Separation of zinc-dependent and zinc-independent events during early LPS-stimulated TLR4 signaling in macrophage cells |
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Authors: | Ying Wan Michael J. Petris Scott C. Peck |
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Affiliation: | 1. Department of Biochemistry, University of Missouri, Columbia, MO 65211, USA;2. Department of Nutrition and Exercise Physiology, University of Missouri, Columbia, MO 65211, USA;3. Christopher S. Bond Life Sciences Center, University of Missouri, Columbia, MO 65211, USA |
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Abstract: | Free zinc is required for proper lipopolysaccharide (LPS)-stimulated signaling, but potential sites of action in the pathway have not been defined. In this work, we provide in vitro and ex vivo evidence that zinc is not required for phosphorylation or ubiquitylation of IRAK1, a kinase functioning early in the TLR4 pathway. However, degradation of ubiquitylated IRAK1 occurred via a zinc-dependent, proteasome-independent pathway. These results provide evidence of a novel site of action for zinc during TLR4-mediated inflammatory responses. |
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Keywords: | Zinc LPS Macrophage Signaling Proteasome-independent degradation |
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