2. Academic Validation
  3. Monocyte Chemotactic Protein-induced Protein 1 and 4 Form a Complex but Act Independently in Regulation of Interleukin-6 mRNA Degradation

Monocyte Chemotactic Protein-induced Protein 1 and 4 Form a Complex but Act Independently in Regulation of Interleukin-6 mRNA Degradation

  • J Biol Chem. 2015 Aug 21;290(34):20782-20792. doi: 10.1074/jbc.M114.635870.
Shengping Huang 1,  Shufeng Liu 2,  Jia J Fu 1,  T Tony Wang 2,  Xiaolan Yao 3,  Anil Kumar 4,  Gang Liu 5,  Mingui Fu 6
Affiliations

Affiliations

  • 1 Shock/Trauma Research Center & Department of Basic Medical Science, School of Medicine, University of Missouri Kansas City, Kansas City, Missouri 64108.
  • 2 Bioscience Division, SRI International, Harrisonburg, Virginia 22802.
  • 3 Division of Molecular Biology and Biochemistry, School of Biological Science, University of Missouri Kansas City, Kansas City, Missouri 64110.
  • 4 Division of Pharmacology and Toxicology, School of Pharmacy, University of Missouri Kansas City, Kansas City, Missouri 64108.
  • 5 Division of Pulmonary, Allergy, and Critical Care Medicine, University of Alabama at Birmingham, School of Medicine, Birmingham, Alabama 35294.
  • 6 Shock/Trauma Research Center & Department of Basic Medical Science, School of Medicine, University of Missouri Kansas City, Kansas City, Missouri 64108. Electronic address: fum@umkc.edu.
PMID: 26134560 DOI: 10.1074/jbc.M114.635870
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.

Keywords

RNase; inflammation; interleukin; mRNA decay; protein domain; protein-protein interaction.

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