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Regulatory Aspects of the Vacuolar CAT2 Arginine Transporter of S. lycopersicum: Role of Osmotic Pressure and Cations

Authors
  • Cosco, Jessica
  • Regina, Teresa M. R.
  • Scalise, Mariafrancesca
  • Galluccio, Michele
  • Indiveri, Cesare
Publication Date
Feb 19, 2019
Source
MDPI
Keywords
Language
English
License
Green
External links

Abstract

differently, the cations had no effect when included in the internal proteoliposome compartment. This data highlighted an asymmetric regulation of SlCAT2. Cholesteryl hemisuccinate, included in the proteoliposomal membrane, stimulated the SlCAT2 transport activity. The homology model of the protein was built using, as a template, the 3D structure of the amino acid transporter GkApcT. Putative substrate binding residues and cholesterol binding domains were proposed. Altogether, the described results open new perspectives for studying the response of SlCAT2 and, in general, of plant vacuolar transporters to metabolic and environmental changes.

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