Abstract
The 58-kDa microspherule protein (MSP58) was initially shown to interact with the nu-cleolar protein p120, a proliferation-associated protein. Earlier studies had proposed a role for MSP58 in the regulation of gene transcription as well as in cellular transfor-mation. We conducted yeast two-hybrid screening using MSP58 as a bait and identified several interacting partners. Here, we identified a novel RING finger gene, which en-codes a protein identical to TRIM family proteins as a MSP58-binding protein. The in-teraction between MSP58 and this proteinwas further validated by co-immunoprecipitation assays in mammalian cells. TRIM proteins could form the scaf-fold and define compartment to host many proteins involved in sumoylation or ubiquiti-nation. Immunofluorescence staining indicated that this protein recruits MSP58 to nu-clear speckles. We further demonstrated that MSP58 regulates this protein-mediated transcription attenuation. Notably, another TRIM family protein, TRIM27, have been reported to form a complex with MSP58 and UBF in the nucleolus, where they play a direct transactivating role on ribosomal gene transcription. Further studies are required to understand the molecular mechanisms of MSP58 and this protein complex in protein post-translational modifications and transcriptional regulation.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
