Characterization of transport mechanisms and determinants critical for Na+-dependent Pi symport of the PiT family paralogs human PiT1 and PiT2.

@article{Bttger2006CharacterizationOT,
  title={Characterization of transport mechanisms and determinants critical for Na+-dependent Pi symport of the PiT family paralogs human PiT1 and PiT2.},
  author={Pernille B{\o}ttger and Susanne E. Hede and Morten Grunnet and Boy. Hoyer and Dan Arne Klaerke and Lene Juul Pedersen},
  journal={American journal of physiology. Cell physiology},
  year={2006},
  volume={291 6},
  pages={
          C1377-87
        }
}
The general phosphate need in mammalian cells is accommodated by members of the P(i) transport (PiT) family (SLC20), which use either Na(+) or H(+) to mediate inorganic phosphate (P(i)) symport. The mammalian PiT paralogs PiT1 and PiT2 are Na(+)-dependent P(i) (NaP(i)) transporters and are exploited by a group of retroviruses for cell entry. Human PiT1 and PiT2 were characterized by expression in Xenopus laevis oocytes with (32)P(i) as a traceable P(i) source. For PiT1, the Michaelis-Menten… 
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52 Citations
Highly Influential Citations
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52 Citations

Phosphate transporters: a tale of two solute carrier families.
TLDR
This review focuses on recent advances in the characterization of the transport kinetics, structure-function relationships, and physiological implications of having two distinct Na+/P(i) cotransporter families.
Phosphate transport kinetics and structure-function relationships of SLC34 and SLC20 proteins.
An Externally Accessible Linker Region in the Sodium-Coupled Phosphate Transporter PiT-1 (SLC20A1) is Important for Transport Function
TLDR
The external accessibility of a linker region in PiT-1 was confirmed and sites were identified that determine substrate selectivity and transport function and underscoring the importance of this linker in defining Pi T-1 transport characteristics.
Identification of a Novel Function of PiT1 Critical for Cell Proliferation and Independent of Its Phosphate Transport Activity*♦
TLDR
This study is the first to describe the effects of a Pi transporter in cell proliferation, tumor growth, and cell signaling and shows that modulation of cell proliferation by PiT1 is independent from its transport function because the proliferation ofPiT1-depleted cells can be rescued by non-transporting PiT2 mutants.
Phosphate transporters and their function.
TLDR
Plasma phosphate concentration is maintained within a relatively narrow range by control of renal reabsorption of filtered inorganic phosphate by controlling the transport mechanism of the two kidney-specific SLC34 proteins and of the ubiquitously expressed SLC20 protein (PiT-2).
Evidence for PiT-Type (SLC20) and NaPi-II-Type (SLC34) Transporters in the Rat Choroid Plexus
TLDR
The results indicate that a PiT-type transporter is responsible for Pi transport in the brain choroid plexus and indicate that NaPi-IIb is potentially present in the CP, indicating that the secondary-active, CP transport of phosphate out of the CSF may involve more than one family of solute carrier transporters.
Phosphate transporters of the SLC 20 and SLC 34 families
TLDR
This review summarizes the current knowledge of SLC20 and SLC34 proteins in terms of their basic molecular characteristics, physiological roles, known pathophysiology and pharmacology.
Sodium-Dependent Phosphate Transporter Protein 1 Is Involved in the Active Uptake of Inorganic Phosphate in Nephrocytes of the Kidney and the Translocation of Pi Into the Tubular Epithelial Cells in the Outer Mantle of the Giant Clam, Tridacna squamosa
TLDR
The accumulation of Pi in the kidney of giant clams might be unrelated to limiting the availability of Pi to the symbiotic dinoflagellates to regulate their population.
Arabidopsis ANTR1 Is a Thylakoid Na+-dependent Phosphate Transporter
TLDR
The putative anion transporter 1 from Arabidopsis thaliana was shown to be localized to the chloroplast thylakoid membrane by Western blotting with two different peptide-specific antibodies, demonstrating the function of ANTR1 as a Na+-dependent Pi transporter.
Intestinal phosphate absorption is mediated by multiple transport systems in rats.
TLDR
Evidence is provided of the presence of a new sodium-coupled Pi transporter that uses [Formula: see text] as the preferred substrate and is inhibited by phosphonoformate, and its expression correlates with Pi transport in all assayed conditions.
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TLDR
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