ArticleProceedings of the National Academy of Sciences of the United States of America1994
Mutational analysis of a critical signaling domain of the human interleukin 4 receptor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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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Who cites it
10 citing papers in PubMed, 46 citations in OpenAlex.
- Temporal phosphoproteomic analysis of VEGF-A signaling in HUVECs: an insight into early signaling events associated with angiogenesis.Journal of cell communication and signaling · 2023Article
- In silico mutational analysis and identification of stability centers in human interleukin-4.Molecular biology research communications · 2018Article
- Pressuromodulation at the cell membrane as the basis for small molecule hormone and peptide regulation of cellular and nuclear function.Journal of translational medicine · 2015Article
- Regulation of inflammation by interleukin-4: a review of "alternatives".Journal of leukocyte biology · 2012Review
- Design of conditionally active STATs: insights into STAT activation and gene regulatory function.Molecular and cellular biology · 1999Article
- Interleukin-4-specific signal transduction events are driven by homotypic interactions of the interleukin-4 receptor alpha subunit.The EMBO journal · 1996Article
- The murine DUB-1 gene is specifically induced by the betac subunit of interleukin-3 receptor.Molecular and cellular biology · 1996Article
- Distinct signal transduction through the tyrosine-containing domains of the granulocyte colony-stimulating factor receptor.The EMBO journal · 1995Article
- Cloning of murine Stat6 and human Stat6, Stat proteins that are tyrosine phosphorylated in responses to IL-4 and IL-3 but are not required for mitogenesis.Molecular and cellular biology · 1995Article
- Direct evidence of a heterotrimeric complex of human interleukin-4 with its receptors.Protein science : a publication of the Protein Society · 1995Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The human interleukin 4 receptor (hIL-4R) is a member of a superfamily of cytokine receptors defined by conserved features of their extracellular domains. The intracellular domains of the hIL-4R and of other members of this family lack any recognizable enzymatic motifs, though ligand-dependent tyrosine phosphorylation of these receptors has been observed. Recent studies have suggested that serine-rich and acidic domains within the cytoplasmic portions of cytokine receptors might be required for signal transduction. Using deletion and truncation mutants of the hIL-4R, we have explored an essential 39-amino acid signaling domain that is rich in acidic amino acid residues and in serine residues that form consensus phosphorylation sites for known serine/threonine kinases. To assess the contribution of these motifs to signaling, we engineered site-directed mutants of these residues. Surprisingly, cells expressing mutant hIL-4R lacking either the serine or the acidic amino acids retain the ability of cells expressing the wild-type receptor to proliferate in hIL-4. Furthermore, receptors in which all six cytoplasmic tyrosines are absent can function, suggesting that tyrosine phosphorylation of the receptor may be an epiphenomenon rather than a requisite event in signaling.
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