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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 [[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 Fbls class and, in addition to an F-box, contains several tandem leucine-rich repeats. Alternative splicing of this gene generates 2 transcript variants.<ref name="entrez" /> |
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 [[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 Fbls class and, in addition to an F-box, contains several tandem leucine-rich repeats. Alternative splicing of this gene generates 2 transcript variants.<ref name="entrez" /> |
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FBXL5 is an [[iron]] and [[oxygen]] sensor. It promotes [[Iron-responsive element-binding protein|IRP2]] ubiquitination and then its degradation in an iron- and oxygen-dependent manner. The [[Cryogenic electron microscopy|cryo-EM]] structure of the FBXL5-IRP2 complex was determined by the research group led by [[Ning Zheng]], which revealed an unexpected 2Fe2S cluster embedded in the leucine-rich repeats domain of the F-box protein in close vicinity of the protein-protein interaction interface.<ref>{{Cite journal |last=Wang |first=Hui |last2=Shi |first2=Hui |last3=Rajan |first3=Malini |last4=Canarie |first4=Elizabeth R. |last5=Hong |first5=Seoyeon |last6=Simoneschi |first6=Daniele |last7=Pagano |first7=Michele |last8=Bush |first8=Matthew F. |last9=Stoll |first9=Stefan |last10=Leibold |first10=Elizabeth A. |last11=Zheng |first11=Ning |date=2020-04-02 |title=FBXL5 Regulates IRP2 Stability in Iron Homeostasis via an Oxygen-Responsive [2Fe2S] Cluster |url=https://pubmed.ncbi.nlm.nih.gov/32126207 |journal=Molecular Cell |volume=78 |issue=1 |pages=31–41.e5 |doi=10.1016/j.molcel.2020.02.011 |issn=1097-4164 |pmc=7159994 |pmid=32126207}}</ref> FBXL5, therefore, is an [[iron-sulfur protein]]. FBXL5 can only engage IRP2 when its 2Fe2S cluster is in the oxidized state, which explains how oxygen tension dictates IRP2 stability. |
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FBXL5 is an iron sensor. It promotes [[Iron-responsive element-binding protein|IRP2]] ubiquitination and then its degradation. |
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==References== |
==References== |
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Revision as of 13:17, 15 June 2024
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | FBXL5, FBL4, FBL5, FLR1, F-box and leucine-rich repeat protein 5, F-box and leucine rich repeat protein 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 605655; MGI: 2152883; HomoloGene: 8129; GeneCards: FBXL5; OMA:FBXL5 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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F-box/LRR-repeat protein 5 is a protein that in humans is encoded by the FBXL5 gene.[5][6]
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 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 Fbls class and, in addition to an F-box, contains several tandem leucine-rich repeats. Alternative splicing of this gene generates 2 transcript variants.[6]
FBXL5 is an iron and oxygen sensor. It promotes IRP2 ubiquitination and then its degradation in an iron- and oxygen-dependent manner. The cryo-EM structure of the FBXL5-IRP2 complex was determined by the research group led by Ning Zheng, which revealed an unexpected 2Fe2S cluster embedded in the leucine-rich repeats domain of the F-box protein in close vicinity of the protein-protein interaction interface.[7] FBXL5, therefore, is an iron-sulfur protein. FBXL5 can only engage IRP2 when its 2Fe2S cluster is in the oxidized state, which explains how oxygen tension dictates IRP2 stability.
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000118564 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000039753 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Cenciarelli C, Chiaur DS, Guardavaccaro D, Parks W, Vidal M, Pagano M (Dec 1999). "Identification of a family of human F-box proteins". Curr Biol. 9 (20): 1177–9. Bibcode:1999CBio....9.1177C. doi:10.1016/S0960-9822(00)80020-2. PMID 10531035. S2CID 7467493.
- ^ a b "Entrez Gene: FBXL5 F-box and leucine-rich repeat protein 5".
- ^ Wang H, Shi H, Rajan M, Canarie ER, Hong S, Simoneschi D, et al. (2020-04-02). "FBXL5 Regulates IRP2 Stability in Iron Homeostasis via an Oxygen-Responsive [2Fe2S] Cluster". Molecular Cell. 78 (1): 31–41.e5. doi:10.1016/j.molcel.2020.02.011. ISSN 1097-4164. PMC 7159994. PMID 32126207.
Further reading
- Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
- Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, et al. (1997). "Large-Scale Concatenation cDNA Sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
- Winston JT, Koepp DM, Zhu C, Elledge SJ, Harper J (1999). "A family of mammalian F-box proteins". Curr. Biol. 9 (20): 1180–2. Bibcode:1999CBio....9.1180W. doi:10.1016/S0960-9822(00)80021-4. PMID 10531037. S2CID 14341845.
- Ilyin GP, Rialland M, Pigeon C, Guguen-Guillouzo C (2001). "cDNA cloning and expression analysis of new members of the mammalian F-box protein family". Genomics. 67 (1): 40–7. doi:10.1006/geno.2000.6211. PMID 10945468.
- Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, et al. (2001). "Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, et al. (2004). "From ORFeome to Biology: A Functional Genomics Pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
- Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
- Mehrle A, Rosenfelder H, Schupp I, Del Val C, Arlt D, Hahne F, et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
- Zhang N, Liu J, Ding X, Aikhionbare F, Jin C, Yao X (2007). "FBXL5 interacts with p150Glued and regulates its ubiquitination". Biochem. Biophys. Res. Commun. 359 (1): 34–9. doi:10.1016/j.bbrc.2007.05.068. PMID 17532294.
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