ArticleNature communications2017
Mechanism of SOS PR-domain autoinhibition revealed by single-molecule assays on native protein from lysate.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 60 citations in OpenAlex.
- Reconstitution of Ras-PI3Kγ membrane communication and feedback using light-induced signaling inputs.Nature communications · 2026Article
- Positive cooperativity between RAS-binding and cysteine-rich domains regulates RAF membrane binding kinetics via lateral rebinding.Nature communications · 2026Article
- The BRAF-specific region suppresses cysteine-rich domain-lipid interaction independently of canonical autoinhibition by the 14-3-3 dimer.Protein science : a publication of the Protein Society · 2026Article
- Enzymatic Reactions Dictated by the 2D Membrane Environment.The journal of physical chemistry letters · 2025Article
- Positive feedback in Ras activation by full-length SOS arises from autoinhibition release mechanism.Biophysical journal · 2024Article
- Bimodality in Ras signaling originates from processivity of the Ras activator SOS without deterministic bistability.Science advances · 2024Article
- A NanoCurvS platform for quantitative and multiplex analysis of curvature-sensing proteins.Biomaterials science · 2023Article
- Binding of active Ras and its mutants to the Ras binding domain of PI-3-kinase: A quantitative approach to KAnalytical biochemistry · 2023Article
- PPDPF Promotes the Development of Mutant KRAS-Driven Pancreatic Ductal Adenocarcinoma by Regulating the GEF Activity of SOS1.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Article
- Competition for shared downstream signaling molecules establishes indirect negative feedback between EGFR and EphA2.Biophysical journal · 2022Article
- A two-component protein condensate of the EGFR cytoplasmic tail and Grb2 regulates Ras activation by SOS at the membrane.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Stochasticity and positive feedback enable enzyme kinetics at the membrane to sense reaction size.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Relating cellular signaling timescales to single-molecule kinetics: A first-passage time analysis of Ras activation by SOS.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Liquid-liquid phase separation: a principal organizer of the cell's biochemical activity architecture.Trends in pharmacological sciences · 2021Review
- Critical requirement of SOS1 RAS-GEF function for mitochondrial dynamics, metabolism, and redox homeostasis.Oncogene · 2021Article
- Raf promotes dimerization of the Ras G-domain with increased allosteric connections.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structure and regulation of phospholipase Cβ and ε at the membrane.Chemistry and physics of lipids · 2021Review
- Diffusion-based determination of protein homodimerization on reconstituted membrane surfaces.BMB reports · 2021Review
- Novel regulation of Ras proteins by direct tyrosine phosphorylation and dephosphorylation.Cancer metastasis reviews · 2020Review
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The guanine nucleotide exchange factor (GEF) Son of Sevenless (SOS) plays a critical role in signal transduction by activating Ras. Here we introduce a single-molecule assay in which individual SOS molecules are captured from raw cell lysate using Ras-functionalized supported membrane microarrays. This enables characterization of the full-length SOS protein, which has not previously been studied in reconstitution due to difficulties in purification. Our measurements on the full-length protein reveal a distinct role of the C-terminal proline-rich (PR) domain to obstruct the engagement of allosteric Ras independently of the well-known N-terminal domain autoinhibition. This inhibitory role of the PR domain limits Grb2-independent recruitment of SOS to the membrane through binding of Ras·GTP in the SOS allosteric binding site. More generally, this assay strategy enables characterization of the functional behaviour of GEFs with single-molecule precision but without the need for purification.
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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.