The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
Plan and verification
- Identity check: The target is Fbxo2 (aliases: Fbs1, Fbx2; also reported as NFB42/OCP1/Fbg1 in older literature), encoding F-box only protein 2 in Mus musculus. Literature consistently describes an N-terminal F-box domain for SCF assembly and a C-terminal F-box-associated/substrate-binding domain (FBA/SBD) that recognizes the innermost N-glycan chitobiose/Man3GlcNAc2 core, in agreement with the UniProt Q80UW2 entry and the provided InterPro domains (F-box_dom, F-box-assoc/FBA, Galactose-binding-like superfamily) (nelson2007selectivecochleardegeneration pages 1-2, yoshida2007fboxproteinsthat pages 4-5, yoshida2007fboxproteinsthat pages 6-7). No conflicting gene symbols were found for a different gene in mouse.
| Aspect | Key details | Primary evidence (journal, year) | URL |
|---|---|---|---|
| Identity / aliases / organism | F-box only protein 2; aliases: Fbs1, Fbx2, NFB42, OCP1; organism: Mus musculus | The Journal of Neuroscience, 2007 (Nelson et al.) (nelson2007selectivecochleardegeneration pages 1-2) | https://doi.org/10.1523/jneurosci.0206-07.2007 |
| Domains / structure | N-terminal F-box; C-terminal F-box-associated substrate-binding domain (SBD/FBA); SBD is a β-sandwich with a small hydrophobic pocket contacting the innermost chitobiose; key pocket residues reported (e.g., Phe177, Tyr279, Trp280, Lys281 in mouse) | Bioscience, Biotechnology, and Biochemistry, 2007 (Yoshida) (yoshida2007fboxproteinsthat pages 4-5) | https://doi.org/10.1271/bbb.70074 |
| Biochemical function | Substrate receptor of SCF (Skp1–Cul1–F-box) E3 ubiquitin ligase; lectin-like recognition of the Man3GlcNAc2 core and preference for high-mannose N-glycans; mediates ubiquitination of glycoproteins for proteasomal degradation | Frontiers in Physiology, 2019 (Yoshida et al.) (yoshida2019sugarrecognizingubiquitinligases pages 1-2) | https://doi.org/10.3389/fphys.2019.00104 |
| Substrate specificity | Binds innermost N-glycan cores (Man3–9GlcNAc2) with highest affinity for high-mannose structures; preferentially recognizes denatured/unfolded glycoproteins where the inner glycan is exposed | Journal of Biological Chemistry, 2003 (Yoshida et al.) (yoshida2003fbs2isa pages 1-2) | https://doi.org/10.1074/jbc.m304157200 |
| Cellular localization | Nucleocytoplasmic / cytosolic F-box protein that interfaces with ERAD machinery at the ER membrane (associates functionally with p97 and retrotranslocation components) | Bioscience, Biotechnology, and Biochemistry, 2007 (Yoshida) (yoshida2007fboxproteinsthat pages 6-7) | https://doi.org/10.1271/bbb.70074 |
| Pathways | ER-associated degradation (ERAD) of misfolded N-glycoproteins; also functions in ubiquitin-mediated xenophagy by recognizing bacterial GlcNAc-containing surface glycans (e.g., GAS) to promote ubiquitin deposition and autophagic clearance | EMBO Reports, 2021 (Yamada et al.) (yamada2021fbxo2scfubiquitinligase pages 1-2) | https://doi.org/10.15252/embr.202152584 |
| In vivo phenotypes | Fbxo2−/− mice develop early-onset, progressive hearing loss with selective degeneration of cochlear epithelial support cells (later hair cells and spiral ganglion); brain largely spared despite CNS expression | The Journal of Neuroscience, 2007 (Nelson et al.) (nelson2007selectivecochleardegeneration pages 1-2) | https://doi.org/10.1523/jneurosci.0206-07.2007 |
| Applications | SBD/glycan-recognition properties enable affinity capture of N-glycans and N-glycopeptides and have motivated engineered high-affinity Fbs1-based reagents for glycoproteomics workflows | Bioscience, Biotechnology, and Biochemistry, 2007 (Yoshida) (yoshida2007fboxproteinsthat pages 4-5) | https://doi.org/10.1271/bbb.70074 |
Table: Compact summary table of FBXO2 (mouse Fbxo2/Fbs1) covering identity, domains, biochemical roles, specificity, localization, pathways, in vivo phenotype, and applied uses, with primary supporting citations for each aspect.
Comprehensive research report on mouse Fbxo2 (Fbs1/Fbx2; UniProt Q80UW2)
1) Key concepts and definitions (current understanding)
- Molecular identity and domain architecture: Fbxo2 encodes an F-box protein that serves as the substrate-recognition component of an SCF (Skp1–Cul1–Rbx1–F-box) E3 ubiquitin ligase. Its N-terminal F-box binds Skp1; its C-terminal substrate-binding domain (also called FBA/SBD) is a β-sandwich that engages the innermost chitobiose of N-linked glycans via a small hydrophobic pocket, with key pocket residues (mouse: Phe177, Tyr279, Trp280, Lys281) supporting glycan binding (Bioscience, Biotechnology, and Biochemistry, 2007; doi:10.1271/bbb.70074) (yoshida2007fboxproteinsthat pages 4-5, yoshida2007fboxproteinsthat pages 6-7).
- Primary biochemical function: FBXO2 is a lectin-type substrate adaptor that recognizes high-mannose N-glycans (especially the Man3GlcNAc2 core) on misfolded or unassembled glycoproteins and directs their ubiquitination by SCF for proteasomal degradation. This places FBXO2 in glycoprotein quality control, especially ER-associated degradation (ERAD), where retrotranslocated glycoproteins expose inner N-glycan moieties for recognition (Frontiers in Physiology, 2019; doi:10.3389/fphys.2019.00104) (yoshida2019sugarrecognizingubiquitinligases pages 1-2, yoshida2007fboxproteinsthat pages 2-3, yoshida2007fboxproteinsthat pages 1-1).
- Substrate specificity: FBXO2 binds innermost N-glycan cores, preferring high-mannose species (Man3–Man9GlcNAc2). Binding is stronger to denatured/unfolded glycoproteins, reflecting exposure of the inner chitobiose; it can interact with complex N-glycans when the glycoprotein is denatured (J. Biol. Chem., 2003; doi:10.1074/jbc.m304157200; Biosci. Biotechnol. Biochem., 2007; doi:10.1271/bbb.70074) (yoshida2003fbs2isa pages 1-2, yoshida2007fboxproteinsthat pages 4-5).
- Cellular localization and pathway context: Although glycoproteins reside in the secretory pathway, FBXO2 is a cytosolic/nucleocytoplasmic F-box protein that operates at the ERAD interface—recognizing retrotranslocated ER glycoproteins, coordinating with p97/VCP for extraction, and targeting them to the proteasome after deglycosylation by PNGase (Biosci. Biotechnol. Biochem., 2007; doi:10.1271/bbb.70074) (yoshida2007fboxproteinsthat pages 6-7, yoshida2007fboxproteinsthat pages 2-3).
2) Recent developments and latest research (prioritizing 2023–2024)
- We found limited 2023–2024 primary literature specifically expanding mouse Fbxo2 mechanism. However, the most recent high-quality advance extending FBXO2 function beyond ERAD is xenophagy of cytosolic bacteria (EMBO Reports, 2021; doi:10.15252/embr.202152584). In human cells, FBXO2 recognizes GlcNAc-containing surface polysaccharide (GAC) on Group A Streptococcus, recruits SCF components, promotes ubiquitin coating of bacteria, and facilitates xenophagy. This underscores a broader paradigm of glycan-driven substrate selection by FBXO2 in immunity (yamada2021fbxo2scfubiquitinligase pages 1-2). The field’s structural/biophysical foundation and ERAD roles remain anchored by earlier, well-cited work (2003–2019) (yoshida2019sugarrecognizingubiquitinligases pages 1-2, yoshida2003fbs2isa pages 1-2, yoshida2007fboxproteinsthat pages 6-7).
3) Current applications and real-world implementations
- Glycoproteomics affinity reagents: The FBXO2/Fbs1 SBD has been engineered into high-affinity variants for unbiased enrichment of N-linked glycopeptides. The GYR variant (Nature Communications, 2017; doi:10.1038/ncomms15487) achieved submicromolar Kd to core structures and enabled simultaneous determination of N-glycan composition and glycosites from complex samples (e.g., human serum), outperforming lectin-based enrichment (chen2017anengineeredhigh pages 1-2). Foundational work also documented practical purification of native FBXO2/Fbs1 using RNase B affinity and chitobiose elution, highlighting its utility as a glycan-binding tool (Biosci. Biotechnol. Biochem., 2007; doi:10.1271/bbb.70074) (yoshida2007fboxproteinsthat pages 3-4, yoshida2007fboxproteinsthat pages 4-5).
- Antiviral restriction: FBXO2 recognizes the high-mannose N-glycans on Epstein–Barr virus glycoprotein B (gB), targeting it for SCF-dependent ubiquitination and proteasomal degradation; FBXO2 depletion increases gB surface transport and enhances viral entry (PLOS Pathogens, 2018; doi:10.1371/journal.ppat.1007208) (zhang2018epsteinbarrvirusactivates pages 1-2, zhang2018epsteinbarrvirusactivates pages 2-5).
4) Expert opinions and analysis from authoritative sources
- Reviews synthesizing sugar-recognizing F-box proteins conclude that FBXO2 (with FBXO6) is a cytosolic lectin-type F-box that interprets the innermost N-glycan as a degradation signal, linking glycan structure to ERAD substrate selection. Structural studies define a β-sandwich SBD with a hydrophobic pocket contacting chitobiose, rationalizing specificity for Man3GlcNAc2 and preference for high-mannose glycans. These reviews emphasize the divergence of lectin-type F-box functions, with FBXO27 acting in lysophagy and FBXO2 in ERAD and, more recently, xenophagy (Frontiers in Physiology, 2019; Biosci. Biotechnol. Biochem., 2007; BioEssays, 2018; doi:10.3389/fphys.2019.00104; 10.1271/bbb.70074; 10.1002/bies.201700215) (yoshida2019sugarrecognizingubiquitinligases pages 1-2, yoshida2007fboxproteinsthat pages 4-5, yoshida2007fboxproteinsthat pages 6-7) (yoshida2019sugarrecognizingubiquitinligases pages 1-2, yoshida2007fboxproteinsthat pages 4-5, yoshida2007fboxproteinsthat pages 6-7, yoshida2007fboxproteinsthat pages 2-3).
5) Relevant statistics and data from recent studies
- Binding and enrichment performance (engineered FBXO2/Fbs1): Quantitative ITC from the engineered Fbs1 study showed Kd ~0.12–0.13 μM for core pentasaccharide motifs (M3N2/M3N2F) versus ~3.0 μM for a sialylglycopeptide, supporting core-preference and explaining efficient, relatively unbiased glycopeptide capture by the GYR variant (Nature Communications, 2017; doi:10.1038/ncomms15487) (chen2017anengineeredhigh pages 1-2).
- Xenophagy functional effect: FBXO2 knockout reduced ubiquitin accumulation on intracellular Group A Streptococcus and impaired xenophagic degradation, with SCF components (SKP1, CUL1, ROC1) required for ubiquitin-mediated xenophagy. These functional phenotypes document FBXO2’s contribution to antibacterial autophagy (EMBO Reports, 2021; doi:10.15252/embr.202152584) (yamada2021fbxo2scfubiquitinligase pages 1-2).
- In vivo phenotype in mouse: Fbxo2−/− mice exhibit early-onset, progressive hearing loss beginning around 2 months of age, with initial degeneration of organ of Corti supporting cells, later involving hair cells and spiral ganglion; CNS largely spared despite widespread expression. Cochlear FBXO2 binds Skp1 and is unusually abundant; cochlear Skp1 levels decline with Fbx2 loss, and connexin 26 levels change during degeneration (J. Neurosci., 2007; doi:10.1523/JNEUROSCI.0206-07.2007) (nelson2007selectivecochleardegeneration pages 1-2).
Mechanistic depth and pathways
- ERAD: FBXO2 recognizes high-mannose N-glycans on misfolded/unassembled glycoproteins retrotranslocated to the cytosol. SCF^FBXO2 mediates polyubiquitination; p97/VCP-associated extraction and PNGase-mediated deglycosylation precede proteasomal degradation (Biosci. Biotechnol. Biochem., 2007; doi:10.1271/bbb.70074; Frontiers in Physiology, 2019; doi:10.3389/fphys.2019.00104) (yoshida2007fboxproteinsthat pages 6-7, yoshida2019sugarrecognizingubiquitinligases pages 1-2).
- Substrates and specificity determinants: Inner-core recognition (chitobiose) underpins preference for high-mannose N-glycans; denaturation exposes cores enabling binding to even complex glycans. Site-directed mutagenesis of SBD pocket residues (Phe177, Tyr279, Trp280, Lys281) reduces/abolishes binding, mapping a specific hydrophobic pocket that governs glycan recognition (Biosci. Biotechnol. Biochem., 2007; doi:10.1271/bbb.70074) (yoshida2007fboxproteinsthat pages 6-7, yoshida2007fboxproteinsthat pages 4-5).
- Beyond ERAD: FBXO2 mediates ubiquitin-dependent xenophagy through GlcNAc recognition on bacterial surfaces (GAS), converging SCF-mediated ubiquitination with autophagic effectors (EMBO Reports, 2021; doi:10.15252/embr.202152584) (yamada2021fbxo2scfubiquitinligase pages 1-2). Viral restriction of EBV via gB degradation indicates FBXO2’s lectin activity surveils pathogen-associated high-mannose glycans (PLOS Pathogens, 2018; doi:10.1371/journal.ppat.1007208) (zhang2018epsteinbarrvirusactivates pages 1-2).
Subcellular localization and context of action
- FBXO2 is a cytosolic/nucleocytoplasmic lectin-type F-box protein that can assemble with Skp1–Cul1–Rbx1. In cochlea, an abundant Fbx2–Skp1 heterodimer and limited full SCF formation were reported, suggesting tissue-specific stoichiometry and potential noncanonical complexes. Functionally, FBXO2 acts at the ER–cytosol interface during ERAD and in the cytosol for xenophagic targeting (J. Neurosci., 2007; doi:10.1523/JNEUROSCI.0206-07.2007; Biosci. Biotechnol. Biochem., 2007; doi:10.1271/bbb.70074) (nelson2007selectivecochleardegeneration pages 1-2, yoshida2007fboxproteinsthat pages 6-7).
Selected primary examples and evidence
- ERAD substrates and neuronal quality control: Foundational studies showed Fbs1/FBXO2 binds high-mannose glycans on canonical ERAD substrates (e.g., TCRα via Fbs2; by analogy and in vitro assays for Fbs1), and can influence neuronal glycoprotein turnover (e.g., NMDA receptor NR1 in some contexts) as part of glycan-directed quality control (J. Biol. Chem., 2003; doi:10.1074/jbc.m304157200; Biosci. Biotechnol. Biochem., 2007; doi:10.1271/bbb.70074) (yoshida2003fbs2isa pages 1-2, yoshida2007fboxproteinsthat pages 3-4).
- Engineered SBDs as analytical tools: The engineered Fbs1 GYR variant improves capture of complex and high-mannose glycopeptides, enabling deep N-glycoproteomics from serum with reduced bias—demonstrating translational utility of FBXO2-derived domains in biomarker discovery workflows (Nat. Commun., 2017; doi:10.1038/ncomms15487) (chen2017anengineeredhigh pages 1-2).
- Host–pathogen interactions: FBXO2 restricts EBV infectivity by ubiquitinating high-mannose–glycosylated gB; loss of FBXO2 stabilizes gB and increases membrane fusion and entry (PLOS Pathogens, 2018; doi:10.1371/journal.ppat.1007208). Separately, FBXO2 promotes ubiquitin deposition on cytosolic Group A Streptococcus, facilitating xenophagy (EMBO Reports, 2021; doi:10.15252/embr.202152584) (zhang2018epsteinbarrvirusactivates pages 1-2, yamada2021fbxo2scfubiquitinligase pages 1-2).
Limitations and open questions
- Time- and tissue-resolved assembly of SCF^FBXO2 vs. FBXO2–Skp1 heterodimer in vivo remains to be mapped quantitatively across tissues (cochlear data suggest atypical stoichiometry) (J. Neurosci., 2007; doi:10.1523/JNEUROSCI.0206-07.2007) (nelson2007selectivecochleardegeneration pages 1-2).
- High-resolution structural data of full-length FBXO2 within SCF bound to glycoprotein substrates would refine mechanistic models beyond isolated SBD structures (Biosci. Biotechnol. Biochem., 2007; doi:10.1271/bbb.70074) (yoshida2007fboxproteinsthat pages 4-5, yoshida2007fboxproteinsthat pages 6-7).
Key references with URLs and dates
- Yoshida Y. F-box proteins that contain sugar-binding domains. Bioscience, Biotechnology, and Biochemistry. 2007 Nov;71:2623–2631. doi:10.1271/bbb.70074. URL: https://doi.org/10.1271/bbb.70074 (yoshida2007fboxproteinsthat pages 4-5, yoshida2007fboxproteinsthat pages 6-7, yoshida2007fboxproteinsthat pages 7-8, yoshida2007fboxproteinsthat pages 2-3, yoshida2007fboxproteinsthat pages 3-4).
- Yoshida Y, Mizushima T, Tanaka K. Sugar-Recognizing Ubiquitin Ligases: Action Mechanisms and Physiology. Frontiers in Physiology. 2019 Feb;10:104. doi:10.3389/fphys.2019.00104. URL: https://doi.org/10.3389/fphys.2019.00104 (yoshida2019sugarrecognizingubiquitinligases pages 1-2).
- Yoshida Y et al. Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains. Journal of Biological Chemistry. 2003 Oct;278:43877–43884. doi:10.1074/jbc.M304157200. URL: https://doi.org/10.1074/jbc.m304157200 (yoshida2003fbs2isa pages 1-2).
- Nelson RF et al. Selective Cochlear Degeneration in Mice Lacking Fbx2. The Journal of Neuroscience. 2007 May 9;27(19):5163–5171. doi:10.1523/JNEUROSCI.0206-07.2007. URL: https://doi.org/10.1523/jneurosci.0206-07.2007 (nelson2007selectivecochleardegeneration pages 1-2).
- Yamada A et al. FBXO2/SCF ligase directs xenophagy via bacterial surface glycan recognition. EMBO Reports. 2021 Sep;22(11):e52584. doi:10.15252/embr.202152584. URL: https://doi.org/10.15252/embr.202152584 (yamada2021fbxo2scfubiquitinligase pages 1-2).
- Zhang H-J et al. EBV activates FBXO2 to limit infectivity by degrading glycoprotein B. PLOS Pathogens. 2018 Jul;14(7):e1007208. doi:10.1371/journal.ppat.1007208. URL: https://doi.org/10.1371/journal.ppat.1007208 (zhang2018epsteinbarrvirusactivates pages 1-2, zhang2018epsteinbarrvirusactivates pages 2-5).
- Chen M et al. Engineered high-affinity Fbs1 for N-glycan/glycopeptide capture. Nature Communications. 2017 May 22;8:15487. doi:10.1038/ncomms15487. URL: https://doi.org/10.1038/ncomms15487 (chen2017anengineeredhigh pages 1-2).
Conclusion
Mouse Fbxo2 encodes a lectin-type F-box protein whose SBD specifically recognizes the inner core of N-linked glycans to target glycoproteins for SCF-mediated ubiquitination in ERAD. Structural studies define a β-sandwich pocket contacting chitobiose; mutagenesis pinpoints essential residues. Beyond ER quality control, FBXO2 participates in host defense (xenophagy; viral restriction) by recognizing pathogen glycans. In vivo, Fbxo2−/− mice exhibit early-onset, progressive hearing loss with selective cochlear degeneration. Engineered FBXO2-derived SBDs are now practical tools for glycoproteomics. Collectively, FBXO2 integrates glycan pattern recognition with ubiquitin signaling across proteostasis and immunity (yoshida2019sugarrecognizingubiquitinligases pages 1-2, yoshida2007fboxproteinsthat pages 6-7, yamada2021fbxo2scfubiquitinligase pages 1-2, zhang2018epsteinbarrvirusactivates pages 1-2, nelson2007selectivecochleardegeneration pages 1-2, chen2017anengineeredhigh pages 1-2).
References
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(yoshida2007fboxproteinsthat pages 4-5): Yukiko YOSHIDA. F-box proteins that contain sugar-binding domains. Bioscience, Biotechnology, and Biochemistry, 71:2623-2631, Nov 2007. URL: https://doi.org/10.1271/bbb.70074, doi:10.1271/bbb.70074. This article has 51 citations.
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(yoshida2019sugarrecognizingubiquitinligases pages 1-2): Yukiko Yoshida, Tsunehiro Mizushima, and Keiji Tanaka. Sugar-recognizing ubiquitin ligases: action mechanisms and physiology. Frontiers in Physiology, Feb 2019. URL: https://doi.org/10.3389/fphys.2019.00104, doi:10.3389/fphys.2019.00104. This article has 30 citations and is from a poor quality or predatory journal.
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(yamada2021fbxo2scfubiquitinligase pages 1-2): Akihiro Yamada, Miyako Hikichi, Takashi Nozawa, and Ichiro Nakagawa. Fbxo2/scf ubiquitin ligase complex directs xenophagy through recognizing bacterial surface glycan. EMBO reports, Sep 2021. URL: https://doi.org/10.15252/embr.202152584, doi:10.15252/embr.202152584. This article has 28 citations and is from a highest quality peer-reviewed journal.
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(chen2017anengineeredhigh pages 1-2): Minyong Chen, Xiaofeng Shi, Rebecca M. Duke, Cristian I. Ruse, Nan Dai, Christopher H. Taron, and James C. Samuelson. An engineered high affinity fbs1 carbohydrate binding protein for selective capture of n-glycans and n-glycopeptides. Nature Communications, May 2017. URL: https://doi.org/10.1038/ncomms15487, doi:10.1038/ncomms15487. This article has 52 citations and is from a highest quality peer-reviewed journal.
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(zhang2018epsteinbarrvirusactivates pages 1-2): Hao-Jiong Zhang, Jinxiu Tian, Xue-Kang Qi, Tong Xiang, Gui-Ping He, Hua Zhang, Xibao Yu, Xiao Zhang, Bingchun Zhao, Qi-Sheng Feng, Ming-Yuan Chen, Mu-Sheng Zeng, Yi-Xin Zeng, and Lin Feng. Epstein-barr virus activates f-box protein fbxo2 to limit viral infectivity by targeting glycoprotein b for degradation. PLOS Pathogens, 14:e1007208, Jul 2018. URL: https://doi.org/10.1371/journal.ppat.1007208, doi:10.1371/journal.ppat.1007208. This article has 46 citations and is from a highest quality peer-reviewed journal.
(zhang2018epsteinbarrvirusactivates pages 2-5): Hao-Jiong Zhang, Jinxiu Tian, Xue-Kang Qi, Tong Xiang, Gui-Ping He, Hua Zhang, Xibao Yu, Xiao Zhang, Bingchun Zhao, Qi-Sheng Feng, Ming-Yuan Chen, Mu-Sheng Zeng, Yi-Xin Zeng, and Lin Feng. Epstein-barr virus activates f-box protein fbxo2 to limit viral infectivity by targeting glycoprotein b for degradation. PLOS Pathogens, 14:e1007208, Jul 2018. URL: https://doi.org/10.1371/journal.ppat.1007208, doi:10.1371/journal.ppat.1007208. This article has 46 citations and is from a highest quality peer-reviewed journal.
(yoshida2007fboxproteinsthat pages 7-8): Yukiko YOSHIDA. F-box proteins that contain sugar-binding domains. Bioscience, Biotechnology, and Biochemistry, 71:2623-2631, Nov 2007. URL: https://doi.org/10.1271/bbb.70074, doi:10.1271/bbb.70074. This article has 51 citations.