ArticleArchives of biochemistry and biophysics2010
Assembly of the Sos1-Grb2-Gab1 ternary signaling complex is under allosteric control.
Article in Archives of biochemistry and biophysics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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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
13 citing papers in PubMed, 21 citations in OpenAlex.
- Article
- The role of CRAF in cancer progression: from molecular mechanisms to precision therapies.Nature reviews. Cancer · 2024Review
- Intrinsically disordered proteins play diverse roles in cell signaling.Cell communication and signaling : CCS · 2022Review
- Allosteric regulation of GRB2 modulates RAS activation.Small GTPases · 2022Article
- Subcellular Dynamic Immunopatterning of Cytosolic Protein Complexes on Microstructured Polymer Substrates.ACS sensors · 2021Article
- Rapid Quantification of Protein-Ligand Binding viaBiophysical journal · 2020Article
- Inhibition of prenylated KRAS in a lipid environment.PloS one · 2017Article
- Conformational recognition of an intrinsically disordered protein.Biophysical journal · 2014Article
- Receptor tyrosine kinase (RTK) signalling in the control of neural stem and progenitor cell (NSPC) development.Molecular neurobiology · 2014Review
- Allostery mediates ligand binding to Grb2 adaptor in a mutually exclusive manner.Journal of molecular recognition : JMR · 2013Article
- Bivalent binding drives the formation of the Grb2-Gab1 signaling complex in a noncooperative manner.The FEBS journal · 2012Article
- Multivalent binding and facilitated diffusion account for the formation of the Grb2-Sos1 signaling complex in a cooperative manner.Biochemistry · 2012Article
- Rule-based modeling: a computational approach for studying biomolecular site dynamics in cell signaling systems.Wiley interdisciplinary reviews. Systems biology and medicineReview
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Allostery has evolved as a form of local communication between interacting protein partners allowing them to quickly sense changes in their immediate vicinity in response to external cues. Herein, using isothermal titration calorimetry (ITC) in conjunction with circular dichroism (CD) and macromolecular modeling (MM), we show that the binding of Grb2 adaptor--a key signaling molecule involved in the activation of Ras GTPase--to its downstream partners Sos1 guanine nucleotide exchange factor and Gab1 docker is under tight allosteric regulation. Specifically, our findings reveal that the binding of one molecule of Sos1 to the nSH3 domain allosterically induces a conformational change within Grb2 such that the loading of a second molecule of Sos1 onto the cSH3 domain is blocked and, in so doing, allows Gab1 access to the cSH3 domain in an exclusively non-competitive manner to generate the Sos1-Grb2-Gab1 ternary signaling complex.
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Registered trials
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.