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MTOR SLC6A8 (1 - 3 of 3)
PMID: 16466692
Stimulation of the creatine transporter SLC6A8 by the protein kinase mTOR.
Stimulation of ... transporter SLC6A8 by ... kinase mTOR.   (details)

MTOR SLC6A8

Type:  positive regulation
Is this interaction correct?
Yes
No

Comments

PMID: 16466692

Stimulation of the creatine transporter SLC6A8 by the protein kinase mTOR.
Source

Biochemical and biophysical research communications (3/24/2006)

Abstract

Stimulation of the creatine transporter SLC6A8 by the protein kinase mTOR. Cellular accumulation of creatine is accomplished by the Na (+), Cl (-), and creatine transporter CreaT (SLC6A8). The mammalian target of rapamycin (mTOR) is a kinase stimulating cellular nutrient uptake. The present experiments explored whether SLC6A8 is regulated by mTOR. In Xenopus oocytes expressing SLC6A8 but not in water injected oocytes, creatine-induced a current which was significantly enhanced by coexpression of mTOR. Kinetic analysis revealed that mTOR enhanced maximal current without significantly altering affinity. Preincubation of the oocytes for 32 h with rapamycin (50 nM) decreased the creatine-induced current and abrogated its stimulation by mTOR. The effect of mTOR on CreaT was blunted by additional coexpression of the inactive mutant of the serum and glucocorticoid-inducible kinase (K119N) SGK1 and mimicked by coexpression of wild type SGK1. In conclusion, mTOR stimulates the creatine transporter SLC6A8 through mechanisms at least partially shared by the serum and glucocorticoid-inducible kinase SGK1.

... whether SLC6A8 is regulated by mTOR.   (details)

MTOR SLC6A8

Type:  positive regulation
Is this interaction correct?
Yes
No

Comments

PMID: 16466692

Stimulation of the creatine transporter SLC6A8 by the protein kinase mTOR.
Source

Biochemical and biophysical research communications (3/24/2006)

Abstract

Stimulation of the creatine transporter SLC6A8 by the protein kinase mTOR. Cellular accumulation of creatine is accomplished by the Na (+), Cl (-), and creatine transporter CreaT (SLC6A8). The mammalian target of rapamycin (mTOR) is a kinase stimulating cellular nutrient uptake. The present experiments explored whether SLC6A8 is regulated by mTOR. In Xenopus oocytes expressing SLC6A8 but not in water injected oocytes, creatine-induced a current which was significantly enhanced by coexpression of mTOR. Kinetic analysis revealed that mTOR enhanced maximal current without significantly altering affinity. Preincubation of the oocytes for 32 h with rapamycin (50 nM) decreased the creatine-induced current and abrogated its stimulation by mTOR. The effect of mTOR on CreaT was blunted by additional coexpression of the inactive mutant of the serum and glucocorticoid-inducible kinase (K119N) SGK1 and mimicked by coexpression of wild type SGK1. In conclusion, mTOR stimulates the creatine transporter SLC6A8 through mechanisms at least partially shared by the serum and glucocorticoid-inducible kinase SGK1.

PMID: 17982255
PIKfyve in the SGK1 mediated regulation of the creatine transporter SLC6A8.
... that SLC6A8 transport ... is enhanced by mammalian target of rapamycin (mTOR) at ...   (details)

MTOR SLC6A8

Type:  positive regulation
Is this interaction correct?
Yes
No

Comments

PMID: 17982255

PIKfyve in the SGK1 mediated regulation of the creatine transporter SLC6A8.
Source

Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology (2007)

Abstract

PIKfyve in the SGK1 mediated regulation of the creatine transporter SLC6A8. The Na (+), Cl (-), creatine transporter CreaT (SLC6A8) mediates concentrative cellular uptake of creatine into a wide variety of cells. Previous observations disclosed that SLC6A8 transport activity is enhanced by mammalian target of rapamycin (mTOR) at least partially through the serum and glucocorticoid inducible kinase isoforms SGK1 and SGK3. As SLC6A8 does not contain a putative SGK consensus motif, the mechanism linking SGK1 with SLC6A8 activity remained elusive. A candidate kinase is the mammalian phosphatidylinositol-3-phosphate-5-kinase PIKfyve (PIP5K3), which has previously been shown to regulate the glucose transporter GLUT4. The present experiments explored the possibility that SLC6A8 is regulated by PIKfyve. In Xenopus oocytes expressing SLC6A8 but not in water injected oocytes creatine induced a current which was significantly enhanced by coexpression of PIKfyve. The effect of PIKfyve on SLC6A8 was blunted by additional coexpression of the inactive mutant of the serum and glucocorticoid inducible kinase (K127N) SGK1. The stimulating effect of PIKfyve was abrogated by replacement of the serine in the SGK consensus sequence by alanine ((S318A) PIKfyve). Moreover, coexpression of (S318A) PIKfyve blunted the effect of SGK1 on SLC6A8 activity. The observations suggest that SGK1 regulates the creatine transporter SLC6A8 at least partially through phosphorylation and activation of PIKfyve and subsequent formation of PI (3,5) P (2).