ArticleBMC structural biology2014
Characterization of the SAM domain of the PKD-related protein ANKS6 and its interaction with ANKS3.
Article in BMC structural biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 45 citations in OpenAlex.
- Exploring the BICC1 Interactome in HEK293T Cells: Insights Into RNA-Mediated Protein Networks and Biomolecular Condensates.FASEB bioAdvances · 2026Article
- High Expression of SAMM50 Indicates Poor Clinical Prognosis in Hepatocellular Carcinoma and Represents a Potential Novel Biomarker.Biological procedures online · 2026Article
- Integrating endogenous TurboID and data-independent acquisition mass spectrometry for in vivo proximity labeling.The EMBO journal · 2026Article
- The impact of curation errors in the PDBBind Database on machine learning predictions of protein-protein binding affinity.Database : the journal of biological databases and curation · 2025Article
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- A Deep Dive into the N-Terminus of STIM Proteins: Structure-Function Analysis and Evolutionary Significance of the Functional Domains.Biomolecules · 2024Review
- TheBiomedicines · 2024Review
- Bicc1 ribonucleoprotein complexes specifying organ laterality are licensed by ANKS6-induced structural remodeling of associated ANKS3.PLoS biology · 2023Article
- The Structural Dynamics, Complexity of Interactions, and Functions in Cancer of Multi-SAM Containing Proteins.Cancers · 2023Review
- Per- and polyfluoroalkyl substances, epigenetic age and DNA methylation: a cross-sectional study of firefighters.Epigenomics · 2021Article
- Novel fibrillar structure in the inversin compartment of primary cilia revealed by 3D single-molecule superresolution microscopy.Molecular biology of the cell · 2020Article
- Cilia-localized LKB1 regulates chemokine signaling, macrophage recruitment, and tissue homeostasis in the kidney.The EMBO journal · 2018Article
- Mutations in six nephrosis genes delineate a pathogenic pathway amenable to treatment.Nature communications · 2018Article
- Crystal Structure of Bicc1 SAM Polymer and Mapping of Interactions between the Ciliopathy-Associated Proteins Bicc1, ANKS3, and ANKS6.Structure (London, England : 1993) · 2018Article
- Novel proteins from proteomic analysis of the trunk disease fungusBiochimie open · 2017Article
- Open Sesame: How Transition Fibers and the Transition Zone Control Ciliary Composition.Cold Spring Harbor perspectives in biology · 2017Review
- Article
- ANKS3 is mutated in a family with autosomal recessive laterality defect.Human genetics · 2016Article
- Structural insights into SAM domain-mediated tankyrase oligomerization.Protein science : a publication of the Protein Society · 2016Article
- A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein.Cell communication and signaling : CCS · 2016Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundAutosomal dominant polycystic kidney disease (ADPKD) is the most common genetic disorder leading to end-stage renal failure in humans. In the PKD/Mhm(cy/+) rat model of ADPKD, the point mutation R823W in the sterile alpha motif (SAM) domain of the protein ANKS6 is responsible for disease. SAM domains are known protein-protein interaction domains, capable of binding each other to form polymers and heterodimers. Despite its physiological importance, little is known about the function of ANKS6 and how the R823W point mutation leads to PKD. Recent work has revealed that ANKS6 interacts with a related protein called ANKS3. Both ANKS6 and ANKS3 have a similar domain structure, with ankyrin repeats at the N-terminus and a SAM domain at the C-terminus.
resultsThe SAM domain of ANKS3 is identified as a direct binding partner of the ANKS6 SAM domain. We find that ANKS3-SAM polymerizes and ANKS6-SAM can bind to one end of the polymer. We present crystal structures of both the ANKS3-SAM polymer and the ANKS3-SAM/ANKS6-SAM complex, revealing the molecular details of their association. We also learn how the R823W mutation disrupts ANKS6 function by dramatically destabilizing the SAM domain such that the interaction with ANKS3-SAM is lost.
conclusionsANKS3 is a direct interacting partner of ANKS6. By structurally and biochemically characterizing the interaction between the ANKS3 and ANKS6 SAM domains, our work provides a basis for future investigation of how the interaction between these proteins mediates kidney function.
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