Fbxo25, an F-box Protein Homologue of Atrogin-1, is Not Induced in Atrophying Muscle.
From: Faculdade de Medicina de Ribeirão Preto da Universidade de São Paulo (FMRP-USP), Department of Biochemistry and Immunology, Av. Bandeirantes, 3900, Ribeirão Preto -SP, Monte Alegre, CEP 14049-900, Brazil.
Biochimica et biophysica acta
- Publish Date: Jun 2006
- ISSN: 0006-3002
- Volume: 1760
- Issue: 6
- Pages: 966-72
- Medium: Print
- Language: English
- Citation (JAMA): Maragno Ana Leticia G C, Baqui Munira M A, Gomes Marcelo D, et al. Fbxo25, an F-box Protein Homologue of Atrogin-1, is Not Induced in Atrophying Muscle.. Biochim. Biophys. Acta Jun 2006;1760:966-72
Abstract
Atrogin-1/MAFbx/FBXO32 is a muscle-specific ubiquitin-ligase (E3) that is dramatically increased in atrophying muscle. Here, we have investigated the functional relationship between atrogin-1 and FBXO25 which shares 65% amino acid identity. Using a RT-PCR, we demonstrated that FBXO25 is highly expressed in brain, kidney, and intestine, whereas atrogin-1 expression is largely restricted to striate muscle. FBXO25 was shown here to contain a functional F-box domain that binds to Skp1 and thereby to Roc1 and Cul1, the major components of SCF-type E3s. In addition, the productive SCF complex containing FBXO25 showed ubiquitin ligase activity. We investigated the differential expression of atrogin-1 and FBXO25 in fasted and dexamethasone-treated mice and also in rats with streptozotocin-induced diabetes. Although the atrogin-1 was strongly induced in muscle in all three models, no changes were observed in the expression of FBXO25. Therefore, here we have shown that FBXO25 is a novel F-box protein analogous to atrogin-1, which is not involved in muscle atrophy. Further functional studies should elucidate the exact role of FBXO25 in the ubiquitin-proteasome pathway.
Mesh Headings (Keywords): Amino Acid Sequence, Animals, Cell Nucleus, F-Box Proteins, Gene Expression Profiling, Gene Expression Regulation, Humans, Male, Mice, Molecular Sequence Data, Muscle Proteins, Muscular Atrophy, Protein Binding, RNA, Messenger, Rats, Rats, Wistar, S-Phase Kinase-Associated Proteins, SKP Cullin F-Box Protein Ligases, Sequence Alignment, Ubiquitin, Ubiquitin-Protein Ligases
Check for Full Text / PubMed Unique Identifier (PMID): 16714087
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