title: SRG3/mBAF155 stabilizes the SWI/SNF-like BAF complex by blocking CHFR mediated ubiquitination and degradation of its major components.
abstract: The murine SWI/SNF-like BAF complex is an ATP-dependent chromatin remodeling complex that functions as a transcriptional regulator in cell proliferation, differentiation and development. The SWI/SNF-like BAF complex consists of several components including core subunits such as BRG1, BAF155/SRG3, BAF47/SNF5/INI1, and BAF170. We have previously shown that the interaction between SRG3/mBAF155 and other components of the complex stabilizes them by attenuating their proteasomal degradation. However, it has not been known how the major components of the SWI/SNF-like BAF complex such as BRG1, SNF5, and BAF60a are targeted for the ubiquitination and degradation, and how SRG3/mBAF155 protects them from the degradation process. Here we report that CHFR interacts with BRG1, SNF5, and BAF60a of the SWI/SNF-like BAF complex and ubiquitinates them to target for degradation through a proteasome-mediated pathway, and that SRG3/mBAF155 stabilizes these components by blocking their interaction with CHFR.
authors.affiliation: Research Center for Functional Cellulomics, Department of Biological Sciences, Institute for Molecular Biology and Genetics, Seoul National University, Seoul 151-742, Republic of Korea.
authors.forename: Inkyung
authors.initials: I
authors.lastname: Jung
authors.forename: Dong H
authors.initials: DH
authors.lastname: Sohn
authors.forename: Jinwook
authors.initials: J
authors.lastname: Choi
authors.forename: Joo Mi
authors.initials: JM
authors.lastname: Kim
authors.forename: Shin
authors.initials: S
authors.lastname: Jeon
authors.forename: Jae Hong
authors.initials: JH
authors.lastname: Seol
authors.forename: Rho Hyun
authors.initials: RH
authors.lastname: Seong
mesh_terms: D000818:Animals; D019556:COS Cells; D002522:Chlorocebus aethiops; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D004265:DNA Helicases / Q000378:metabolism; D004795:Enzyme Stability; D006801:Humans; D051379:Mice; D009687:Nuclear Proteins / Q000378:metabolism; D000075223:Poly-ADP-Ribose Binding Proteins; D059748:Proteolysis; D000071796:SMARCB1 Protein; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism*; D025521:Tumor Suppressor Proteins / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*; D054875:Ubiquitination
chemical_list: D002868:Chromosomal Proteins, Non-Histone; D009687:Nuclear Proteins; D000075223:Poly-ADP-Ribose Binding Proteins; D000071796:SMARCB1 Protein; C445179:SWI-SNF-B chromatin-remodeling complex; C513265:Smarcb1 protein, mouse; C491090:Smarcc1 protein, mouse; C529549:Smarcd1 protein, mouse; D014157:Transcription Factors; D025521:Tumor Suppressor Proteins; C558788:CHFR protein, mouse; D044767:Ubiquitin-Protein Ligases; C513194:Smarca4 protein, mouse; D004265:DNA Helicases