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MBC in Press, published online ahead of print February 20, 2008
Mol. Biol. Cell 10.1091/mbc.E07-08-0815

A more recent version of this article appeared on May 1, 2008
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Submitted on August 23, 2007
Revised on January 28, 2008
Accepted on February 8, 2008

FBXO25-associated Nuclear Domains: A Novel Subnuclear Structure

Adriana O. Manfiolli,* Ana Leticia G. C. Marango,* Munira M. A. Baqui,{dagger} Sami Yokoo,* Felipe R. Teixeira, Eduardo B. Oliveira,* and Marcelo D. Gomes*

*Departments of Biochemistry and Immunology, and {dagger}Cellular and Molecular Biology, Faculty of Medicine of Ribeirão Preto, University of São Paulo, Brazil

Monitoring Editor: Wendy Bickmore

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 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 FANDs for 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 HEK293 cells, suggesting that this protein can be a target for the nuclear FBXO25 mediated ubiquitination.

Address correspondence to: Marcelo D. Gomes (mdamario{at}fmrp.usp.br)




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