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Literature summary for 2.7.1.150 extracted from

  • Alesutan, I.S.; Ureche, O.N.; Laufer, J.; Klaus, F.; Zuern, A.; Lindner, R.; Strutz-Seebohm, N.; Tavare, J.M.; Boehmer, C.; Palmada, M.; Lang, U.E.; Seebohm, G.; Lang, F.
    Regulation of the glutamate transporter EAAT4 by PIKfyve (2010), Cell. Physiol. Biochem., 25, 187-194.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
S318A in Xenopus oocytes expressing mammalian excitatory amino acid transporter EAAT4, glutamate induces a current which is significantly enhanced by coexpression of isoform PIKfyve and glucocorticoid inducible kinase SGK1. The stimulating effect of PIKfyve is abrogated by mutation S318A in the SGK consensus sequence of PIKfyve. Coexpression of PIKfyve S318A mutant significantly blunts the stimulating effect of SGK1 on EAAT4 activity Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus Q9Z1T6
-
-

Synonyms

Synonyms Comment Organism
PIKfyve
-
 Mus musculus
PIP5K3
-
 Mus musculus

General Information

General Information Comment Organism
physiological function in Xenopus oocytes expressing mammalian excitatory amino acid transporter EAAT4, glutamate induces a current which is significantly enhanced by coexpression of isoform PIKfyve and glucocorticoid inducible kinase SGK1. This glutamate-induced current is significantly larger than the current in Xenopus oocytes expressing EAAT4 together with either kinase alone. Coexpression of the inactive SGK1 mutant K127N does not significantly alter glutamate-induced current in EAAT4-expressing Xenopus oocytes and abolishes the stimulation of glutamate-induced current by coexpression of isoform PIKfyve. The stimulating effect of PIKfyve is abrogated by mutation S318A in the SGK consensus sequence of PIKfyve. Coexpression of PIKfyve S318A mutant significantly blunts the stimulating effect of SGK1 on EAAT4 activity Mus musculus