ArticleBiochemistry2008
Structure of the S100A6 complex with a fragment from the C-terminal domain of Siah-1 interacting protein: a novel mode for S100 protein target recognition.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 64 citations in OpenAlex.
- Calcium mediated static and dynamic allostery in S100A12: Implications for target recognition by S100 proteins.Protein science : a publication of the Protein Society · 2024Article
- The structural properties of full-length annexin A11.Frontiers in molecular biosciences · 2024Article
- S100A6 Protein-Expression and Function in Norm and Pathology.International journal of molecular sciences · 2023Review
- Were Ancestral Proteins Less Specific?Molecular biology and evolution · 2021Article
- Identification and Biochemical Characterization of High Mobility Group Protein 20A as a Novel CaBiomolecules · 2021Article
- Studying the Structures of Relaxed and Fuzzy Interactions: The Diverse World of S100 Complexes.Frontiers in molecular biosciences · 2021Review
- Learning peptide recognition rules for a low-specificity protein.Protein science : a publication of the Protein Society · 2020Article
- Lysozyme as the anti-proliferative agent to block the interaction between S100A6 and the RAGE V domain.PloS one · 2019Article
- S100 proteins as therapeutic targets.Biophysical reviews · 2018Review
- Conservation of Specificity in Two Low-Specificity Proteins.Biochemistry · 2018Article
- Article
- S100A6 protein: functional roles.Cellular and molecular life sciences : CMLS · 2017Review
- Effects of S100A6 gene silencing on the biological features of eutopic endometrial stromal cells and β‑catenin expression.Molecular medicine reports · 2017Article
- Article
- The potential role of CacyBP/SIP in tumorigenesis.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Review
- Dimerization and phosphatase activity of calcyclin-binding protein/Siah-1 interacting protein: the influence of oxidative stress.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- S100 calcium-binding protein A6 promotes epithelial-mesenchymal transition through β-catenin in pancreatic cancer cell line.PloS one · 2015Article
- Increased expression of S100A6 promotes cell proliferation and migration in human hepatocellular carcinoma.Journal of molecular medicine (Berlin, Germany) · 2014Article
- Article
- Structure of the S100A4/myosin-IIA complex.BMC structural biology · 2013Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
S100A6 is a member of the S100 subfamily of EF-hand Ca (2+) binding proteins that has been shown to interact with calcyclin binding protein/Siah-1 interacting protein (CacyBP/SIP or SIP), a subunit of an SCF-like E3 ubiquitin ligase complex (SCF-TBL1) formed under genotoxic stress. SIP serves as a scaffold in this complex, linking the E2-recruiting module Siah-1 to the substrate-recruiting module Skp1-TBL1. A cell-based functional assay suggests that S100A6 modulates the activity of SCF-TBL1. The results from the cell-based experiments could be enhanced if it were possible to selectively inhibit S100A6-SIP interactions without perturbing any other functions of the two proteins. To this end, the structure of the S100A6-SIP complex was determined in solution by NMR and the strength of the interaction was characterized by isothermal titration calorimetry. In an initial step, the minimal S100A6 binding region in SIP was mapped to a 31-residue fragment (Ser189-Arg219) in the C-terminal domain. The structure of the S100A6-SIP(189-219) complex revealed that SIP(189-219) forms two helices, the first of which (Met193-Tyr200) interacts with S100A6 in a canonical binding mode. The second helix (Met207-Val216) lies over the S100A6 dimer interface, a mode of binding to S100A6 that has not previously been observed for any target bound to an S100 protein. A series of structure-based SIP mutations showed reduced S100A6 binding affinity, setting the stage for direct functional analysis of S100A6-SIP interactions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.