ArticleJournal of virology1999
Modulation of phosphate uptake and amphotropic murine leukemia virus entry by posttranslational modifications of PIT-2.
Article in Journal of virology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
17 citing papers in PubMed, 44 citations in OpenAlex.
- Modulation of Intestinal Phosphate Transport in Young Goats Fed a Low Phosphorus Diet.International journal of molecular sciences · 2021Article
- PiT2 regulates neuronal outgrowth through interaction with microtubule-associated protein 1B.Scientific reports · 2017Article
- Macropinocytosis is the entry mechanism of amphotropic murine leukemia virus.Journal of virology · 2015Article
- A novel analytical method for in vivo phosphate tracking.FEBS letters · 2006Article
- Use of replication-competent retroviral vectors in an immunocompetent intracranial glioma model.Neurosurgical focus · 2006Article
- Caveola-dependent endocytic entry of amphotropic murine leukemia virus.Journal of virology · 2005Article
- The SLC20 family of proteins: dual functions as sodium-phosphate cotransporters and viral receptors.Pflugers Archiv : European journal of physiology · 2004Review
- Relationship between SU subdomains that regulate the receptor-mediated transition from the native (fusion-inhibited) to the fusion-active conformation of the murine leukemia virus glycoprotein.Journal of virology · 2002Article
- Genetic and biochemical analyses of receptor and cofactor determinants for T-cell-tropic feline leukemia virus infection.Journal of virology · 2002Article
- Apical barriers to airway epithelial cell gene transfer with amphotropic retroviral vectors.Gene therapy · 2002Article
- Pit2 assemblies at the cell surface are modulated by extracellular inorganic phosphate concentration.Journal of virology · 2002Article
- Transmembrane topology of PiT-2, a phosphate transporter-retrovirus receptor.Journal of virology · 2001Article
- Activation of membrane fusion by murine leukemia viruses is controlled in cis or in trans by interactions between the receptor-binding domain and a conserved disulfide loop of the carboxy terminus of the surface glycoprotein.Journal of virology · 2001Article
- Subcellular redistribution of Pit-2 P(i) transporter/amphotropic leukemia virus (A-MuLV) receptor in A-MuLV-infected NIH 3T3 fibroblasts: involvement in superinfection interference.Journal of virology · 2000Article
- A comprehensive approach to mapping the interacting surfaces of murine amphotropic and feline subgroup B leukemia viruses with their cell surface receptors.Journal of virology · 2000Article
- Activation of a cell entry pathway common to type C mammalian retroviruses by soluble envelope fragments.Journal of virology · 2000Article
- Effects of Npt2 gene ablation and low-phosphate diet on renal Na(+)/phosphate cotransport and cotransporter gene expression.The Journal of clinical investigation · 1999Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PIT-2 is a type III sodium phosphate cotransporter and the receptor for amphotropic murine leukemia viruses. We have investigated the expression and the functions of a tagged version of PIT-2 in CHO cells. PIT-2 remained equally abundant at the cell surface within 6 h following variation of the phosphate supply. In contrast, the efficiency of phosphate uptake and retrovirus entry was inversely related to the extracellular phosphate concentration, indicating that PIT-2 activities are modulated by posttranslational modifications of cell surface molecules induced by phosphate. Conformational changes of PIT-2 contribute to both activities, as shown by the inhibitory effect of sulfhydryl reagents known as inhibitors of type II cotransporters. A physical association of PIT-2 with actin was demonstrated. Modifications of the actin network were induced by variations of the concentrations of extracellular phosphate, cytochalasin D, or lysophosphatidic acid. They revealed that the formation of actin stress fibers determines the cell surface distribution of PIT-2, the internalization of the receptor in response to virus binding, and the capacity to process retrovirus entry. Thus, the presence of PIT-2 at the cell surface is not sufficient to ensure phosphate transport and susceptibility to amphotropic retrovirus infection. Further activation of cell surface PIT-2 molecules is required for these functions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.