Cited by 149Ubiquitin and proteasome pathwaysWnt/β-catenin signaling in development and cancerProtein Degradation and Inhibitors

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A binding motif for Siah ubiquitin ligase

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House, Colin M., Frew, Ian J., Huang, Huei-Luen, Wiche, Gerhard, Traficante, Nadia, Nice, Edouard, Catimel, Bruno, Bowtell, David D. L.·2003·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0534783100PMC PMC152253

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Abstract

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.

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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: House, Colin M.
Frew, Ian J.
Wiche, Gerhard
Traficante, Nadia
Nice, Edouard
Catimel, Bruno
Bowtell, David D. L.
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
DOI: 10.1073/pnas.0534783100
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

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A binding motif for Siah ubiquitin ligase

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