Feedback inhibition of pro-inflammatory cytokine-mediated signalling is essential for preventing chronic inflammation. Crosstalk between cytokine signalling pathways occurs at multiple levels; for example, interleukin-1β (IL-1β) inhibits IL-6-mediated signalling by acting at IL-6 target gene promoters, by regulating expression of the IL-6 feedback inhibitor SOCS3 and by suppressing IL-6-induced activation of the transcriptional activator STAT3. On page 947, Fred Schaper, Heike Hermanns and colleagues shed light on the molecular details of this latter mechanism. They first show that inhibition of IL-6-mediated STAT3 activation by IL-1β requires activation of the p38 MAPK signalling pathway. Second, IL-1β triggers increased internalisation and degradation of the gp130 subunit of the IL-6 receptor (which also forms receptors for other IL-6-family cytokines). Third, IL-1β-induced gp130 internalisation requires phosphorylation of Ser782 in the cytoplasmic domain of gp130. Fourth, the authors identify MAPK-activated kinase 2 (MK2; a downstream target of p38) as the kinase that phosphorylates gp130 Ser782. Finally, the authors show that TNFα and cellular stress also induce this novel inhibitory pathway of cytokine crosstalk.