ArticleOncogene2001
The C-terminal SH3 domain of the adapter protein Grb2 binds with high affinity to sequences in Gab1 and SLP-76 which lack the SH3-typical P-x-x-P core motif.
Article in Oncogene, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 106 citations in OpenAlex.
- Structural and mechanistic insights into the constitutive Themis-Grb2 complex in T cell signalling.Nature communications · 2026Article
- The Caenorhabditis elegans protein SOC-3 permits an alternative mode of signal transduction by the EGL-15 FGF receptor.Developmental biology · 2024Article
- Targeting Grb2 SH3 Domains with Affimer Proteins Provides Novel Insights into Ras Signalling Modulation.Biomolecules · 2024Article
- The Configuration of GRB2 in Protein Interaction and Signal Transduction.Biomolecules · 2024Review
- Allosteric regulation of GRB2 modulates RAS activation.Small GTPases · 2022Article
- Elucidation of protein interactions necessary for the maintenance of the BCR-ABL signaling complex.Cellular and molecular life sciences : CMLS · 2020Article
- Crystal structure of the SH3 domain of growth factor receptor-bound protein 2.Acta crystallographica. Section F, Structural biology communications · 2020Article
- The SH3 domains of the protein kinases ITK and LCK compete for adjacent sites on T cell-specific adapter protein.The Journal of biological chemistry · 2019Article
- The 11-Kilodalton Nonstructural Protein of Human Parvovirus B19 Facilitates Viral DNA Replication by Interacting with Grb2 through Its Proline-Rich Motifs.Journal of virology · 2019Article
- Grb2 carboxyl-terminal SH3 domain can bivalently associate with two ligands, in an SH3 dependent manner.Scientific reports · 2017Article
- Changes in Gab2 phosphorylation and interaction partners in response to interleukin (IL)-2 stimulation in T-lymphocytes.Scientific reports · 2016Article
- PfIRR Interacts with HrIGF-I and Activates the MAP-kinase and PI3-kinase Signaling Pathways to Regulate Glycogen Metabolism in Pinctada fucata.Scientific reports · 2016Article
- SUMOylation of Grb2 enhances the ERK activity by increasing its binding with Sos1.Molecular cancer · 2014Article
- Conformational recognition of an intrinsically disordered protein.Biophysical journal · 2014Article
- An Interaction Library for the FcεRI Signaling Network.Frontiers in immunology · 2014Review
- Current concepts in pediatric Philadelphia chromosome-positive acute lymphoblastic leukemia.Frontiers in oncology · 2014Review
- Novel inhibitors of a Grb2 SH3C domain interaction identified by a virtual screen.Bioorganic & medicinal chemistry · 2013Article
- GRB2-mediated recruitment of THEMIS to LAT is essential for thymocyte development.Journal of immunology (Baltimore, Md. : 1950) · 2013Article
- Protein tyrosine phosphatase-1B regulates the tyrosine phosphorylation of the adapter Grb2-associated binder 1 (Gab1) in the retina.Cell communication and signaling : CCS · 2013Article
- Allostery mediates ligand binding to Grb2 adaptor in a mutually exclusive manner.Journal of molecular recognition : JMR · 2013Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The adapter Grb2 is an important mediator of normal cell proliferation and oncogenic signal transduction events. It consists of a central SH2 domain flanked by two SH3 domains. While the binding specificities of the Grb2 SH2 and N-terminal SH3 domain [Grb2 SH3(N)] have been studied in detail, binding properties of the Grb2 SH3(C) domain remained poorly defined. Gab1, a receptor tyrosine kinase substrate which associates with Grb2 and the c-Met receptor, was previously shown to bind Grb2 via a region which lacks a Grb2 SH3(N)-typical motif (P-x-x-P-x-R). Precipitation experiments with the domains of Grb2 show now that Gab1 can bind stably to the Grb2 SH3(C) domain. For further analyses, Gab1 mutants were generated by PCR to test in vivo residues thought to be crucial for Grb2 SH3(C) binding. The Grb2 SH3(C) binding region of Gab1 has significant homology to a region of the adapter protein SLP-76. Peptides corresponding to epitopes SLP-76, Gab1, SoS and other proteins with related sequences, as well as mutant peptides were synthesized and analysed by tryptophan-fluorescence spectrometry and by in vitro competition experiments. These experiments define a 13 amino acid sequence with the unusual consensus motif P-x-x-x-R-x-x-K-P as required for a stable binding to the SH3(C) domain of Grb2. Additional analyses point to a distinct binding specificity of the Grb2-homologous adapter protein Mona (Gads), indicating that the proteins of the Grb2 adapter family may have partially overlapping, yet distinct protein binding properties.
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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.