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Open AccessCommunication

The Membrane Proximal Domain of TRPV1 and TRPV2 Channels Mediates Protein–Protein Interactions and Lipid Binding In Vitro

1
Biophysics Unit, Department of Biochemistry and Molecular Biology, School of Medicine, Universitat Autònoma de Barcelona, 08193 Cerdanyola del Vallés, Catalonia, Spain
2
Departament d’Enginyeria Agroalimentària i Biotecnologia, Universitat Politècnica de Catalunya, 08860 Barcelona, Catalonia, Spain
3
Institut de Biologie Intégrative de la Cellule, CEA-Saclay, 91191 Gif-sur-Yvette, France
4
Institut des Sciences du Vivant Frédéric-JOLIOT, CEA-Saclay, 91191 Gif-sur-Yvette, France
5
Institut de Neurociències, Universitat Autònoma de Barcelona, 08193 Cerdanyola del Vallés, Catalonia, Spain
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2019, 20(3), 682; https://doi.org/10.3390/ijms20030682
Received: 14 January 2019 / Revised: 30 January 2019 / Accepted: 31 January 2019 / Published: 5 February 2019
Constitutive or regulated membrane protein trafficking is a key cell biology process. Transient receptor potential channels are somatosensory proteins in charge of detecting several physical and chemical stimuli, thus requiring fine vesicular trafficking. The membrane proximal or pre-S1 domain (MPD) is a highly conserved domain in transient receptor potential channels from the vanilloid (TRPV) subfamily. MPD shows traits corresponding to protein-protein and lipid-protein interactions, and protein regulatory regions. We have expressed MPD of TRPV1 and TRPV2 as green fluorescente protein (GFP)-fusion proteins to perform an in vitro biochemical and biophysical characterization. Pull-down experiments indicate that MPD recognizes and binds Soluble N-ethylmaleimide-sensitive factor Attachment Protein Receptors (SNARE). Synchrotron radiation scattering experiments show that this domain does not self-oligomerize. MPD interacts with phosphatidic acid (PA), a metabolite of the phospholipase D (PLD) pathway, in a specific manner as shown by lipid strips and Trp fluorescence quenching experiments. We show for the first time, to the best of our knowledge, the binding to PA of an N-terminus domain in TRPV channels. The presence of a PA binding domain in TRPV channels argues for putative PLD regulation. Findings in this study open new perspectives to understand the regulated and constitutive trafficking of TRPV channels exerted by protein-protein and lipid-protein interactions. View Full-Text
Keywords: Transient Receptor Potential (TRP) channels; exocytosis; biophysics; protein–protein interactions; lipid-protein interactions Transient Receptor Potential (TRP) channels; exocytosis; biophysics; protein–protein interactions; lipid-protein interactions
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MDPI and ACS Style

Doñate-Macián, P.; Álvarez-Marimon, E.; Sepulcre, F.; Vázquez-Ibar, J.L.; Perálvarez-Marín, A. The Membrane Proximal Domain of TRPV1 and TRPV2 Channels Mediates Protein–Protein Interactions and Lipid Binding In Vitro. Int. J. Mol. Sci. 2019, 20, 682. https://doi.org/10.3390/ijms20030682

AMA Style

Doñate-Macián P, Álvarez-Marimon E, Sepulcre F, Vázquez-Ibar JL, Perálvarez-Marín A. The Membrane Proximal Domain of TRPV1 and TRPV2 Channels Mediates Protein–Protein Interactions and Lipid Binding In Vitro. International Journal of Molecular Sciences. 2019; 20(3):682. https://doi.org/10.3390/ijms20030682

Chicago/Turabian Style

Doñate-Macián, Pau; Álvarez-Marimon, Elena; Sepulcre, Francesc; Vázquez-Ibar, José L.; Perálvarez-Marín, Alex. 2019. "The Membrane Proximal Domain of TRPV1 and TRPV2 Channels Mediates Protein–Protein Interactions and Lipid Binding In Vitro" Int. J. Mol. Sci. 20, no. 3: 682. https://doi.org/10.3390/ijms20030682

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