ArticleProceedings of the National Academy of Sciences of the United States of America2013
Transmembrane helix orientation influences membrane binding of the intracellular juxtamembrane domain in Neu receptor peptides.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 66 citations in OpenAlex.
- Lipids regulate epidermal growth factor receptor activation by its ligands.Biochemical Society transactions · 2026Review
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- Therapeutic advances of targeting receptor tyrosine kinases in cancer.Signal transduction and targeted therapy · 2024Review
- How Neuromembrane Lipids Modulate Membrane Proteins: Insights from G-Protein-Coupled Receptors (GPCRs) and Receptor Tyrosine Kinases (RTKs).Cold Spring Harbor perspectives in biology · 2023Review
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- Elucidating activation and deactivation dynamics of VEGFR-2 transmembrane domain with coarse-grained molecular dynamics simulations.PloS one · 2023Article
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- Molecular and clinicopathological characteristics ofFrontiers in oncology · 2022Article
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- CHIP/STUB1 Ubiquitin Ligase Functions as a Negative Regulator of ErbB2 by Promoting Its Early Post-Biosynthesis Degradation.Cancers · 2021Article
- Role of Cholesterol in Transmembrane Dimerization of the ErbB2 Growth Factor Receptor.The Journal of membrane biology · 2021Article
- Driving the catalytic activity of a transmembrane thermosensor kinase.Cellular and molecular life sciences : CMLS · 2020Article
- Membrane receptor activation mechanisms and transmembrane peptide tools to elucidate them.The Journal of biological chemistry · 2020Review
- Understanding Membrane Domain-Partitioning Thermodynamics of Transmembrane Domains with Potential of Mean Force Calculations.The journal of physical chemistry. B · 2019Article
- Interactions of the EphA2 Kinase Domain with PIPs in Membranes: Implications for Receptor Function.Structure (London, England : 1993) · 2018Article
- Lipid-Protein Interplay in Dimerization of Juxtamembrane Domains of Epidermal Growth Factor Receptor.Biophysical journal · 2018Article
- The Dipole Potential Modifies the Clustering and Ligand Binding Affinity of ErbB Proteins and Their Signaling Efficiency.Scientific reports · 2016Article
- Lipid interaction sites on channels, transporters and receptors: Recent insights from molecular dynamics simulations.Biochimica et biophysica acta · 2016Review
- Juxtamembrane contribution to transmembrane signaling.Biopolymers · 2015Review
- Interactions of the EGFR juxtamembrane domain with PIP2-containing lipid bilayers: Insights from multiscale molecular dynamics simulations.Biochimica et biophysica acta · 2015Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The transmembrane (TM) and juxtamembrane (JM) regions of the ErbB family receptor tyrosine kinases connect the extracellular ligand-binding domain to the intracellular kinase domain. Evidence for the role of these regions in the mechanism of receptor dimerization and activation is provided by TM-JM peptides corresponding to the Neu (or rat ErbB2) receptor. Solid-state NMR and fluorescence spectroscopy show that there are tight interactions of the JM sequence with negatively charged lipids, including phosphatidylinositol 4,5-bisphosphate, in TM-JM peptides corresponding to the wild-type receptor sequence. We observe a release of the JM sequence from the negatively charged membrane surface using peptides containing an activating V664E mutation within the TM domain or in peptides engineered to form TM helix dimers with Val664 in the interface. These results provide the basis of a mechanism for coupling ligand binding to kinase activation in the full-length receptor.
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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.