Skip to main content
Download PDF
- Main
A catalytically silent FAAH-1 variant drives anandamide transport in neurons
- Fu, Jin;
- Bottegoni, Giovanni;
- Sasso, Oscar;
- Bertorelli, Rosalia;
- Rocchia, Walter;
- Masetti, Matteo;
- Guijarro, Ana;
- Lodola, Alessio;
- Armirotti, Andrea;
- Garau, Gianpiero;
- Bandiera, Tiziano;
- Reggiani, Angelo;
- Mor, Marco;
- Cavalli, Andrea;
- Piomelli, Daniele
Published Web Location
https://doi.org/10.1038/nn.2986Abstract
After its release, the endocannabinoid anandamide is taken up from the synaptic cleft by internalization by neurons and astrocytes. Although several lines of evidence suggest that the anandamide uptake itself is a carrier-mediated diffusion process, the molecular identity of the transporter was unknown until now. Here Fu et al. show that anandamide uptake is mediated by a novel protein named FAAH-like anandamide transporter (FLAT) that is generated as an alternative splicing product of the fatty acid amide hydrolase-1 (Faah) mRNA.
Many UC-authored scholarly publications are freely available on this site because of the UC's open access policies. Let us know how this access is important for you.