ArticleInternational journal of molecular sciences2019
Oligomeric Architecture of Mouse Activating Nkrp1 Receptors on Living Cells.
Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- NKR-P1A/CD161: A Multifunctional Immune Receptor at the Crossroads of Antitumor Immunity.Biomolecules · 2026Review
- Transmembrane helix interactions regulate oligomerization of the receptor tyrosine kinase EphA2.The Journal of biological chemistry · 2024Article
- Quantitative characterization of tetraspanin 8 homointeractions in the plasma membrane.The Biochemical journal · 2021Article
- Human herpesvirus 8 molecular mimicry of ephrin ligands facilitates cell entry and triggers EphA2 signaling.PLoS biology · 2021Article
- Interactions between Ligand-Bound EGFR and VEGFR2.Journal of molecular biology · 2021Article
- Probing Membrane Protein Association Using Concentration-Dependent Number and Brightness.Angewandte Chemie (International ed. in English) · 2021Article
- The Biased Ligands NGF and NT-3 Differentially Stabilize Trk-A Dimers.Biophysical journal · 2021Article
- The biophysical basis of receptor tyrosine kinase ligand functional selectivity: Trk-B case study.The Biochemical journal · 2020Article
- Quantifying the strength of heterointeractions among receptor tyrosine kinases from different subfamilies: Implications for cell signaling.The Journal of biological chemistry · 2020Article
- The cryo-EM structure of the endocytic receptor DEC-205.The Journal of biological chemistryArticle
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Mouse activating Nkrp1 proteins are commonly described as type II transmembrane receptors with disulfide-linked homodimeric structure. Their function and the manner in which Nkrp1 proteins of mouse strain (C57BL/6) oligomerize are still poorly understood. To assess the oligomerization state of Nkrp1 proteins, mouse activating EGFP-Nkrp1s were expressed in mammalian lymphoid cells and their oligomerization evaluated by Förster resonance energy transfer (FRET). Alternatively, Nkrp1s oligomers were detected by Western blotting to specify the ratio between monomeric and dimeric forms. We also performed structural characterization of recombinant ectodomains of activating Nkrp1 receptors. Nkrp1 isoforms c1, c2 and f were expressed prevalently as homodimers, whereas the Nkrp1a displays larger proportion of monomers on the cell surface. Cysteine-to-serine mutants revealed the importance of all stalk cysteines for protein dimerization in living cells with a major influence of cysteine at position 74 in two Nkrp1 protein isoforms. Our results represent a new insight into the oligomerization of Nkrp1 receptors on lymphoid cells, which will help to determine their function.
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