ArticleScientific reports2013
Signaling efficiency of Gαq through its effectors p63RhoGEF and GEFT depends on their subcellular location.
Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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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.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- The working lives of neuronal 5-HTRSC chemical biology · 2026Review
- Article
- The C-terminus of the oncoprotein TGAT is necessary for plasma membrane association and efficient RhoA-mediated signaling.BMC cell biology · 2018Article
- The role of a conserved membrane proximal cysteine in altering αPS2CβPS integrin diffusion.Physical biology · 2016Article
- Kinetics of recruitment and allosteric activation of ARHGEF25 isoforms by the heterotrimeric G-protein Gαq.Scientific reports · 2016Article
- Plasma membrane restricted RhoGEF activity is sufficient for RhoA-mediated actin polymerization.Scientific reports · 2015Article
- Altered reactivity of resistance vasculature contributes to hypertension in elastin insufficiency.American journal of physiology. Heart and circulatory physiology · 2014Article
- Strike a pose: Gαq complexes at the membrane.Trends in pharmacological sciences · 2014Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The p63RhoGEF and GEFT proteins are encoded by the same gene and both members of the Dbl family of guanine nucleotide exchange factors. These proteins can be activated by the heterotrimeric G-protein subunit Gαq. We show that p63RhoGEF is located at the plasma membrane, whereas GEFT is confined to the cytoplasm. Live-cell imaging studies yielded quantitative information on diffusion coefficients, association rates and encounter times of GEFT and p63RhoGEF. Calcium signaling was examined as a measure of the signal transmission, revealing more efficient signaling through the membrane-associated p63RhoGEF. A rapamycin dependent recruitment system was used to dynamically alter the subcellular location and concentration of GEFT, showing efficient signaling through GEFT only upon membrane recruitment. Together, our results show efficient signal transmission through membrane located effectors, and highlight a role for increased concentration rather than increased encounter times due to membrane localization in the Gαq mediated pathways to p63RhoGEF and PLCβ.
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Registered trials
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