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The transmembrane domain structure of TNFR1 suppresses ligand-independent autoactivation but is not required for TNF-induced signaling
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DOI：10.1126/scisignal.adz0203.png)
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Abstract
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Signaling by the cytokine TNF mediates immune responses to infections, and its dysregulation underlies numerous inflammatory disorders. Binding of trimeric TNF to its receptor TNFR1 stimulates signaling by trimeric and higher-order TNFR1. Noting that the transmembrane domains (TMDs) of other TNFR superfamily members support ligand-dependent receptor activation, Wang et al. investigated signaling by variant TNFRs expressing engineered TMDs that enforced monomeric to tetrameric receptor structures. Rather than contributing to TNF-stimulated signaling, associations between TMDs prevented ligand-independent TNFR1 activation. This approach may provide insights into structure-function relationships of similar receptors. —John F. Foley
Keywords:
TNFR1
TNF
transmembrane domain
receptor activation
signaling pathway
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