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NAK Is Recruited to the TNFR1 Complex in a TNFα-dependent Manner and Mediates the Production of RANTES

Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 279, Issue: 51, Page: 53266-53271
2004
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Article Description

Tumor necrosis factor α (TNFα) is a proinflammatory cytokine with pleiotropic immunological and biological activities. TNFα signaling is triggered by the engagement of soluble TNFα to two types of cell surface receptors, TNFR1 and TNFR2. This recruits cytosolic proteins to the intracellular domains of the receptors and initiates signaling to downstream effectors. In this study, we used a proteomic approach to identify these cytosolic proteins from affinity-purified, endogenous TNFα·TNFR complexes in human myelomonocytic U937 cells. Seven proteins were identified, including TRADD, TRAP2, and TRAF2, which are three proteins known to be recruited to TNFα receptors. NAK, RasGAP3, TRCP1, and TRCP2 were also identified. We further showed that NAK is recruited to TNFR1 in a temporally regulated and TNFα-dependent manner and that it mediates the TNFα-induced production of the chemokine RANTES ( r egulated on a ctivation n ormal T cell e xpressed and s ecreted). These data demonstrate that NAK is a component of the TNFα·TNFR1 signaling complex and confirm the physiological role of NAK in the TNFα-mediated response.

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