ArticleBiophysical journal2010
Self-association of models of transmembrane domains of ErbB receptors in a lipid bilayer.
Article in Biophysical journal, 2010. 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, 44 citations in OpenAlex.
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- Spontaneous Dimerization and Distinct Packing Modes of Transmembrane Domains in Receptor Tyrosine Kinases.Biochemistry · 2024Article
- Spontaneous Dimerization and Distinct Packing Modes of Transmembrane Domains in Receptor Tyrosine Kinases.bioRxiv : the preprint server for biology · 2024Article
- Structural basis of dimerization of chemokine receptors CCR5 and CXCR4.Nature communications · 2023Article
- Role of Cholesterol in Transmembrane Dimerization of the ErbB2 Growth Factor Receptor.The Journal of membrane biology · 2021Article
- Addressing the Excessive Aggregation of Membrane Proteins in the MARTINI Model.Journal of chemical theory and computation · 2021Article
- Tunicamycin induces ER stress and inhibits tumorigenesis of head and neck cancer cells by inhibiting N-glycosylation.American journal of translational research · 2020Article
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- Effect of Membrane Composition on Receptor Association: Implications of Cancer Lipidomics on ErbB Receptors.The Journal of membrane biology · 2018Review
- Fast Calculation of Protein-Protein Binding Free Energies Using Umbrella Sampling with a Coarse-Grained Model.Journal of chemical theory and computation · 2018Article
- RPN2 promotes colorectal cancer cell proliferation through modulating the glycosylation status of EGFR.Oncotarget · 2017Article
- Death Receptor 5 Activation Is Energetically Coupled to Opening of the Transmembrane Domain Dimer.Biophysical journal · 2017Article
- An Ensemble-Based Protocol for the Computational Prediction of Helix-Helix Interactions in G Protein-Coupled Receptors using Coarse-Grained Molecular Dynamics.Journal of chemical theory and computation · 2017Article
- Article
- Lipid interaction sites on channels, transporters and receptors: Recent insights from molecular dynamics simulations.Biochimica et biophysica acta · 2016Review
- Free Energy Landscape of Lipid Interactions with Regulatory Binding Sites on the Transmembrane Domain of the EGF Receptor.The journal of physical chemistry. B · 2016Article
- 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
- Membrane-Mediated Oligomerization of G Protein Coupled Receptors and Its Implications for GPCR Function.Frontiers in physiology · 2016Review
- N-Glycosylation as determinant of epidermal growth factor receptor conformation in membranes.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Association of transmembrane (TM) helices is facilitated by the close packing of small residues present along the amino-acid sequence. Extensive studies have established the role of such small residue motifs (GxxxG) in the dimerization of Glycophorin A (GpA) and helped to elucidate the association of TM domains in the epidermal growth factor family of receptors (ErbBs). Although membrane-mediated interactions are known to contribute under certain conditions to the dimerization of proteins, their effect is often considered nonspecific, and any potential dependence on protein sequence has not been thoroughly investigated. We recently reported that the association of GpA is significantly assisted by membrane-induced contributions as quantified in different lipid bilayers. Herein we extend our studies to explore the origin of these effects and quantify their magnitude using different amino-acid sequences in the same lipid environment. Using a coarse-grained model that accounts for amino-acid specificity, we perform extensive parallel Monte Carlo simulations of ErbB homodimerization in dipalmitoyl-phosphatidylcholine lipid bilayers. A detailed characterization of dimer formation and estimates of the free energy of association reveal that the TM domains show a significant affinity to self-associate in lipid bilayers, in qualitative agreement with experimental findings. The presence of GxxxG motifs enhances favorable protein-protein interactions at short separations. However, the lipid-induced attraction presents a more complex character than anticipated. Depending on the interfacial residues, lipid-entropic contributions support a decrease of separation or a parallel orientation to the membrane normal, with important implications for protein function.
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