Phosphate transport processes in eukaryotic cells

Wehrle, Janna P.; Pedersen, Peter L.

doi:10.1007/bf01871006

Cited by 50 publications

(20 citation statements)

References 126 publications

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“…These properties ofGlvr-i and Ram-i indicate that they mediate the coupled influx of a stoichiometric excess of sodium relative to phosphate. This result is in agreement with the general finding that the electrochemical gradient of sodium is the major driving force for phosphate uptake across the plasma membrane of animal cells, while phosphate uptake in prokaryotes, plant cells, and mitochondria is driven by a proton gradient (26). Mammalian cell internal phosphate levels (75 milliequivalents per liter) are maintained at about 10-fold higher levels than external levels (4 milliequivalents per liter) in opposition to an electrochemical gradient that favors anion movement out of cells.…”

Section: Methodssupporting

confidence: 92%

Cell-surface receptors for gibbon ape leukemia virus and amphotropic murine retrovirus are inducible sodium-dependent phosphate symporters.

Kavanaugh

Miller

Zhang

et al. 1994

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

564

461

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Cell surface receptors for gibbon ape leukemia virus (Glvr-1) and marine amphotropic retrovirus (Ram-i) Ram-i (10) and human Glvr-1 (7) cDNAs were cloned into pGEM-7Z (Promega) with their 5' ends adjacent to the SP6 promoter. For mRNA synthesis, the plasmids were linearized and transcribed with SP6 polymerase in the presence of m7G(5')ppp(5')G caps according to the manufacturer's directions (Pharmacia). Xenopus laevis oocytes were injected with 50 nl of mRNA (1 ng/nl) or with an equal volume of H20 and were incubated for 4-6 days at 17'C; then two-microelectrode voltage-clamp recordings or radiolabel uptake assays were performed at room temperature as described (23).Abbreviations: GALV, gibbon ape leukemia virus; Glvr-1, cell surface receptor for GALV; Ram-i, cell surface receptor for amphotropic murine retrovirus; HIV, human immunodeficiency virus; MLV, murine leukemia virus; Mo-MLV, Moloney MLV.

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Section: Methodssupporting

confidence: 92%

Cell-surface receptors for gibbon ape leukemia virus and amphotropic murine retrovirus are inducible sodium-dependent phosphate symporters.

Kavanaugh

Miller

Zhang

et al. 1994

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

564

461

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“…It should be noted that the binding site for CAT is located in the cytosol side of the ADP/ATP translocase [20]. be rationalized, considering that Pi is a necessary component for the electrophoretic uptake of Ca 2÷ [21]; in addition, the increased phosphate accumulation conduces to the formation of insoluble Ca-phosphate deposits [22] that stimulate Ca 2÷ retention.…”

Section: Discussionmentioning

confidence: 99%

On the mechanism by which 6‐ketocholestanol protects mitochondria against uncoupling‐induced Ca²⁺ efflux

et al. 1996

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This work shows that 6-ketocholestanol (kCh) inhibits the effect of carbonyl cyanide-m-chlorophenyl hydrazone (CCP) on mitochondrial Ca 2÷ efflux. Such an effect proved to be caused by diminution of membrane fluidity, therefore, it is affected by the incubation temperature. Furthermore, kCh reversed CCPinduced Ca 2+ efflux depending on the accumulation of phosphate. It is also shown that kCh enhances the effect of carboxyatractyloside on membrane permeability transition.

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“…The mitochondrial phosphate carrier (PIC) 1 catalyzes transport of inorganic phosphate into the mitochondrial matrix where the phosphate is utilized for phosphorylating ADP to ATP (LaNoue and Schoolwerth, 1984;Wohlrab, 1986;Wehrle and Pedersen, 1989;Krä mer andPalmieri, 1989, 1992). The function of the PIC was described as P i Ϫ /H ϩ symport, respectively, P i Ϫ /OH Ϫ antiport.…”

mentioning

confidence: 99%

“…The function of the PIC was studied after purification from various kinds of mitochondria (for reviews see Wohlrab (1986), Wehrle and Pedersen (1989), and Krä mer and Palmieri (1989)) and reconstitution into proteoliposomes (Wohlrab, 1980;De Pinto et al, 1982;Wehrle and Pedersen, 1982). PIC catalyzes both homologous P i Ϫ /P i Ϫ as well as heterologous P i Ϫ /OH Ϫ antiport with high activity (Wohlrab and Flowers, 1982;Stappen andKrä mer, 1993, 1994).…”

mentioning

confidence: 99%

The Reversible Antiport-Uniport Conversion of the Phosphate Carrier from Yeast Mitochondria Depends on the Presence of a Single Cysteine

Schroers

Krämer

Wohlrab

1997

Journal of Biological Chemistry

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Wild type and mutant phosphate carriers (PIC) fromSaccharomyces cerevisiae mitochondria were expressed in Escherichia coli as inclusion bodies, solubilized, purified, and optimally reconstituted into liposomal membranes. This PIC can function as coupled antiport (P i ؊ / P i ؊ antiport and P i ؊ net transport, i.e. P i ؊ /OH ؊ antiport) and uncoupled uniport (mercuric chloride-induced P i ؊ efflux). The basic kinetic properties of these three transport modes were analyzed. The kinetic properties closely resemble those of the reconstituted PIC from beef heart mitochondria. A competitive inhibitor of phosphate transport by the PIC, phosphonoformic acid, was used to establish functional overlap between the the physiological transport modes and the induced efflux mode. Replacement mutants were used to relate the reversible switch from antiport to uniport to a specific residue of the carrier. There are only three cysteines in the yeast PIC. They are at positions 28, 134, and 300 and were replaced by serine, both individually and in combinations. Cysteine 300 near the C-terminal loop and cysteine 134 located within the third transmembrane segment are accessible to bulky hydrophilic reagents from the cytosolic side, whereas cysteine 28 within the first transmembrane segment is not. None of the three cysteines is relevant to the two antiport modes. Cysteine 134 was identified to be the major target of bulky SH reagents, that lead to complete inactivation of the physiological transport modes. The reversible conversion between coupled antiport and uncoupled uniport of the PIC depends on the presence of one single cysteine (cysteine 28) in the PIC monomer, i.e. two cysteines in the functionally active dimer. The consequences of this result with respect to a functional model of the carrier protein are discussed.

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Phosphate transport processes in eukaryotic cells

Cited by 50 publications

References 126 publications

Cell-surface receptors for gibbon ape leukemia virus and amphotropic murine retrovirus are inducible sodium-dependent phosphate symporters.

Cell-surface receptors for gibbon ape leukemia virus and amphotropic murine retrovirus are inducible sodium-dependent phosphate symporters.

On the mechanism by which 6‐ketocholestanol protects mitochondria against uncoupling‐induced Ca²⁺ efflux

The Reversible Antiport-Uniport Conversion of the Phosphate Carrier from Yeast Mitochondria Depends on the Presence of a Single Cysteine

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Phosphate transport processes in eukaryotic cells

Cited by 50 publications

References 126 publications

Cell-surface receptors for gibbon ape leukemia virus and amphotropic murine retrovirus are inducible sodium-dependent phosphate symporters.

Cell-surface receptors for gibbon ape leukemia virus and amphotropic murine retrovirus are inducible sodium-dependent phosphate symporters.

On the mechanism by which 6‐ketocholestanol protects mitochondria against uncoupling‐induced Ca2+ efflux

The Reversible Antiport-Uniport Conversion of the Phosphate Carrier from Yeast Mitochondria Depends on the Presence of a Single Cysteine

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On the mechanism by which 6‐ketocholestanol protects mitochondria against uncoupling‐induced Ca²⁺ efflux