Evidence for new homotypic and heterotypic interactions between transmembrane helices of proteins involved in receptor tyrosine kinase and neuropilin signaling
| Autor: | Dominique Bagnard, Cécile Blanchard, Pierre Hubert, Paul Sawma, Lise Roth, Gérard Crémel, Jean-Pierre Duneau, James N. Sturgis, Emmanuelle Bouveret |
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| Přispěvatelé: | Laboratoire d'ingénierie des systèmes macromoléculaires (LISM), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale, Immuno-Rhumatologie Moléculaire, Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Aix Marseille Université (AMU), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Strasbourg (UNISTRA) |
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Models
Molecular animal structures Neuropilins Two-hybrid screening Blotting Western Molecular Sequence Data Nerve Tissue Proteins Neural Cell Adhesion Molecule L1 Receptors Cell Surface Protein Structure Secondary Receptor tyrosine kinase Structural Biology Two-Hybrid System Techniques Protein Interaction Mapping Neuropilin 1 Neuropilin Humans [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Amino Acid Sequence Molecular Biology Sequence Homology Amino Acid biology Cell Membrane Plexin Receptor Protein-Tyrosine Kinases Neuropilin-1 Neuropilin-2 Protein Structure Tertiary Cell biology Transmembrane domain Microscopy Fluorescence Biochemistry embryonic structures biology.protein Protein Multimerization Signal transduction Protein Binding |
| Zdroj: | Journal of Molecular Biology Journal of Molecular Biology, Elsevier, 2014, 426 (24), pp.4099--111. ⟨10.1016/j.jmb.2014.10.007⟩ Journal of Molecular Biology, 2014, 426 (24), pp.4099--111. ⟨10.1016/j.jmb.2014.10.007⟩ |
| ISSN: | 0022-2836 1089-8638 |
| DOI: | 10.1016/j.jmb.2014.10.007⟩ |
| Popis: | International audience; Signaling in eukaryotic cells frequently relies on dynamic interactions of single-pass membrane receptors involving their transmembrane (TM) domains. To search for new such interactions, we have developed a bacterial two-hybrid system to screen for both homotypic and heterotypic interactions between TM helices. We have explored the dimerization of TM domains from 16 proteins involved in both receptor tyrosine kinase and neuropilin signaling. This study has revealed several new interactions. We found that the TM domain of Mucin-4, a putative intramembrane ligand for erbB2, dimerizes not only with erbB2 but also with all four members of the erbB family. In the Neuropilin/Plexin family of receptors, we showed that the TM domains of Neuropilins 1 and 2 dimerize with themselves and also with Plexin-A1, Plexin-B1, and L1CAM, but we were unable to observe interactions with several other TM domains notably those of members of the VEGF receptor family. The potentially important Neuropilin 1/Plexin-A1 interaction was confirmed using a surface plasmon resonance assay. This work shows that TM domain interactions can be highly specific. Exploring further the propensities of TM helix-helix association in cell membrane should have important practical implications related to our understanding of the structure-function of bitopic proteins' assembly and subsequent function, especially in the regulation of signal transduction. |
| Databáze: | OpenAIRE |
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