FBXO32

F-box only protein 32 is a protein that in humans is encoded by the FBXO32 gene.[5][6][7]

FBXO32
Identifiers
Aliases	FBXO32, Fbx32, MAFbx, F-box protein 32
External IDs	OMIM: 606604 MGI: 1914981 HomoloGene: 12182 GeneCards: FBXO32
Gene location (Human) Chr. Chromosome 8 (human)[1] Band 8q24.13 Start 123,497,889 bp[1] End 123,541,206 bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15|15 D1 Start 58,175,879 bp[2] End 58,214,932 bp[2]
Gene ontology Molecular function • GO:0001948 protein binding • ubiquitin-protein transferase activity Cellular component • cytoplasm • Z disc • nucleoplasm • cytosol • cell nucleus • SCF ubiquitin ligase complex Biological process • response to denervation involved in regulation of muscle adaptation • cellular response to dexamethasone stimulus • protein polyubiquitination • protein ubiquitination • post-translational modification Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	114907	67731
Ensembl	ENSG00000156804	ENSMUSG00000022358
UniProt	Q969P5	Q9CPU7
RefSeq (mRNA)	NM_148177 NM_001242463 NM_058229	NM_026346
RefSeq (protein)	NP_001229392 NP_478136 NP_680482	NP_080622
Location (UCSC)	Chr 8: 123.5 – 123.54 Mb	Chr 15: 58.18 – 58.21 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class and contains an F-box domain. This protein is highly expressed during muscle atrophy, whereas mice deficient in this gene were found to be resistant to atrophy. This protein is thus a potential drug target for the treatment of muscle atrophy. Alternative splicing of this gene results in two transcript variants encoding two isoforms of different sizes.[7]

Interactions

FBXO32 has been shown to interact with EIF3A.[8]

Cancer

FBXO32 gene has been observed progressively downregulated in Human papillomavirus-positive neoplastic keratinocytes derived from uterine cervical preneoplastic lesions at different levels of malignancy.[9] For this reason, FBXO32 is likely to be associated with tumorigenesis and may be a potential prognostic marker for uterine cervical preneoplastic lesions progression.[9]

References

1. GRCh38: Ensembl release 89: ENSG00000156804 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022358 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Bodine SC, Latres E, Baumhueter S, Lai VK, Nunez L, Clarke BA, Poueymirou WT, Panaro FJ, Na E, Dharmarajan K, Pan ZQ, Valenzuela DM, DeChiara TM, Stitt TN, Yancopoulos GD, Glass DJ (Nov 2001). "Identification of ubiquitin ligases required for skeletal muscle atrophy". Science. 294 (5547): 1704–8. doi:10.1126/science.1065874. PMID 11679633.
6. Gomes MD, Lecker SH, Jagoe RT, Navon A, Goldberg AL (Dec 2001). "Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy". Proc. Natl. Acad. Sci. U.S.A. 98 (25): 14440–5. doi:10.1073/pnas.251541198. PMC 64700. PMID 11717410.
7. "Entrez Gene: FBXO32 F-box protein 32".
8. Lagirand-Cantaloube J, Offner N, Csibi A, Leibovitch MP, Batonnet-Pichon S, Tintignac LA, Segura CT, Leibovitch SA (Apr 2008). "The initiation factor eIF3-f is a major target for atrogin1/MAFbx function in skeletal muscle atrophy". EMBO J. 27 (8): 1266–76. doi:10.1038/emboj.2008.52. PMC 2367397. PMID 18354498.
9. Rotondo JC, Bosi S, Bassi C, Ferracin M, Lanza G, Gafà R, Magri E, Selvatici R, Torresani S, Marci R, Garutti P, Negrini M, Tognon M, Martini F (April 2015). "Gene expression changes in progression of cervical neoplasia revealed by microarray analysis of cervical neoplastic keratinocytes". J Cell Physiol. 230 (4): 802–812. doi:10.1002/jcp.24808. PMID 25205602.

Further reading

• Hanai J, Cao P, Tanksale P, Imamura S, Koshimizu E, Zhao J, Kishi S, Yamashita M, Phillips PS, Sukhatme VP, Lecker SH (2007). "The muscle-specific ubiquitin ligase atrogin-1/MAFbx mediates statin-induced muscle toxicity". J. Clin. Invest. 117 (12): 3940–51. doi:10.1172/JCI32741. PMC 2066198. PMID 17992259.
• de Palma L, Marinelli M, Pavan M, Orazi A (2008). "Ubiquitin ligases MuRF1 and MAFbx in human skeletal muscle atrophy". Joint Bone Spine. 75 (1): 53–7. doi:10.1016/j.jbspin.2007.04.019. PMID 17977773.
• Mascher H, Tannerstedt J, Brink-Elfegoun T, Ekblom B, Gustafsson T, Blomstrand E (2008). "Repeated resistance exercise training induces different changes in mRNA expression of MAFbx and MuRF-1 in human skeletal muscle". Am. J. Physiol. Endocrinol. Metab. 294 (1): E43-51. doi:10.1152/ajpendo.00504.2007. hdl:10616/40320. PMID 17971512.
• de Boer MD, Selby A, Atherton P, Smith K, Seynnes OR, Maganaris CN, Maffulli N, Movin T, Narici MV, Rennie MJ (2007). "The temporal responses of protein synthesis, gene expression and cell signalling in human quadriceps muscle and patellar tendon to disuse". J. Physiol. 585 (Pt 1): 241–51. doi:10.1113/jphysiol.2007.142828. PMC 2375459. PMID 17901116.
• Petersen AM, Magkos F, Atherton P, Selby A, Smith K, Rennie MJ, Pedersen BK, Mittendorfer B (2007). "Smoking impairs muscle protein synthesis and increases the expression of myostatin and MAFbx in muscle". Am. J. Physiol. Endocrinol. Metab. 293 (3): E843-8. doi:10.1152/ajpendo.00301.2007. PMID 17609255. S2CID 2608857.
• Kostek MC, Chen YW, Cuthbertson DJ, Shi R, Fedele MJ, Esser KA, Rennie MJ (2007). "Gene expression responses over 24 h to lengthening and shortening contractions in human muscle: major changes in CSRP3, MUSTN1, SIX1, and FBXO32". Physiol. Genomics. 31 (1): 42–52. doi:10.1152/physiolgenomics.00151.2006. PMID 17519359.
• Doucet M, Russell AP, Léger B, Debigaré R, Joanisse DR, Caron MA, LeBlanc P, Maltais F (2007). "Muscle atrophy and hypertrophy signaling in patients with chronic obstructive pulmonary disease". Am. J. Respir. Crit. Care Med. 176 (3): 261–9. doi:10.1164/rccm.200605-704OC. PMID 17478621.
• Ogawa T, Furochi H, Mameoka M, Hirasaka K, Onishi Y, Suzue N, Oarada M, Akamatsu M, Akima H, Fukunaga T, Kishi K, Yasui N, Ishidoh K, Fukuoka H, Nikawa T (2006). "Ubiquitin ligase gene expression in healthy volunteers with 20-day bedrest". Muscle Nerve. 34 (4): 463–9. doi:10.1002/mus.20611. PMID 16868939.
• Léger B, Vergani L, Sorarù G, Hespel P, Derave W, Gobelet C, D'Ascenzio C, Angelini C, Russell AP (2006). "Human skeletal muscle atrophy in amyotrophic lateral sclerosis reveals a reduction in Akt and an increase in atrogin-1". FASEB J. 20 (3): 583–5. doi:10.1096/fj.05-5249fje. PMID 16507768.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.