ArticleBiophysical journal2013
The association of polar residues in the DAP12 homodimer: TOXCAT and molecular dynamics simulation studies.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Membrane-Based Assembly and Interactions in Immune Receptors.Chemical reviews · 2026Review
- Packing of apolar amino acids is not a strong stabilizing force in transmembrane helix dimerization.Biophysical journal · 2025Article
- Pilot Screening of TREM1 Inhibitors in Cell-Based Reporter Assays Reflecting TREM1/DAP12 Receptor Assembly and Functionality.ACS chemical neuroscience · 2025Article
- Elucidation of the molecular interactions that enable stable assembly and structural diversity in multicomponent immune receptors.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The structural basis for membrane assembly of immunoreceptor signalling complexes.Journal of molecular modeling · 2019Article
- Combination of Cα-H Hydrogen Bonds and van der Waals Packing Modulates the Stability of GxxxG-Mediated Dimers in Membranes.Journal of the American Chemical Society · 2017Article
- TREM2-Ligand Interactions in Health and Disease.Journal of molecular biology · 2017Review
- Critical residues and motifs for homodimerization of the first transmembrane domain of the plasma membrane glycoprotein CD36.The Journal of biological chemistry · 2017Article
- Screening for transmembrane association in divisome proteins using TOXGREEN, a high-throughput variant of the TOXCAT assay.Biochimica et biophysica acta · 2016Article
- Transmembrane Complexes of DAP12 Crystallized in Lipid Membranes Provide Insights into Control of Oligomerization in Immunoreceptor Assembly.Cell reports · 2015Article
- Dimerization of the EphA1 receptor tyrosine kinase transmembrane domain: Insights into the mechanism of receptor activation.Biochemistry · 2014Article
- Cholesterol modulates the dimer interface of the β₂-adrenergic receptor via cholesterol occupancy sites.Biophysical journal · 2014Article
- Molecular dynamic simulation of the self-assembly of DAP12-NKG2C activating immunoreceptor complex.PloS one · 2014Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dimerization of the transmembrane (TM) adaptor protein DAP12 plays a key role in mediating activation signals through TM-TM association with cell-surface receptors. Herein, we apply the TOXCAT assay and molecular dynamics simulation to analyze dynamics and dimerization of the TM helix of DAP12 in the membrane bilayer. In the TOXCAT assay, we performed site-specific mutagenesis of potential dimerization motifs in the DAP12 TM domain. Instead of the common GxxxG dimerization motif, mutating either of the polar residues Asp-50 and Thr-54 significantly decreased the TOXCAT signal for the dimerization of DAP12 TM domain. Furthermore, through the conformational difference between wild-type and mutant DAP12 TM homodimers, a combined coarse-grained and atomistic molecular dynamics simulation has identified both Asp-50 and Thr-54 at the dimerization interface. The experimental and computational results of the DAP12 TM dimer are in excellent agreement with the previously reported NMR structure obtained in detergent micelles. Such a combination of dynamics simulation and cell-based experiments can be applied to produce insights at the molecular level into the TM-TM association of many other transmembrane proteins.
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