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Abstract
It is recently demonstrated that MCPIP1 is a critical factor that controls inflammation and immune homeostasis, however, the relationship between MCPIP1 and other members in this protein family is largely unknown. Here we report that MCPIP1 interacts with MCPIP4 to form a protein complex but they act independently in regulation of IL-6 mRNA degradation. In an effort to identify MCPIP1-interacting proteins by co-immunoprecipitation (Co-IP) and Mass-spec analysis, MCPIP4 was identified as a MCPIP1-interacting protein, which was further confirmed by Co-IP and mammalian two-hybrid assay. Immunofluorescence staining showed that MCPIP4 was co-localized with MCPIP1 in GW-body, which is featured by GW182 and Argonaute 2. Further studies showed that MCPIP1 and MCPIP4 act independently in regulation of IL-6 mRNA degradation. These results suggest that MCPIP1 and MCPIP4 may additively contribute to control IL-6 production in vivo.