The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
A binding motif for Siah ubiquitin ligase
Open accessAbstract
The Drosophila SINA (seven in absentia) protein and its mammalian orthologs (Siah, seven in absentia homolog) are RING domain proteins that function in E3 ubiquitin ligase complexes and facilitate ubiquitination and degradation of a wide range of cellular proteins, including β-catenin. Despite these diverse targets, the means by which SINA/Siah recognize substrates or binding proteins has remained unknown. Here we identify a peptide motif (RPVAxVxPxxR) that mediates the interaction of Siah protein with a range of protein partners. Sequence alignment and mutagenesis scanning revealed residues that are important to this interaction. This consensus sequence correctly predicted a high-affinity interaction with a peptide from the cytoskeletal protein plectin-1 (residues 95–117). The unusually high-affinity binding obtained with a 23-residue peptide ( K Dapp = 29 nM with SINA) suggests that it may serve as a useful dominant negative reagent for SINA/Siah proteins.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The SIAH1 E3 ligase recognizes a VxP motif on substrate proteins25,26”
From Small-molecule-induced polymerization triggers degradation of BCL6 (2020) · cites this paper as [25]
Citations
Cites
Thompson, J. D., Higgins, D. G., & Gibson, T. J. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.22.4673 · Cited by 64,617
Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535
HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 Sensing
Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735
Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex
Zheng, N., Schulman, B. A., Song, L., Miller, J. J., Jeffrey, P. D., Wang, P., Chu, C., Koepp, D. M., Elledge, S. J., Pagano, M., et al. (2002) · Nature · doi:10.1038/416703a · Cited by 1,507
The ubiquitin–proteasome pathway: on protein death and cell life
Ciechanover, A. J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7151 · Cited by 1,419
RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination
Lorick, K. L., Jensen, J. P., Fang, S., Ong, A. M., Hatakeyama, S., & Weissman, A. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11364 · Cited by 1,151
Structure of a c-Cbl–UbcH7 Complex
Zheng, N., Wang, P., Jeffrey, P. D., & Pavletich, N. P. (2000) · Cell · doi:10.1016/s0092-8674(00)00057-x · Cited by 839
HIF-1α binding to VHL is regulated by stimulus-sensitive proline hydroxylation
Yu, F., White, S. B., Zhao, Q., & Lee, F. S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.181341498 · Cited by 796
Matsuzawa, S.-I., & Reed, J. C. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00242-8 · Cited by 591
Liu, J., Stevens, J., Rote, C. A., Yost, H. J., Hu, Y., Neufeld, K. L., White, R. L., & Matsunami, N. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00241-6 · Cited by 422
Cited by
Sorted by citations
S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding
Hara, M. R., Agrawal, N., Kim, S. F., Cascio, M. B., Fujimuro, M., Ozeki, Y., Takahashi, M., Cheah, J. H., Tankou, S. K., Hester, L. D., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1268 · Cited by 1,079
A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin
Willems, A. R., Schwab, M. G., & Tyers, M. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.09.027 · Cited by 476
Molecular traces of alternative social organization in a termite genome
Terrapon, N., Li, C., Robertson, H. M., Ji, L., Meng, X., Booth, W., Chen, Z., Childers, C. P., Glastad, K. M., Gokhale, K., et al. (2014) · Nature Communications · doi:10.1038/ncomms4636 · Cited by 397
Thiol-based redox switches in eukaryotic proteins
Brandes, N., Schmitt, S., & Jakob, U. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2285 · Cited by 373
Small-molecule-induced polymerization triggers degradation of BCL6
Słabicki, M., Yoon, H., Koeppel, J., Nitsch, L., Roy Burman, S. S., Di Genua, C., Donovan, K. A., Sperling, A. S., Hunkeler, M., Tsai, J. M., et al. (2020) · Nature · doi:10.1038/s41586-020-2925-1 · Cited by 270
Metadata
- Authors
- House, C. M., Frew, I. J., Huang, H.-L., Wiche, G., Traficante, N., Nice, E., Catimel, B., & Bowtell, D. D. L.
- Affiliations
- Peter MacCallum Cancer Centre (AU)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2003-03-07
- Volume
- 100
- Issue
- 6
- Pages
- 3101-3106
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC152253
- OpenAlex
- W2165179747
- Cited by
- 148
- References
- 38
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 6 · 2023: 2 · 2022: 9 · 2021: 7 · 2020: 5 · 2019: 5 · 2018: 2 · 2017: 6 · 2016: 3 · 2015: 6 · 2014: 4 · 2013: 10 · 2012: 7
- FWCI
- 3.11
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Wnt/β-catenin signaling in development and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- SIAH, Sina, RING domain, E3 ubiquitin ligase, substrate recognition, peptide binding motifs, protein-protein interaction, β-catenin degradation, Drosophila
- MeSH terms
- Seven in Absentia Proteins, Amino Acid Sequence, Animals, Binding Sites, Calcium-Binding Proteins, Carrier Proteins, Heat-Shock Proteins, Ligases, Molecular Sequence Data, Nuclear Proteins, Recombinant Proteins, Mutagenesis, Conserved Sequence, Sequence Homology, Amino Acid, Amino Acid Motifs, Drosophila Proteins, Ubiquitin-Protein Ligases, Mice, In Vitro Techniques
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review