ArticleMolecular biology of the cell2004
Transmembrane peptides as inhibitors of ErbB receptor signaling.
Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 111 citations in OpenAlex.
- Plexin-B1 and Plexin-B2 play non-redundant roles in GABAergic synapse formation.Molecular and cellular neurosciences · 2024Article
- System-Level Analysis of the Effects of RPTPs on Cellular Signaling Networks.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Transmembrane peptide effects on bacterial membrane integrity and organization.Biophysical journal · 2022Article
- A peptide-derived strategy for specifically targeting the mitochondria and ER of cancer cells: a new approach in fighting cancer.Chemical science · 2022Article
- The emerging complexity of PDGFRs: activation, internalization and signal attenuation.Biochemical Society transactions · 2020Review
- Membrane receptor activation mechanisms and transmembrane peptide tools to elucidate them.The Journal of biological chemistry · 2020Review
- Transmembrane Peptides as a New Strategy to Inhibit Neuraminidase-1 Activation.Frontiers in cell and developmental biology · 2020Article
- Molecular Bases of VEGFR-2-Mediated Physiological Function and Pathological Role.Frontiers in cell and developmental biology · 2020Review
- Transmembrane Peptides as Inhibitors of Protein-Protein Interactions: An Efficient Strategy to Target Cancer Cells?Frontiers in oncology · 2020Review
- Disrupting the transmembrane domain-mediated oligomerization of protein tyrosine phosphatase receptor J inhibits EGFR-driven cancer cell phenotypes.The Journal of biological chemistry · 2019Article
- Targeting trimeric transmembrane domain 5 of oncogenic latent membrane protein 1 using a computationally designed peptide.Chemical science · 2019Article
- De novo designed transmembrane peptides activating the α5β1 integrin.Protein engineering, design & selection : PEDS · 2018Article
- Targeting Intramembrane Protein-Protein Interactions: Novel Therapeutic Strategy of Millions Years Old.Advances in protein chemistry and structural biology · 2018Review
- NMR relaxation parameters of methyl groups as a tool to map the interfaces of helix-helix interactions in membrane proteins.Journal of biomolecular NMR · 2017Article
- Hendra virus fusion protein transmembrane domain contributes to pre-fusion protein stability.The Journal of biological chemistry · 2017Article
- Conformational Changes in the Epidermal Growth Factor Receptor: Role of the Transmembrane Domain Investigated by Coarse-Grained MetaDynamics Free Energy Calculations.Journal of the American Chemical Society · 2016Article
- Drugging Membrane Protein Interactions.Annual review of biomedical engineering · 2016Review
- Role of ErbB Receptors in Cancer Cell Migration and Invasion.Frontiers in pharmacology · 2015Review
- An immunomodulating motif of the HIV-1 fusion protein is chirality-independent: implications for its mode of action.The Journal of biological chemistry · 2013Article
- Drug efflux by a small multidrug resistance protein is inhibited by a transmembrane peptide.Antimicrobial agents and chemotherapy · 2012Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Receptor tyrosine kinases have a single transmembrane (TM) segment that is usually assumed to play a passive role in ligand-induced dimerization and activation of the receptor. However, mutations within some of these receptors, and recent studies with the epidermal growth factor (EGF) and ErbB2 receptors have indicated that interactions between TM domains do contribute to stabilization of ligand-independent and/or ligand-induced receptor dimerization and activation. One consequence of the importance of these interactions is that short hydrophobic peptides corresponding to these domains should act as specific inhibitors. To test this hypothesis, we constructed expression vectors encoding short fusion peptides encompassing native or mutated TM domains of the EGF, ErbB2, and insulin receptors. In human cell lines overexpressing the wild-type EGF receptor or ErbB2, we observed that the peptides are expressed at the cell surface and that they inhibit specifically the autophosphorylation and signaling pathway of their cognate receptor. Identical results were obtained with peptides chemically synthesized. Mechanism of action involves inhibition of dimerization of the receptors as shown by the lack of effects of mutant nondimerizing sequences, completed by density centrifugation and covalent cross-linking experiments. Our findings stress the role of TM domain interactions in ErbB receptor function, and possibly for other single-spanning membrane proteins.
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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.