Tlr4: central component of the sole mammalian LPS sensor.
Mutations of the mouse Lps locus abolish responses to lipopolysaccharide (LPS). Positional cloning work has revealed that Lps encodes the Toll-like receptor 4 (Tlr4), which functions as the transmembrane component of the LPS receptor complex, an unduplicated pathway for the detection of endotoxin. The structurally related protein Tlr2 makes no contribution to LPS signal transduction.
Beutler
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Department of Internal Medicine, Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75235-9050, USA. beutler@howie.swmed.edu
D000483:Alleles; D029721:Drosophila Proteins; D005799:Genes, Dominant; D005808:Genes, Recessive; D019476:Insect Proteins / Q000235:genetics; D018950:Lipopolysaccharide Receptors / Q000235:genetics / Q000378:metabolism*; D008070:Lipopolysaccharides / Q000276:immunology*; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism*; D018448:Models, Immunological; D011956:Receptors, Cell Surface / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction; D051195:Toll-Like Receptor 2; D051197:Toll-Like Receptor 4; D051193:Toll-Like Receptors
D029721:Drosophila Proteins; D019476:Insect Proteins; D018950:Lipopolysaccharide Receptors; D008070:Lipopolysaccharides; D008562:Membrane Glycoproteins; D011956:Receptors, Cell Surface; C068721:Tl protein, Drosophila; D051195:Toll-Like Receptor 2; D051197:Toll-Like Receptor 4; D051193:Toll-Like Receptors