ArticleMolecular biology of the cell2008
FBXO25-associated nuclear domains: a novel subnuclear structure.
Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Revisiting the clastosome: a stress-induced nuclear proteolytic compartment of mammalian cells.Frontiers in neuroanatomy · 2026Review
- Review
- LncRNA ODIR1 inhibits osteogenic differentiation of hUC-MSCs through the FBXO25/H2BK120ub/H3K4me3/OSX axis.Cell death & disease · 2019Article
- An Integrated Approach to Explore Composition and Dynamics of Cholesterol-rich Membrane Microdomains in Sexual Stages of Malaria Parasite.Molecular & cellular proteomics : MCP · 2017Article
- FBXO25 promotes cell proliferation, invasion, and migration of NSCLC.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Article
- The F-box protein FBXO25 promotes the proteasome-dependent degradation of ELK-1 protein.The Journal of biological chemistry · 2013Article
- Molecular characterization and association analysis of FBXO40 with partial hematological indexes in pig.Molecular biology reports · 2010Article
- Impact of nuclear organization and dynamics on epigenetic regulation in the central nervous system: implications for neurological disease states.Annals of the New York Academy of Sciences · 2010Review
- Identification of FBXO25-interacting proteins using an integrated proteomics approach.Proteomics · 2010Article
- Lipid microdomains in cell nucleus.Molecular biology of the cell · 2008Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Skp1, Cul1, Rbx1, and the FBXO25 protein form a functional ubiquitin ligase complex. Here, we investigate the cellular distribution of FBXO25 and its colocalization with some nuclear proteins by using immunochemical and biochemical approaches. FBXO25 was monitored with affinity-purified antibodies raised against the recombinant fragment spanning residues 2-62 of the FBXO25 sequence. FBXO25 protein was expressed in all mouse tissues tested except striated muscle, as indicated by immunoblot analysis. Confocal analysis revealed that the endogenous FBXO25 was partially concentrated in a novel dot-like nuclear domain that is distinct from clastosomes and other well-characterized structures. These nuclear compartments contain a high concentration of ubiquitin conjugates and at least two other components of the ubiquitin-proteasome system: 20S proteasome and Skp1. We propose to name these compartments FBXO25-associated nuclear domains. Interestingly, inhibition of transcription by actinomycin D or heat-shock treatment drastically affected the nuclear organization of FBXO25-containing structures, indicating that they are dynamic compartments influenced by the transcriptional activity of the cell. Also, we present evidences that an FBXO25-dependent ubiquitin ligase activity prevents aggregation of recombinant polyglutamine-containing huntingtin protein in the nucleus of human embryonic kidney 293 cells, suggesting that this protein can be a target for the nuclear FBXO25 mediated ubiquitination.
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