ArticleThe EMBO journal1999
Activation of the erythropoietin receptor by the gp55-P viral envelope protein is determined by a single amino acid in its transmembrane domain.
Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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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
20 citing papers in PubMed, 58 citations in OpenAlex.
- Article
- Biologically Active Ultra-Simple Proteins Reveal Principles of Transmembrane Domain Interactions.Journal of molecular biology · 2019Article
- Transmembrane Protein Aptamer Induces Cooperative Signaling by the EPO Receptor and the Cytokine Receptor β-Common Subunit.iScience · 2019Article
- Single methyl groups can act as toggle switches to specify transmembrane Protein-protein interactions.eLife · 2017Article
- Article
- Activation of the N-terminally truncated form of the Stk receptor tyrosine kinase Sf-Stk by Friend virus-encoded gp55 is mediated by cysteine residues in the ecotropic domain of gp55 and the extracellular domain of Sf-Stk.Journal of virology · 2010Article
- Construction and genetic selection of small transmembrane proteins that activate the human erythropoietin receptor.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- The bovine papillomavirus E5 protein and the PDGF beta receptor: it takes two to tango.Virology · 2009Review
- Ligand-independent homomeric and heteromeric complexes between interleukin-2 or -9 receptor subunits and the gamma chain.The Journal of biological chemistry · 2008Article
- Protein-protein interactions in the membrane: sequence, structural, and biological motifs.Structure (London, England : 1993) · 2008Review
- Role of erythropoietin receptor signaling in Friend virus-induced erythroblastosis and polycythemia.Blood · 2006Article
- Modulation of cell function by small transmembrane proteins modeled on the bovine papillomavirus E5 protein.Oncogene · 2005Review
- Helix packing and orientation in the transmembrane dimer of gp55-P of the spleen focus forming virus.Biophysical journal · 2005Article
- Expression and function of chemokines during viral infections: from molecular mechanisms to in vivo function.Journal of leukocyte biology · 2003Review
- Ligand-independent oligomerization of cell-surface erythropoietin receptor is mediated by the transmembrane domain.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Disruption of TGF-beta growth inhibition by oncogenic ras is linked to p27Kip1 mislocalization.Oncogene · 2000Article
- Article
- Stem cell generation and choice of fate: role of cytokines and cellular microenvironment.Journal of cellular and molecular medicineArticle
- Transmembrane helix-helix interactions involved in ErbB receptor signaling.Cell adhesion & migrationReview
- Single-spanning transmembrane domains in cell growth and cell-cell interactions: More than meets the eye?Cell adhesion & migrationReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The spleen focus forming virus (SFFV) gp55-P envelope glycoprotein specifically binds to and activates murine erythropoietin receptors (EpoRs) coexpressed in the same cell, triggering proliferation of erythroid progenitors and inducing erythroleukemia. Here we demonstrate specific interactions between the single transmembrane domains of the two proteins that are essential for receptor activation. The human EpoR is not activated by gp55-P but by mutation of a single amino acid, L238, in its transmembrane sequence to its murine counterpart serine, resulting in its ability to be activated. The converse mutation in the murine EpoR (S238L) abolishes activation by gp55-P. Computational searches of interactions between the membrane-spanning segments of murine EpoR and gp55-P provide a possible explanation: the face of the EpoR transmembrane domain containing S238 is predicted to interact specifically with gp55-P but not gp55-A, a variant which is much less effective in activating the murine EpoR. Mutational studies on gp55-P M390, which is predicted to interact with S238, provide additional support for this model. Mutation of M390 to isoleucine, the corresponding residue in gp55-A, abolishes activation, but the gp55-P M390L mutation is fully functional. gp55-P is thought to activate signaling by the EpoR by inducing receptor oligomerization through interactions involving specific transmembrane residues.
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Registered trials
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.