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SASH1 is a scaffold molecule in endothelial TLR4 signaling.

Dauphinee S.M., Clayton A., Hussainkhel A., Yang C., Park Y.J., Fuller M.E., Blonder J., Veenstra T.D., Karsan A.

Recognition of microbial products by TLRs is critical for mediating innate immune responses to invading pathogens. In this study, we identify a novel scaffold protein in TLR4 signaling called SAM and SH3 domain containing protein 1 (SASH1). Sash1 is expressed across all microvascular beds and functions as a scaffold molecule to independently bind TRAF6, TAK1, IκB kinase α, and IκB kinase β. This interaction fosters ubiquitination of TRAF6 and TAK1 and promotes LPS-induced NF-κB, JNK, and p38 activation, culminating in increased production of proinflammatory cytokines and increased LPS-induced endothelial migration. Our findings suggest that SASH1 acts to assemble a signaling complex downstream of TLR4 to activate early endothelial responses to receptor activation.

J. Immunol. 191:892-901(2013) [PubMed] [Europe PMC]

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