Abstract
It was recently demonstrated that MCPIP1 is a critical factor that controls inflammation and immune homeostasis; however, the relationship between MCPIP1 and other members of this protein family is largely unknown. Here, we report that MCPIP1 interacts with MCPIP4 to form a protein complex, but acts independently in the 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 the GW-body, which features 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.
Highlights
The post-transcriptional regulation of interleukin-6 (IL-6) production is critical for immune homeostasis
Identification of MCPIP4 as a Monocyte chemotactic protein-induced protein 1 (MCPIP1)-interacting Protein— Previously, we and others have demonstrated that MCPIP1 is crucial to control inflammation and immune homeostasis (10, 11, 24 –26)
Flag-tagged MCPIP1 was transiently expressed in HEK293 cells, and MCPIP1-bound proteins were immunoprecipitated with anti-Flag M2-agarose beads
Summary
The post-transcriptional regulation of interleukin-6 (IL-6) production is critical for immune homeostasis. Results: Monocyte chemotactic protein-induced protein 1 (MCPIP1) and MCPIP4 form a complex but they act independently in regulation of IL-6 mRNA degradation. Significance: The study may help to understand the mechanisms by which MCPIP1 protein family control immune homeostasis. It was recently demonstrated that MCPIP1 is a critical factor that controls inflammation and immune homeostasis; the relationship between MCPIP1 and other members of this protein family is largely unknown. We report that MCPIP1 interacts with MCPIP4 to form a protein complex, but acts independently in the regulation of IL-6 mRNA degradation. 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
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