ArticleThe Journal of biological chemistry2019
Structural and functional analysis of parameters governing tankyrase-1 interaction with telomeric repeat-binding factor 1 and GDP-mannose 4,6-dehydratase.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed.
- Disrupting the tumor-associated TNKS-USP25 protein-protein interface in cancer: structural basis, druggability, and therapeutic opportunities.RSC advances · 2026Review
- Tankyrases and Their Binding Proteins: Origins of Their Roles in Diverse Cellular Pathways.Cells · 2026Review
- Phosphorylation as a candidate regulatory mechanism for effector recruitment to tankyrase.Royal Society open science · 2025Article
- Deltex and RING-UIM E3 ligases cooperate to create a ubiquitin-ADP-ribose hybrid mark on tankyrase, promoting its stabilization.Science advances · 2025Article
- PARP enzyme de novo synthesis of protein-free poly(ADP-ribose).Molecular cell · 2024Article
- Time-dependent changes in genome-wide gene expression and post-transcriptional regulation across the post-death process in silkworm.DNA research : an international journal for rapid publication of reports on genes and genomes · 2024Article
- Genomic and Transcriptomic Analyses Reveal Multiple Strategies forFoods (Basel, Switzerland) · 2024Article
- Tankyrase-1 regulates RBP-mediated mRNA turnover to promote muscle fiber formation.Nucleic acids research · 2024Article
- TBM Hunter: Identify and Score Canonical, Extended, and Unconventional Tankyrase-Binding Motifs in Any Protein.International journal of molecular sciences · 2023Review
- Genomic and Transcriptomic Analysis Reveal Multiple Strategies for the Cadmium Tolerance inFoods (Basel, Switzerland) · 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
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- Tankyrase inhibition ameliorates lipid disorder via suppression of PGC-1α PARylation in db/db mice.International journal of obesity (2005) · 2020Article
- Nuclear PARPs and genome integrity.Genes & development · 2020Review
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Authors and funding
3 authors.
Funding
Abstract
Human tankyrase-1 (TNKS) is a member of the poly(ADP-ribose) polymerase (PARP) superfamily of proteins that posttranslationally modify themselves and target proteins with ADP-ribose (termed PARylation). The TNKS ankyrin repeat domain mediates interactions with a growing number of structurally and functionally diverse binding partners, linking TNKS activity to multiple critical cell processes, including Wnt signaling, Golgi trafficking, and telomere maintenance. However, some binding partners can engage TNKS without being modified, suggesting that separate parameters influence TNKS interaction and PARylation. Here, we present an analysis of the sequence and structural features governing TNKS interactions with two model binding partners: the PARylated partner telomeric repeat-binding factor 1 (TRF1) and the non-PARylated partner GDP-mannose 4,6-dehydratase (GMD). Using a combination of TNKS-binding assays, PARP activity assays, and analytical ultracentrifugation sedimentation analysis, we found that both the specific sequence of a given TNKS-binding peptide motif and the quaternary structure of individual binding partners play important roles in TNKS interactions. We demonstrate that GMD forms stable 1:1 complexes with the TNKS ankyrin repeat domain; yet, consistent with results from previous studies, we were unable to detect GMD modification. We also report
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