ArticleProtein science : a publication of the Protein Society2016
Structural insights into SAM domain-mediated tankyrase oligomerization.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- TBM Hunter: Identify and Score Canonical, Extended, and Unconventional Tankyrase-Binding Motifs in Any Protein.International journal of molecular sciences · 2023Review
- Sticky, Adaptable, and Many-sided: SAM protein versatility in normal and pathological hematopoietic states.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Review
- The Structural Dynamics, Complexity of Interactions, and Functions in Cancer of Multi-SAM Containing Proteins.Cancers · 2023Review
- SAM1 domain of SASH1 harbors distinctive structural heterogeneity.Journal of structural biology · 2022Article
- An Evolutionary Perspective on the Origin, Conservation and Binding Partner Acquisition of Tankyrases.Biomolecules · 2022Article
- The zinc-binding motif in tankyrases is required for the structural integrity of the catalytic ADP-ribosyltransferase domain.Open biology · 2022Article
- Tankyrase regulates epithelial lumen formation via suppression of Rab11 GEFs.The Journal of cell biology · 2021Article
- Tankyrases as modulators of pro-tumoral functions: molecular insights and therapeutic opportunities.Journal of experimental & clinical cancer research : CR · 2021Review
- A FRET-based high-throughput screening platform for the discovery of chemical probes targeting the scaffolding functions of human tankyrases.Scientific reports · 2020Article
- Research Progress on PARP14 as a Drug Target.Frontiers in pharmacology · 2019Review
- PARP family enzymes: regulation and catalysis of the poly(ADP-ribose) posttranslational modification.Current opinion in structural biology · 2018Review
- Regulation of tankyrase activity by a catalytic domain dimer interface.Biochemical and biophysical research communications · 2018Article
- Structural basis for tankyrase-RNF146 interaction reveals noncanonical tankyrase-binding motifs.Protein science : a publication of the Protein Society · 2018Article
- Regulation of Wnt/β-catenin signalling by tankyrase-dependent poly(ADP-ribosyl)ation and scaffolding.British journal of pharmacology · 2017Review
- Tankyrase1-mediated poly(ADP-ribosyl)ation of TRF1 maintains cell survival after telomeric DNA damage.Nucleic acids research · 2017Article
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4 authors.
Funding
Abstract
Tankyrase 1 (TNKS1; a.k.a. ARTD5) and tankyrase 2 (TNKS2; a.k.a ARTD6) are highly homologous poly(ADP-ribose) polymerases (PARPs) that function in a wide variety of cellular processes including Wnt signaling, Src signaling, Akt signaling, Glut4 vesicle translocation, telomere length regulation, and centriole and spindle pole maturation. Tankyrase proteins include a sterile alpha motif (SAM) domain that undergoes oligomerization in vitro and in vivo. However, the SAM domains of TNKS1 and TNKS2 have not been structurally characterized and the mode of oligomerization is not yet defined. Here we model the SAM domain-mediated oligomerization of tankyrase. The structural model, supported by mutagenesis and NMR analysis, demonstrates a helical, homotypic head-to-tail polymer that facilitates TNKS self-association. Furthermore, we show that TNKS1 and TNKS2 can form (TNKS1 SAM-TNKS2 SAM) hetero-oligomeric structures mediated by their SAM domains. Though wild-type tankyrase proteins have very low solubility, model-based mutations of the SAM oligomerization interface residues allowed us to obtain soluble TNKS proteins. These structural insights will be invaluable for the functional and biophysical characterization of TNKS1/2, including the role of TNKS oligomerization in protein poly(ADP-ribosyl)ation (PARylation) and PARylation-dependent ubiquitylation.
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