Disease relevance of SLC5A11

• RESULTS: No association between SLC5A11, ISYNA1, and SLC39A4 and spina bifida was shown, chi2SLC5A11=0.016, P=0.90; chi2SYNA1=1.52, P=0.22; chi2SLC39A4=0.016, P=0.90; and degrees of freedom (df)=1 [1].
• Transgenic potato plants carrying a fusion between the KST1 promoter and the E. coli uidA (beta-glucuronidase) reporter gene revealed promoter activity in guard cells and in flowers [2].

High impact information on SLC5A11

• Electrophysiological investigations on the voltage-gated, inward rectifying K+ channel in guard cell protoplasts from Solanum tuberosum (KST1), and the kst1 gene product expressed in Xenopus oocytes revealed that pH dependence is an intrinsic property of the channel protein [3].
• Among the single mutants, replacement of the pore histidine, which is highly conserved in plant K+ channels, increased or even inverted the pH sensitivity of KST1 [3].
• The expressed protein, which we have named SMIT2, cotransports myo-inositol with a K(m) of 120 microm and displays a current-voltage relationship similar to that seen with SMIT (now called SMIT1) [4].
• Based on previous publications, the tissue distribution of SMIT2 is different from that of SMIT1, and the existence of this second cotransporter may explain much of the heterogeneity that has been reported for inositol transport [4].
• SMIT2 exhibits stereospecific cotransport of both d-glucose and d-xylose but does not transport fucose [4].

Chemical compound and disease context of SLC5A11

• We investigated the biochemical concentrations of these nutrients and polymorphisms in the myo-inositol transporter SLC5A11, myo-inositol synthase ISYNA1, and zinc transporter SLC39A4 in association with spina bifida risk [1].

Biological context of SLC5A11

• Maternal glucose concentrations were comparable for the SLC5A11 genotypes [1].
• Due to its broad expression in human tissues, the human KST1 gene could be involved in several other diseases mapped to human chromosome 16p12-p11 [5].
• An almost identical high Cs+ sensitivity (IC50 = 90 microM) was found for the potato guard-cell K+in channel KST1 after expression in insect cells [6].
• The KST1 gene encodes a K+ influx channel of guard cells in potato, and was therefore chosen as a model to study regulation of guard cell-specific gene expression [2].

Anatomical context of SLC5A11

• In contrast, expression of an inwardly rectifying K+ channel from guard cells (kst1) and of a plasma membrane H(+)-ATPase (pha2) was reduced to 26% and 36%, respectively, of the expression in watered controls [7].

Associations of SLC5A11 with chemical compounds

• Moreover, maternal SLC5A11 544C > T polymorphism contributes to the serum myo-inositol concentration [1].

Other interactions of SLC5A11

• In mothers, fathers, and spina bifida children polymorphisms determined were SLC5A11 (544C > T), ISYNA1 (1029A > G), and SLC39A4 (1069C > T) [1].
• At least three, and up to six, Na+-dependent glucose transporters (SGLT1-SGLT6; gene name SLC5A) have been identified [8].

Analytical, diagnostic and therapeutic context of SLC5A11

• A detailed dissection of the KST1 promoter led to the discovery of two independent small TATA box-proximal regulatory units, each of which was sufficient to direct guard cell-specific gene transcription [2].

References