Alkaline-shifted pH  Sensitivity of AE2c1-mediated Anion Exchange Reveals Novel Regulatory Determinants in the AE2 N-terminal Cytoplasmic Domain

Kurschat, Christine; Shmukler, Boris E.; Jiang, Liang; Wilhelm, Sabine; Kim, Edward H.; Chernova, Marina N.; Kinne, Rolf K. H.; Stewart, Andrew K.; Alper, Seth L.

doi:10.1074/jbc.m509734200

Cited by 36 publications

(49 citation statements)

References 31 publications

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“…Some AE proteins participate in mammalian cell pH regulation, and regulatory motifs have been identified in their cytoplasmic domains (17)(18)(19)(20)(21). The differing sensitivity of OsNRT2.3a and OsNRT2.3b to nitrate transport-elicited changes in cytosolic pH prompted us to look for possible pH-sensing motifs.…”

Section: Resultsmentioning

confidence: 99%

“…Because AE proteins participate in pH regulation (17,31), these motifs may be important for pH sensing in the plant nitrate transporters. In view of the critical importance of histidine residues within pH-sensing motifs (22), we chose the histidine within the VYEAIHKI as a target for single site mutagenesis, and it was changed to an arginine residue.…”

Section: Discussionmentioning

confidence: 99%

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Overexpression of a pH-sensitive nitrate transporter in rice increases crop yields

Fan

Tang

Tan

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

328

234

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Fig. 3. Growth, yield, and NUE of OsNRT2.3b, OsNRT2.3a, and H167R mutation overexpressing lines. (A) Phenotypes and transcriptional and translational expression of OsNRT2.3b-and OsNRT2.3a-overexpressing lines and Nipponbare WT. (B) Phenotypes and transcriptional and translational expression of WT and OsNRT2.3b-H167R mutant-overexpressing lines. (C) Average grain yield and NUE of OsNRT2.3b-(O), OsNRT2.3a-(a-O), and H167R-(H167R) overexpressing lines and WT in field plots. RT-PCR with the specific primers (SI Appendix, Table S10) and Western blot analyses with monoclonal antibodies were performed to identify protein expression levels. NUE = grain yield/applied N fertilizer. Values are mean ± SE (n = 3). a and b above bars indicate significant differences (P < 0.05) between the transgenic lines and WT estimated by one-way ANOVA.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Overexpression of a pH-sensitive nitrate transporter in rice increases crop yields

Fan

Tang

Tan

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

328

234

View full text Add to dashboard Cite

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“…17 Because our targeting construct disrupted only Ae2a, Ae2b1, and Ae2b2 messages, 27 one could expect a possible compensatory increase in the expression of Ae2c transcripts, and more in particular of Ae2c1, which in mouse and rat has been reported to be stomach-specific. 14,17,20,22,26,33 However, quantitation by real-time PCR revealed no increase in the gastric expression level of type c transcripts in the Ae2 a,b Ϫ/Ϫ mice. In fact, the levels of Ae2c1 variant showed lower values in targeted mice compared with wild-type and heterozygous mice (both P Ͻ 0.05; see Figure 1).…”

Section: Transcriptional Expression Of the Ae2 Gene And Other Acid Sementioning

confidence: 99%

“…Interestingly, however, Ae2c1 differs from Ae2a, Ae2b1, and Ae2b2 in its alkaline-shifted pH o(50) sensitivity. 26 Whether Ae2c transcripts are translated into proteins in the stomach remains to be determined, as no immunocytochemical detection of resultant Ae2c polypeptides has yet been performed in this tissue.…”

Section: In Parietal Cells Basolateral Ae2 CLmentioning

confidence: 99%

Inefficient Chronic Activation of Parietal Cells in Ae2−/− Mice

Recalde

Muruzábal

Looije

et al. 2006

The American Journal of Pathology

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In parietal cells, basolateral Ae2 Cl ؊ /HCO 3؊ exchanger (Slc4a2) appears to compensate for luminal H ؉ pumping while providing Cl ؊ for apical secretion. In mouse and rat, mRNA variants Ae2a, Ae2b1, Ae2b2, and Ae2c2 are all found in most tissues (although the latter at very low levels), whereas Ae2c1 is restricted to the stomach. We studied the acid secretory function of gastric mucosa in mice with targeted disruption of Ae2a, Ae2b1, and Ae2b2 (but not Ae2c) isoforms. In the oxyntic mucosa of Ae2 a,b ؊/؊ mice, total Ae2 protein was nearly undetectable, indicating low gastric expression of the Ae2c isoforms. In Ae2 a,b ؊/؊ mice basal acid secretion was normal, whereas carbachol/histamine-stimulated acid secretion was impaired by 70%. These animals showed increased serum gastrin levels and hyperplasia of G

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“…PCR was used to introduce the Kozak consensus sequence CACTCCCGCAGG from mouse Ae2b1 (Lecanda et al 2000) immediately 5′ to the Rv1739c initiator methionine, and the modified DNA was subcloned into the Xenopus oocyte expression vector pXT7. This Kozak sequence is active in Xenopus oocytes (Kurschat et al 2006).…”

Section: Molecular Cloningmentioning

confidence: 99%

Increased sulfate uptake by E. coli overexpressing the SLC26-related SulP protein Rv1739c from Mycobacterium tuberculosis

Zolotarev

Unnikrishnan

Shmukler

et al. 2008

Comparative Biochemistry and Physiology Part A: Molecular &

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Growth and virulence of mycobacteria requires sulfur uptake. The Mycobacterium tuberculosis genome contains, in addition to the ABC sulfate permease cysTWA, three SLC26-related SulP genes of unknown function. We report that induction of Rv1739c expression in E. coli increased bacterial uptake of sulfate, but not Cl − , formate, or oxalate. Uptake was time-dependent, maximal at pH 6.0, and exhibited a K 1/2 for sulfate of 4.0 μM. Na + -independent sulfate uptake was not reduced by bicarbonate, nitrate, or phosphate, but was inhibited by sulfite, selenate, thiosulfate, Nethylmaleimide and carbonyl cyanide 3-chloro-phenylhydrazone. Sulfate uptake was also increased by overexpression of the Rv1739c transmembrane domain, but not of the cytoplasmic C-terminal STAS domain. Mutation to serine of the three cysteine residues of Rv1739c did not affect magnitude, pH-dependence, or pharmacology of sulfate uptake. Expression of Rv1739c in a M. bovis BCG strain lacking the ABC sulfate permease subunit CysA could not complement sulfate auxotrophy. Moreover, inducible expression of Rv1739c in an E. coli strain lacking CysA did not increase sulfate uptake by intact cells. Our data show that facilitation of bacterial sulfate uptake by Rv1739c requires CysA and its associated sulfate permease activity, and suggest that Rv1739c may be a CysTWAdependent sulfate transporter.

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Alkaline-shifted pH Sensitivity of AE2c1-mediated Anion Exchange Reveals Novel Regulatory Determinants in the AE2 N-terminal Cytoplasmic Domain

Cited by 36 publications

References 31 publications

Overexpression of a pH-sensitive nitrate transporter in rice increases crop yields

Overexpression of a pH-sensitive nitrate transporter in rice increases crop yields

Inefficient Chronic Activation of Parietal Cells in Ae2−/− Mice

Increased sulfate uptake by E. coli overexpressing the SLC26-related SulP protein Rv1739c from Mycobacterium tuberculosis

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