The membrane proximal domain of TRPV1 and TRPV2 channels mediates protein–protein interactions and lipid binding in vitro

Pau Doñate-Macián, Elena Álvarez-Marimon, Francesc Sepulcre, José Luis Vázquez-Ibar, Alex Perálvarez-Marín

Research output: Contribution to journalArticleResearch

1 Citation (Scopus)


© 2019 by the authors. Licensee MDPI, Basel, Switzerland. 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.
Original languageEnglish
Article number682
JournalInternational Journal of Molecular Sciences
Publication statusPublished - 1 Jan 2019


  • Biophysics
  • Exocytosis
  • Lipid-protein interactions
  • Protein–protein interactions
  • Transient Receptor Potential (TRP) channels

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