Structure of the Cytosolic Portion of the Motor Protein Prestin and Functional Role of the STAS Domain in SLC26/SulP Anion Transporters

Pasqualetto, Elisa; Aiello, R.; Gesiot, Lorenzo; Bonetto, G.; Bellanda, Massimo; Battistutta, Roberto

doi:10.1016/j.jmb.2010.05.013

Cited by 64 publications

(123 citation statements)

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“…Na 36 Cl was from GE Healthcare (Pittsburgh, PA), Na2 35 SO 4 2Ϫ was from PerkinElmer (Waltham, MA), and [ 14 C]oxalate was from NEN-DuPont (now PerkinElmer). Restriction enzymes were from New England Biolabs (Beverly, MA).…”

Section: Methodsmentioning

confidence: 99%

“…Unidirectional 36 Cl Ϫ efflux assays were performed as previously described (51,52). Individual oocytes were injected with 50 nl of 260 mM Na 36 Cl (10,000 -15,000 cpm).…”

Section: Methodsmentioning

confidence: 99%

“…Individual oocytes were injected with 50 nl of 260 mM Na 36 Cl (10,000 -15,000 cpm). After ϳ10 min recovery in Cl Ϫ -free medium (in mM: 96 Na isethionate, 2 K gluconate, 1.8 Ca gluconate, 1 Mg gluconate, 5 HEPES, pH 7.4), 36 Cl Ϫ efflux was initiated by transferring individual oocytes to 6-ml borosilicate glass tubes containing 1 ml ND-96 (in mM: 96 NaCl, 2 KCl, 1.8 CaCl2, 1 MgCl2, 5 HEPES, pH 7.4). At intervals of 3 min, 0.95 ml of this efflux solution was removed and replaced by an equal volume of fresh ND-96.…”

Section: Methodsmentioning

confidence: 99%

“…Bath Cl Ϫ concentration-response curves were generated by fitting 36 Cl Ϫ uptake data to the Michaelis-Menten equation to generate values of K0.5 and Vmax (SigmaPlot v.11). All functional analyses of gpSlc26a6 were with Xenopus oocytes or HEK 293 cells expressing the long NH2-terminal variant polypeptide.…”

Section: Methodsmentioning

confidence: 99%

“…The gpSlc26a11 STAS domain exhibits less interspecies aa sequence conservation than do the STAS domains of Slc26a3 or gpSlc26a6, despite the absence from the Slc26a11 STAS domain of the central "intervening sequence" (INV), believed to be an intrinsically unstructured subdomain (36).The STAS INV subdomain is poorly conserved among Slc26a6 orthologs but highly conserved among Slc26a3 orthologs, along with the other STAS subdomains. The STAS COOH-terminal subdomain of Slc26a11 is also remarkable for lower sequence conservation than evident among species orthologs of gpSlc26a3 and gpSlc26a6.…”

Section: Molecular Cloning Of Slc26a3 Slc26a6 and Slc26a11 Cdnas Frmentioning

confidence: 99%

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SLC26 anion exchangers of guinea pig pancreatic duct: molecular cloning and functional characterization

Stewart

Shmukler

Vandorpe

et al. 2011

American Journal of Physiology-Cell Physiology

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The secretin-stimulated human pancreatic duct secretes HCO3−-rich fluid essential for normal digestion. Optimal stimulation of pancreatic HCO3− secretion likely requires coupled activities of the cystic fibrosis transmembrane regulator (CFTR) anion channel and apical SLC26 Cl−/HCO3− exchangers. However, whereas stimulated human and guinea pig pancreatic ducts secrete ∼140 mM HCO3− or more, mouse and rat ducts secrete ∼40–70 mM HCO3−. Moreover, the axial distribution and physiological roles of SLC26 anion exchangers in pancreatic duct secretory processes remain controversial and may vary among mammalian species. Thus the property of high HCO3− secretion shared by human and guinea pig pancreatic ducts prompted us to clone from guinea pig pancreatic duct cDNAs encoding Slc26a3, Slc26a6, and Slc26a11 polypeptides. We then functionally characterized these anion transporters in Xenopus oocytes and human embryonic kidney (HEK) 293 cells. In Xenopus oocytes, gpSlc26a3 mediated only Cl−/Cl− exchange and electroneutral Cl−/HCO3− exchange. gpSlc26a6 in Xenopus oocytes mediated Cl−/Cl− exchange and bidirectional exchange of Cl− for oxalate and sulfate, but Cl−/HCO3− exchange was detected only in HEK 293 cells. gpSlc26a11 in Xenopus oocytes exhibited pH-dependent Cl−, oxalate, and sulfate transport but no detectable Cl−/HCO3− exchange. The three gpSlc26 anion transporters exhibited distinct pharmacological profiles of 36Cl− influx, including partial sensitivity to CFTR inhibitors Inh-172 and GlyH101, but only Slc26a11 was inhibited by PPQ-102. This first molecular and functional assessment of recombinant SLC26 anion transporters from guinea pig pancreatic duct enhances our understanding of pancreatic HCO3− secretion in species that share a high HCO3− secretory output.

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Section: Methodsmentioning

confidence: 99%

“…Unidirectional 36 Cl Ϫ efflux assays were performed as previously described (51,52). Individual oocytes were injected with 50 nl of 260 mM Na 36 Cl (10,000 -15,000 cpm).…”

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Molecular Cloning Of Slc26a3 Slc26a6 and Slc26a11 Cdnas Frmentioning

confidence: 99%

See 3 more Smart Citations

SLC26 anion exchangers of guinea pig pancreatic duct: molecular cloning and functional characterization

Stewart

Shmukler

Vandorpe

et al. 2011

American Journal of Physiology-Cell Physiology

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Chansporter complexes in cell signaling

Abbott

2017

FEBS Letters

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Ion channels facilitate diffusion of ions across cell membranes for such diverse purposes as neuronal signalling, muscular contraction, and fluid homeostasis. Solute transporters often utilize ionic gradients to move aqueous solutes up their concentration gradient, also fulfilling a wide variety of tasks. Recently, an increasing number of ion channel-transporter (“chansporter”) complexes has been discovered. Chansporter complex formation may overcome what could otherwise be considerable spatial barriers to rapid signal integration and feedback between channels and transporters, the ions and other substrates they transport, and environmental factors to which they must respond. Here, current knowledge in this field is summarized, covering both heterologous expression structure/function findings and potential mechanisms by which chansporter complexes fulfil contrasting roles in cell signalling in vivo.

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Slc26 Family of Anion Transporters in the Gastrointestinal Tract: Expression, Function, Regulation, and Role in Disease

Seidler

Nikolovska

2019

Comprehensive Physiology

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SLC26 family members are multifunctional transporters of small anions, including Cl − , HCO 3 − , sulfate, oxalate, and formate. Most SLC26 isoforms act as secondary (coupled) anion transporters, while others mediate uncoupled electrogenic transport resembling Cl − channels. Of the 11 described SLC26 isoforms, the SLC26A1,2,3,6,7,9,11 are expressed in the gastrointestinal tract, where they participate in salt and water transport, surface pH‐microclimate regulation, affect the microbiome composition, the absorption, and secretion of oxalate and sulfate, and other functions that require further study. Several intestinal or extra‐intestinal diseases are related to SLC26A mutations. Patients with congenital chloride diarrhea (CLD) suffer from Cl − ‐rich acidic diarrhea and systemic alkalosis due to SLC26A3 mutations. Patients with osteochondrodysplastic syndromes experience skeletal defects due to SLC26A2 mutations, resulting in defective sulfate absorption in enterocytes and sulfate uptake in chondrocytes. Because of functional interactions between SLC26 and other proteins, such as the Cl − channel CFTR, some of the intestinal cystic fibrosis manifestations may be attributed to impaired SLC26 isoform localization and function. The altered expression of SLC26 members due to inflammation or operative procedures have important consequences on intestinal transport and barrier function in common diseases as inflammatory bowel disease or bariatric surgery. The present review gives an overview on the current state of knowledge of the intestinally expressed SLC26A isoforms (SLC26A1,2,3,6,7,9,11) from the history of their functional identification, cloning and expression, the insights into their function, interaction partners and regulation gained in heterologous expression systems and Slc26a‐deficient mice, to information about their transcriptional regulation and roles in gastrointestinal disease manifestations. © 2019 American Physiological Society. Compr Physiol 9:839‐872, 2019.

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Structure of the Cytosolic Portion of the Motor Protein Prestin and Functional Role of the STAS Domain in SLC26/SulP Anion Transporters

Cited by 64 publications

References 58 publications

SLC26 anion exchangers of guinea pig pancreatic duct: molecular cloning and functional characterization

SLC26 anion exchangers of guinea pig pancreatic duct: molecular cloning and functional characterization

Chansporter complexes in cell signaling

Slc26 Family of Anion Transporters in the Gastrointestinal Tract: Expression, Function, Regulation, and Role in Disease

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