonkyung Oh, Arzu Ulu, Heather S Carr, Yan Zuo, Jeffrey A Frost

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2015. 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
2.9field-weighted citation impact, top 9% 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, 43 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Eun Hyeon SongDepartment of Integrative Biology and Pharmacology, University of Texas Health Science Center at Houston, 6431 Fannin St., Houston, TX 77030, USA.
Wonkyung OhDepartment of Integrative Biology and Pharmacology, University of Texas Health Science Center at Houston, 6431 Fannin St., Houston, TX 77030, USA.
Arzu UluDepartment of Integrative Biology and Pharmacology, University of Texas Health Science Center at Houston, 6431 Fannin St., Houston, TX 77030, USA.
Heather S CarrDepartment of Integrative Biology and Pharmacology, University of Texas Health Science Center at Houston, 6431 Fannin St., Houston, TX 77030, USA.
Yan ZuoDepartment of Integrative Biology and Pharmacology, University of Texas Health Science Center at Houston, 6431 Fannin St., Houston, TX 77030, USA.
Jeffrey A FrostDepartment of Integrative Biology and Pharmacology, University of Texas Health Science Center at Houston, 6431 Fannin St., Houston, TX 77030, USA jeffrey.a.frost@uth.tmc.edu.
The University of Texas Health Science Center at Houston · US

Funding

Role of the RhoGEF Net1 in breast cancer cell motility and metastasisR01CA172129 · NCI · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI FROST, JEFFREY A. · 2014 to 2018
$1.6M
Rho GEFs in Cellular Proliferation and TransformationR01CA116356 · NCI · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI FROST, JEFFREY A. · 2007 to 2011
$1.4M
ERK/MAP KINASE SIGNALLING PATHWAYSF32GM016926 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI FROST, JEFFREY A · 1994 to 1996
–
NCI NIH HHS CA116356NCI NIH HHS CA172129NCI NIH HHS R01 CA116356NCI NIH HHS R01 CA172129NIGMS NIH HHS F32 GM016926
6 · The paper itself

Abstract

Net1 isoform A (Net1A) is a RhoA GEF that is required for cell motility and invasion in multiple cancers. Nuclear localization of Net1A negatively regulates its activity, and we have recently shown that Rac1 stimulates Net1A relocalization to the plasma membrane to promote RhoA activation and cytoskeletal reorganization. However, mechanisms controlling the subcellular localization of Net1A are not well understood. Here, we show that Net1A contains two nuclear localization signal (NLS) sequences within its N-terminus and that residues surrounding the second NLS sequence are acetylated. Treatment of cells with deacetylase inhibitors or expression of active Rac1 promotes Net1A acetylation. Deacetylase inhibition is sufficient for Net1A relocalization outside the nucleus, and replacement of the N-terminal acetylation sites with arginine residues prevents cytoplasmic accumulation of Net1A caused by deacetylase inhibition or EGF stimulation. By contrast, replacement of these sites with glutamine residues is sufficient for Net1A relocalization, RhoA activation and downstream signaling. Moreover, the N-terminal acetylation sites are required for rescue of F-actin accumulation and focal adhesion maturation in Net1 knockout MEFs. These data indicate that Net1A acetylation regulates its subcellular localization to impact on RhoA activity and actin cytoskeletal organization.

Indexed as

AcetylationActive Transport, Cell NucleusAnimalsCell MembraneCell NucleusCytoskeletonHeLa CellsHumansMiceMice, KnockoutNeuropeptidesNuclear Localization SignalsOncogene ProteinsProtein Isoformsrac1 GTP-Binding ProteinrhoA GTP-Binding ProteinNET1 protein, humanNet1 protein, mouseNeuropeptidesNuclear Localization SignalsOncogene ProteinsProtein Isoformsrac1 GTP-Binding ProteinRAC1 protein, humanRac1 protein, mouserhoA GTP-Binding ProteinRHOA protein, humanRhoA protein, mouserho GTP-Binding ProteinsAcetylationEGFF-actinLocalizationNet1RhoA

Identifiers

PMID25588829
PMCPMC4342578
OpenAlexW1997442473

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.