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

International Journal of Molecular Sciences
Jessica CoscoCesare Indiveri

Abstract

Many proteins are localized at the vacuolar membrane, but most of them are still poorly described, due to the inaccessibility of this membrane from the extracellular environment. This work focused on the characterization of the CAT2 transporter from S. lycopersicum (SlCAT2) that was previously overexpressed in E. coli and reconstituted in proteoliposomes for transport assay as [³H]Arg uptake. The orientation of the reconstituted transporter has been attempted and current data support the hypothesis that the protein is inserted in the liposome in the same orientation as in the vacuole. SlCAT2 activity was dependent on the pH, with an optimum at pH 7.5. SlCAT2 transport activity was stimulated by the increase of internal osmolality from 0 to 175 mOsmol while the activity was inhibited by the increase of external osmolality. K⁺, Na⁺, and Mg2+ present on the external side of proteoliposomes at physiological concentrations, inhibited the transport activity; 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 m...Continue Reading

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Citations

Feb 16, 2020·International Journal of Molecular Sciences·Mariafrancesca Scalise, Cesare Indiveri
Oct 9, 2020·Scientific Reports·Jessica CoscoCesare Indiveri

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Methods Mentioned

BETA
size exclusion chromatography

Software Mentioned

ArgusLab
Clustal Omega
Grafit
Planaria
MolProbity

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