title: Monocyte Chemotactic Protein-induced Protein 1 and 4 Form a Complex but Act Independently in Regulation of Interleukin-6 mRNA Degradation.
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.
authors.affiliation: Shock/Trauma Research Center & Department of Basic Medical Science, School of Medicine, University of Missouri Kansas City, Kansas City, Missouri 64108.
authors.forename: Shengping
authors.initials: S
authors.lastname: Huang
authors.affiliation: Bioscience Division, SRI International, Harrisonburg, Virginia 22802.
authors.forename: Shufeng
authors.initials: S
authors.lastname: Liu
authors.affiliation: Shock/Trauma Research Center & Department of Basic Medical Science, School of Medicine, University of Missouri Kansas City, Kansas City, Missouri 64108.
authors.forename: Jia J
authors.initials: JJ
authors.lastname: Fu
authors.affiliation: Bioscience Division, SRI International, Harrisonburg, Virginia 22802.
authors.forename: T
authors.initials: T
authors.lastname: Tony Wang
authors.affiliation: Division of Molecular Biology and Biochemistry, School of Biological Science, University of Missouri Kansas City, Kansas City, Missouri 64110.
authors.forename: Xiaolan
authors.initials: X
authors.lastname: Yao
authors.affiliation: Division of Pharmacology and Toxicology, School of Pharmacy, University of Missouri Kansas City, Kansas City, Missouri 64108.
authors.forename: Anil
authors.initials: A
authors.lastname: Kumar
authors.affiliation: Division of Pulmonary, Allergy, and Critical Care Medicine, University of Alabama at Birmingham, School of Medicine, Birmingham, Alabama 35294.
authors.forename: Gang
authors.initials: G
authors.lastname: Liu
authors.affiliation: 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.
authors.forename: Mingui
authors.initials: M
authors.lastname: Fu
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019556:COS Cells; D018797:Cell Cycle Proteins; D002460:Cell Line; D002522:Chlorocebus aethiops; D004720:Endonucleases; D004722:Endoribonucleases; D005786:Gene Expression Regulation; D057809:HEK293 Cells; D006367:HeLa Cells; D006801:Humans; D047468:Immunoprecipitation; D015850:Interleukin-6 / Q000235:genetics / Q000378:metabolism*; D008264:Macrophages / Q000166:cytology / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D010957:Plasmids / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D011506:Proteins / Q000235:genetics / Q000378:metabolism*; D020871:RNA Stability / Q000235:genetics*; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D012260:Ribonucleases / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism*; D020798:Two-Hybrid System Techniques
chemical_list: D018797:Cell Cycle Proteins; C508600:IL6 protein, human; D015850:Interleukin-6; D011506:Proteins; D012333:RNA, Messenger; D011994:Recombinant Proteins; D014157:Transcription Factors; D004720:Endonucleases; D004722:Endoribonucleases; D012260:Ribonucleases; C510646:ZC3H12A protein, human; C489862:ZC3H12D protein, human
keywords: RNase; inflammation; interleukin; mRNA decay; protein domain; protein-protein interaction