STRAP Acts as a Scaffolding Protein in Controlling the TLR2/4 Signaling Pathway

Hyunbin D. Huh, Eun A. Ra, Taeyun A. Lee, Sujin Kang, Areum Park, Eunhye Lee, Junhee L. Choi, Eunji Jang, Ji Eun Lee, Sungwook Lee, Boyoun Park

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8 Citations (Scopus)


The WD40-repeat protein serine/threonine kinase receptor-associated protein (STRAP) is involved in the regulation of several biological processes, including cell proliferation and apoptosis, in response to various stresses. Here, we show that STRAP is a new scaffold protein that functions in Toll-like receptor (TLR)-mediated immune responses. STRAP specifically binds transforming growth factor β-activated kinase 1 (TAK1) and Iκ B kinase alpha (IKKα) along with nuclear factor-κ B (NF-κ B) subunit p65, leading to enhanced association between TAK1, IKKα, and p65, and subsequent facilitation of p65 phosphorylation and nuclear translocation. Consequently, the depletion of STRAP severely impairs interleukin-6 (IL-6), tumor necrosis factor alpha (TNF-α), and IL-1β production, whereas its overexpression causes a significant increase in the secretion of these pro-inflammatory cytokines by TLR2 or TLR4 agonist-stimulated macrophages. Notably, STRAP translocates to the nucleus and subsequently binds to NF-κ B at later times after lipopolysaccharide (LPS) stimulation, resulting in prolonged IL-6 mRNA production. Moreover, the C-terminal region of STRAP is essential for its functional activity in facilitating IL-6 production. Collectively, these observations suggest that STRAP acts as a scaffold protein that positively contributes to innate host defenses against pathogen infections.

Original languageEnglish
Article number38849
JournalScientific reports
Publication statusPublished - 2016 Dec 9

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© The Author(s) 2016.

All Science Journal Classification (ASJC) codes

  • General


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