ArticleBiophysics and physicobiology2017
Single-molecule fluorescence imaging of RalGDS on cell surfaces during signal transduction from Ras to Ral.
Article in Biophysics and physicobiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- Cell cycle dependence of ERK activation dynamics is regulated by PI3K and PAK1 signaling.Scientific reports · 2025Article
- The Isoforms of Ral Guanine Nucleotide Dissociation Stimulator (RalGDS) in LLC-PK1 Cells.Current issues in molecular biology · 2025Article
- Application of single-molecule analysis to singularity phenomenon of cells.Biophysics and physicobiology · 2024Article
- Impact of KRAS mutation on the tumor microenvironment in colorectal cancer.International journal of biological sciences · 2024Review
- Study on antihepatocellular carcinoma effect of 6-shogaol and curcumin through network-based pharmacological and cellular assay.Frontiers in pharmacology · 2024Article
- p52Shc regulates the sustainability of ERK activation in a RAF-independent manner.Molecular biology of the cell · 2021Article
- Workflows of the Single-Molecule Imaging Analysis in Living Cells: Tutorial Guidance to the Measurement of the Drug Effects on a GPCR.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Biphasic spatiotemporal regulation of GRB2 dynamics by p52SHC for transient RAS activation.Biophysics and physicobiology · 2021Article
- The effects of mutant Ras proteins on the cell signalome.Cancer metastasis reviews · 2020Review
- Single-molecule fluorescence-based analysis of protein conformation, interaction, and oligomerization in cellular systems.Biophysical reviews · 2018Review
- Mutation-Specific Mechanisms of Hyperactivation of Noonan Syndrome SOS Molecules Detected with Single-molecule Imaging in Living Cells.Scientific reports · 2017Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RalGDS is one of the Ras effectors and functions as a guanine nucleotide exchange factor for the small G-protein, Ral, which regulates membrane trafficking and cytoskeletal remodeling. The translocation of RalGDS from the cytoplasm to the plasma membrane is required for Ral activation. In this study, to understand the mechanism of Ras-Ral signaling we performed a single-molecule fluorescence analysis of RalGDS and its functional domains (RBD and REMCDC) on the plasma membranes of living HeLa cells. Increased molecular density of RalGDS and RBD, but not REMCDC, was observed on the plasma membrane after EGF stimulation of the cells to induce Ras activation, suggesting that the translocation of RalGDS involves an interaction between the GTP-bound active form of Ras and the RBD of RalGDS. Whereas the RBD played an important role in increasing the association rate constant between RalGDS and the plasma membrane, the REMCDC domain affected the dissociation rate constant from the membrane, which decreased after Ras activation or the hyperexpression of Ral. The Y64 residue of Ras and clusters of RalGDS molecules were involved in this reduction. From these findings, we infer that Ras activation not merely increases the cell-surface density of RalGDS, but actively stimulates the RalGDS-Ral interaction through a structural change in RalGDS and/or the accumulation of Ral, as well as the GTP-Ras/RalGDS clusters, to induce the full activation of Ral.
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