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The full-length interleukin-33 (FLIL33)-importin-5 interaction does not regulate nuclear localization of FLIL33 but controls its intracellular degradation Protein Synthesis and Degradation
Human mature IL-33 is a member of the IL-1 family and a potent regulator of immunity through its pro-T helper cell 2 activity. Its precursor form, full-length interleukin-33 (FLIL33), is an intranuclear protein in many cell types, including fibroblasts, and its intracellular levels can change in response to stimuli. However, the mechanisms controlling the nuclear localization of FLIL33 or its stability in cells are not understood. Here, we identified importin-5 (IPO5), a member of the importin family of nuclear transport proteins, as an intracellular binding partner of FLIL33. By overexpressing various FLIL33 protein segme...
Source: Journal of Biological Chemistry - December 29, 2017 Category: Chemistry Authors: Andrew Clerman, Zahid Noor, Rita Fishelevich, Virginia Lockatell, Brian S. Hampton, Nirav G. Shah, Mariah V. Salcedo, Nevins W. Todd, Sergei P. Atamas, Irina G. Luzina Tags: Cell Biology Source Type: research

E6-AP/UBE3A Ubiquitinates SOX9 Cell Biology
SOX9 is a transcription factor that acts as a key regulator at various stages of cartilage differentiation. There is ample evidence that intracellular SOX9 protein levels are tightly regulated both by sumoylation and by degradation through the ubiquitin-proteasome pathway. Using a proteomics approach, here we report the identification of a SOX9-binding protein, E6-AP/UBE3A, that may act as a ubiquitin ligase toward Sox9. E6-AP bound SOX9 through the region consisting mostly of its high mobility group domain in vitro. In nuclear lysates, FLAG-tagged E6-AP coprecipitated with Sox9 and its high mobility group domain. This fin...
Source: Journal of Biological Chemistry - December 6, 2013 Category: Chemistry Authors: Hattori, T., Kishino, T., Stephen, S., Eberspaecher, H., Maki, S., Takigawa, M., de Crombrugghe, B., Yasuda, H. Tags: Protein Synthesis and Degradation Source Type: research