Evolutionary and experimental analyses of inorganic phosphate transporter PiT family reveals two related signature sequences harboring highly conserved aspartic acids critical for sodium‐dependent phosphate transport function of human PiT2

@article{Bttger2005EvolutionaryAE,
  title={Evolutionary and experimental analyses of inorganic phosphate transporter PiT family reveals two related signature sequences harboring highly conserved aspartic acids critical for sodium‐dependent phosphate transport function of human PiT2},
  author={Pernille B{\o}ttger and Lene Juul Pedersen},
  journal={The FEBS Journal},
  year={2005},
  volume={272}
}
The mammalian members of the inorganic phosphate (Pi) transporter (PiT) family, the type III sodium‐dependent phosphate (NaPi) transporters PiT1 and PiT2, have been assigned housekeeping Pi transport functions and are suggested to be involved in chondroblastic and osteoblastic mineralization and ectopic calcification. The PiT family members are conserved throughout all kingdoms and use either sodium (Na+) or proton (H+) gradients to transport Pi. Sequence logo analyses revealed that independent… 
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.
Structure of the sodium-dependent phosphate transporter reveals insights into human solute carrier SLC20
TLDR
The three-dimensional structure of TmPiT provides a framework for understanding PiT dysfunction and for future structure-based drug design and proposes an elevator-like mechanism for sodium and phosphate transport by Tm piT, with the Tm PiT-Na/Pi complex adopting an inward occluded conformation.
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.
Phosphate (Pi)-regulated heterodimerization of the high-affinity sodium-dependent Pi transporters PiT1/Slc20a1 and PiT2/Slc20a2 underlies extracellular Pi sensing independently of Pi uptake
TLDR
It is shown that deletion of PiT1 or PiT2 blunted the Pi-dependent ERK1/2-mediated phosphorylation and subsequent gene up-regulation of the mineralization inhibitors matrix Gla protein and osteopontin, suggesting that both PiTs are necessary for Pi signaling.
Functional PTB phosphate transporters are present in streptophyte algae and early diverging land plants.
TLDR
Land plants inherited two Pi uptake mechanisms - mediated by the PTB and PHT1 proteins, respectively - from their streptophyte algal ancestor, both of which operate in parallel in extant early diverging land plants.
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.
Isolation and Characterization of Three Sodium-Phosphate Cotransporter Genes and Their Transcriptional Regulation in the Grass Carp Ctenopharyngodon idella
TLDR
For the first time, the transcriptional regulatory mechanisms of SLC20s and their responses to Pi offered new insights into the Pi homeostatic regulation and provided the basis for reducing phosphorus discharge into the waters.
Mechanisms of PiT2-loop7 Missense Mutations Induced Pi Dyshomeostasis.
TLDR
It is suggested that missense mutations in PiT2-loop7 can cause Pi dyshomeostasis by affecting the phosphorylation-regulated cell-surface localization ofPiT2, and indicates that increasing theosphorylation levels of PiT 2- loop7 could be a promising strategy for developing PFBC therapies.
Characterization of transport mechanisms and determinants critical for Na+-dependent Pi symport of the PiT family paralogs human PiT1 and PiT2.
TLDR
The results imply that putative transmembrane amino acids E(55) and E(575) are responsible for linking P(i) import to Na(+) transport in PiT2, the first time decoupling of P( i) from Na(+ transport has been demonstrated for a PiT family member.
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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