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Pathway Description
EPO Signaling Pathway
Homo sapiens
Protein Pathway
Created: 2018-08-01
Last Updated: 2019-08-16
The hormone erythropoietin, is a 166 amino acid protein with an apparent molecular weight in its native form of 39,000 Da. The molecule is heavily glycosylated since its mass derived from its amino acid content is 18,398. The selective interaction of a hormone with its target cells is usually mediated by cell membrane receptors specific for the particular hormone. Erythropoietin-responsive cells have a trypsin-sensitive receptor for the hormone which requires protein synthesis for its maintenance. Erythropoietin-responsive cells can interact with other hematopoietic growth factors, and such interactions may lead to competition for pathway-specific differentiation, particularly under conditions of high cell density. The amino-terminal region of the hormone is not involved in receptor binding.
References
EPO Signaling Pathway References
Kuhrt D, Wojchowski DM: Emerging EPO and EPO receptor regulators and signal transducers. Blood. 2015 Jun 4;125(23):3536-41. doi: 10.1182/blood-2014-11-575357. Epub 2015 Apr 17.
Pubmed: 25887776
Ma C, Cheng F, Wang X, Zhai C, Yue W, Lian Y, Wang Q: Erythropoietin Pathway: A Potential Target for the Treatment of Depression. Int J Mol Sci. 2016 May 6;17(5). pii: ijms17050677. doi: 10.3390/ijms17050677.
Pubmed: 27164096
Wu P, Zhang N, Wang X, Zhang C, Li T, Ning X, Gong K: The erythropoietin/erythropoietin receptor signaling pathway promotes growth and invasion abilities in human renal carcinoma cells. PLoS One. 2012;7(9):e45122. doi: 10.1371/journal.pone.0045122. Epub 2012 Sep 18.
Pubmed: 23028796
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Pubmed: 15534001
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Pubmed: 7719937
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Pubmed: 14702039
Glockner G, Scherer S, Schattevoy R, Boright A, Weber J, Tsui LC, Rosenthal A: Large-scale sequencing of two regions in human chromosome 7q22: analysis of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17 genes. Genome Res. 1998 Oct;8(10):1060-73. doi: 10.1101/gr.8.10.1060.
Pubmed: 9799793
Kim AR, Ulirsch JC, Wilmes S, Unal E, Moraga I, Karakukcu M, Yuan D, Kazerounian S, Abdulhay NJ, King DS, Gupta N, Gabriel SB, Lander ES, Patiroglu T, Ozcan A, Ozdemir MA, Garcia KC, Piehler J, Gazda HT, Klein DE, Sankaran VG: Functional Selectivity in Cytokine Signaling Revealed Through a Pathogenic EPO Mutation. Cell. 2017 Mar 9;168(6):1053-1064.e15. doi: 10.1016/j.cell.2017.02.026.
Pubmed: 28283061
Jacobs K, Shoemaker C, Rudersdorf R, Neill SD, Kaufman RJ, Mufson A, Seehra J, Jones SS, Hewick R, Fritsch EF, et al.: Isolation and characterization of genomic and cDNA clones of human erythropoietin. Nature. 1985 Feb 28-Mar 6;313(6005):806-10. doi: 10.1038/313806a0.
Pubmed: 3838366
Friedman AD, Nimbalkar D, Quelle FW: Erythropoietin receptors associate with a ubiquitin ligase, p33RUL, and require its activity for erythropoietin-induced proliferation. J Biol Chem. 2003 Jul 18;278(29):26851-61. doi: 10.1074/jbc.M210039200. Epub 2003 May 13.
Pubmed: 12746455
Winkelmann JC, Penny LA, Deaven LL, Forget BG, Jenkins RB: The gene for the human erythropoietin receptor: analysis of the coding sequence and assignment to chromosome 19p. Blood. 1990 Jul 1;76(1):24-30.
Pubmed: 2163695
Jones SS, D'Andrea AD, Haines LL, Wong GG: Human erythropoietin receptor: cloning, expression, and biologic characterization. Blood. 1990 Jul 1;76(1):31-5.
Pubmed: 2163696
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Pubmed: 2167438
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Pubmed: 11780052
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Pubmed: 15489334
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Pubmed: 9326218
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Pubmed: 15805263
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Pubmed: 7665165
Yi TL, Cleveland JL, Ihle JN: Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13. Mol Cell Biol. 1992 Feb;12(2):836-46. doi: 10.1128/mcb.12.2.836.
Pubmed: 1732748
Shen SH, Bastien L, Posner BI, Chretien P: A protein-tyrosine phosphatase with sequence similarity to the SH2 domain of the protein-tyrosine kinases. Nature. 1991 Aug 22;352(6337):736-9. doi: 10.1038/352736a0.
Pubmed: 1652101
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