Ribosomal protein S19
Lua error in Module:Infobox_gene at line 33: attempt to index field 'wikibase' (a nil value). 40S ribosomal protein S19 is a protein that in humans is encoded by the RPS19 gene.[1][2]
Contents
Function
Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit. The protein belongs to the S19E family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.[2]
Clinical significance
Mutations in this gene cause Diamond-Blackfan anemia (DBA), a constitutional erythroblastopenia characterized by absent or decreased erythroid precursors, in a subset of patients. This suggests a possible extra-ribosomal function for this gene in erythropoietic differentiation and proliferation, in addition to its ribosomal function. Higher expression levels of this gene in some primary colon carcinomas compared to matched normal colon tissues has been observed.[2]
Interactions
Ribosomal protein S19 has been shown to interact with basic fibroblast growth factor.[3] RPS19 is also secreted extracellularly and its extracellular oligomers (crosslinked by the transglutaminase Coagulation factor XIII) is also known to bind and probably inhibit Macrophage migration inhibitory factor; though S19 oligomers themselves share MCIP's function as another very strong macrophage chemoattractant and bind to anaphylotoxin C5 receptor[4]
References
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- ↑ Molecular Basis of Cell and Developmental Biology: Ana-Maria Filip, Jörg Klug, Sevil Cayli, Suada Fröhlich, Tamara Henke, Philipp Lacher, Regina Eickhoff, Patrick Bulau, Monika Linder, Christine Carlsson-Skwirut, Lin Leng, Richard Bucala, Sandra Kraemer, Jürgen Bernhagen, and Andreas Meinhardt. Ribosomal Protein S19 Interacts with Macrophage Migration Inhibitory Factor and Attenuates Its Pro-inflammatory Function J. Biol. Chem. 2009 284: 7977-7985. First Published on January 20, 2009, doi:10.1074/jbc.M808620200
Further reading
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External links
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