The Structural Differences between a Glycoprotein Specific F-Box Protein Fbs1 and Its Homologous Protein FBG3
Open accessAbstract
The Skp1-Cul1-F-box protein (SCF) complex catalyzes protein ubiquitination in diverse cellular processes and is one of the best-characterized ubiquitin ligases. F-box proteins determine the substrate specificities of SCF ubiquitin ligases. Among these, Fbs1/FBG1/FBXO2, Fbs2/FBG2/FBXO6, and Fbs3/FBG5/FBXO27 recognize the N-glycans of glycoproteins, whereas FBG3/FBXO44 has no sugar-binding activity, despite the high sequence homology and conservation of the residues necessary for oligosaccharide binding between Fbs1-3 and FBG3. Here we determined the crystal structure of the Skp1-FBG3 complex at a resolution of 2.6 Å. The substrate-binding domain of FBG3 is composed of a 10-stranded antiparallel β-sandwich with three helices. Although the overall structure of FBG3 is similar to that of Fbs1, the residues that form the Fbs1 carbohydrate-binding pocket failed to be superposed with the corresponding residues of FBG3. Structure-based mutational analysis shows that distinct hydrogen bond networks of four FBG3 loops, i.e., β2-β3, β5-β6, β7-β8, and β9-β10, prevent the formation of the carbohydrate-binding pocket shown in Fbs1.
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FBXO44 is enriched in some tissues but not specific to any.
“F-box protein 44 (FBXO44)150 that is enriched in some tissues but not specific to any151.”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [150]
Structural studies of FBXO44 indicate cavities at the surface of the FBA domain, but no ligand has been described so far.
“Structural studies of FBXO44 indicate the presence of cavities at the surface of the FBA domain, but no ligand has been described so far 116 .”
From Targeted protein degradation: expanding the toolbox (2019) · cites this paper as [116]
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References 33 · Cited by 21
- Authors
- Kumanomidou, T., Nishio, K., Takagi, K., Nakagawa, T., Suzuki, A., Yamane, T., Tokunaga, F., Iwai, K., Murakami, A., Yoshida, Y., Tanaka, K., & Mizushima, T.
- Affiliations
- Nagoya University (JP)
- University of Hyogo (JP)
- Gunma University (JP)
- Tokyo Metropolitan Institute of Medical Science (JP)
- Corresponding author
- Yoshida, Yukiko
- Mizushima, Tsunehiro
- ORCID
- Venue
- PLOS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2015-10-13
- Volume
- 10
- Issue
- 10
- Pages
- e0140366
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC4603797
- OpenAlex
- W1864634785
- Cited by
- 21
- References
- 33
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 6 · 2022: 2 · 2020: 5 · 2019: 2 · 2017: 1 · 2016: 2
- FWCI
- 0.43
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Institutional Repositories DataBase (IRDB) (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Kyoto University Research Information Repository (Kyoto University) (submittedVersion, cc-by)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology (24112009)
- Japan Society for the Promotion of Science (15K08259, 25253019, 24112002, 26000014, 24580152)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Keywords
- F-box protein, SCF ubiquitin ligase, Skp1, glycoprotein recognition, substrate specificity, hydrogen bond network, crystal structure, structure-guided mutagenesis
- MeSH terms
- Amino Acid Sequence, Glycoproteins, Humans, Models, Molecular, Molecular Sequence Data, Mutation, Nerve Tissue Proteins, Protein Binding, Ribonucleases, Substrate Specificity, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Crystallography, X-Ray, Cell Cycle Proteins, F-Box Proteins, S-Phase Kinase-Associated Proteins, Mutant Proteins
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