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Up-Regulation of Amino Acid Transporter SLC6A19 Activity and Surface Protein Abundance by PKB/Akt and PIKfyve
Author(s) -
Evgenii Bogatikov,
Carlos Muñoz,
Tatsiana Pakladok,
Ioana Alesutan,
Manzar Shojaiefard,
Guiscard Seebohm,
Michael Föller,
Mònica Palmada,
Christoph Böhmer,
Stefan Bröer,
Florian Läng
Publication year - 2012
Publication title -
cellular physiology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.486
H-Index - 87
eISSN - 1421-9778
pISSN - 1015-8987
DOI - 10.1159/000343341
Subject(s) - protein kinase b , phosphorylation , microbiology and biotechnology , biochemistry , akt1 , pi3k/akt/mtor pathway , biology , amino acid , chemistry , signal transduction
The amino acid transporter B0AT1 (SLC6A19) accomplishes concentrative cellular uptake of neutral amino acids. SLC6A19 is stimulated by serum- & glucocorticoid-inducible kinase (SGK) isoforms. SGKs are related to PKB/Akt isoforms, which also stimulate several amino acid transporters. PKB/Akt modulates glucose transport in part by phosphorylating and thus activating phosphatidylinositol-3-phosphate-5-kinase (PIKfyve), which fosters carrier protein insertion into the cell membrane. The present study explored whether PKB/Akt and/or PIKfyve stimulate SLC6A19.

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