ArticleJournal of virology2001
Transmembrane topology of PiT-2, a phosphate transporter-retrovirus receptor.
Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 68 citations in OpenAlex.
- Computational molecular characterization of a novel SLC20A2 variant associated with primary familial brain calcification.Scientific reports · 2025Article
- Sodium-dependent phosphate transporter PiT1/SLC20A1 as the receptor for the endogenous retroviral envelope syncytin-B involved in mouse placenta formation.Journal of virology · 2024Article
- Mechanisms of PiT2-loop7 Missense Mutations Induced Pi Dyshomeostasis.Neuroscience bulletin · 2023Article
- A guide to plasma membrane solute carrier proteins.The FEBS journal · 2021Review
- Structure of the sodium-dependent phosphate transporter reveals insights into human solute carrier SLC20.Science advances · 2020Article
- Partial reduced Pi transport function of PiT-2 might not be sufficient to induce brain calcification of idiopathic basal ganglia calcification.Scientific reports · 2019Article
- Covalently modified carboxyl side chains on cell surface leads to a novel method toward topology analysis of transmembrane proteins.Scientific reports · 2019Article
- Phosphate (PThe Journal of biological chemistry · 2018Article
- PiT2 regulates neuronal outgrowth through interaction with microtubule-associated protein 1B.Scientific reports · 2017Article
- Glycosylation of solute carriers: mechanisms and functional consequences.Pflugers Archiv : European journal of physiology · 2016Review
- Mapping of the minimal inorganic phosphate transporting unit of human PiT2 suggests a structure universal to PiT-related proteins from all kingdoms of life.BMC biochemistry · 2011Article
- Primate gammaretroviruses require an ancillary factor not required for murine gammaretroviruses to infect BHK cells.Journal of virology · 2011Article
- Identification of a novel function of PiT1 critical for cell proliferation and independent of its phosphate transport activity.The Journal of biological chemistry · 2009Article
- New structural arrangement of the extracellular regions of the phosphate transporter SLC20A1, the receptor for gibbon ape leukemia virus.The Journal of biological chemistry · 2009Article
- Regulation of phosphate transport in proximal tubules.Pflugers Archiv : European journal of physiology · 2009Review
- The Na+-Pi cotransporter PiT-2 (SLC20A2) is expressed in the apical membrane of rat renal proximal tubules and regulated by dietary Pi.American journal of physiology. Renal physiology · 2009Article
- Use of different but overlapping determinants in a retrovirus receptor accounts for non-reciprocal interference between xenotropic and polytropic murine leukemia viruses.Retrovirology · 2005Article
- The central half of Pit2 is not required for its function as a retroviral receptor.Journal of virology · 2004Article
- The SLC20 family of proteins: dual functions as sodium-phosphate cotransporters and viral receptors.Pflugers Archiv : European journal of physiology · 2004Review
- Identification of an extracellular domain within the human PiT2 receptor that is required for amphotropic murine leukemia virus binding.Journal of virology · 2004Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses. Two copies of a homology domain that is found in distantly related species assign these proteins to a large family of phosphate transporters. A current membrane topology model of PiT-1 and PiT-2 predicts 10 transmembrane domains. However, the validity of this model has not been addressed experimentally. We addressed this issue by a comprehensive study of human PiT-2. Evidence was obtained for glycosylation of asparagine 81. Epitope tagging showed that the N- and C-terminal extremities are extracellular. The orientation of C-terminal-truncation mutants expressed in cell-free translation assays and incorporated into microsomal membranes was examined by immunoprecipitation. Data were interpreted with respect to previous knowledge about retrovirus binding sites, to the existence of repeated homology domains, and to predictions made in family members. A model in which PiT-2 has 12 transmembrane domains and extracellular N- and C-terminal extremities is proposed. This model, which differs significantly from previous predictions about PiT-2 topology, may be useful for further investigations of PiT-2 interactions with other proteins and for the understanding of PiT-2 transporter and virus receptor 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.