ArticlePloS one2010
Structural transformation of the tandem ubiquitin-interacting motifs in ataxin-3 and their cooperative interactions with ubiquitin chains.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Polyglutamine-Expanded Ataxin-3 Accelerates CFTR Degradation Through K63-Linked Ubiquitination to Exacerbate Microglial Inflammation.ASN neuro · 2026Article
- Evolutionary model of repeat insertions in Ataxin-3 traces the origin of the polyglutamine stretch to an ancestral ubiquitin binding module.Protein science : a publication of the Protein Society · 2024Article
- ATXN3: a multifunctional protein involved in the polyglutamine disease spinocerebellar ataxia type 3.Expert reviews in molecular medicine · 2024Review
- K48- and K63-linked ubiquitin chain interactome reveals branch- and length-specific ubiquitin interactors.Life science alliance · 2024Article
- Mutant Ataxin-3-Containing Aggregates (MATAGGs) in Spinocerebellar Ataxia Type 3: Dynamics of the Disorder.Molecular neurobiology · 2021Review
- The Structural Properties in Solution of the Intrinsically Mixed Folded Protein Ataxin-3.Biophysical journal · 2018Article
- K63-linked polyubiquitin chains bind to DNA to facilitate DNA damage repair.Science signaling · 2018Article
- Identification of a novel site of interaction between ataxin-3 and the amyloid aggregation inhibitor polyglutamine binding peptide 1.European journal of mass spectrometry (Chichester, England) · 2018Article
- Tandem UIMs confer Lys48 ubiquitin chain substrate preference to deubiquitinase USP25.Scientific reports · 2017Article
- Effects of the enlargement of polyglutamine segments on the structure and folding of ataxin-2 and ataxin-3 proteins.Journal of biomolecular structure & dynamics · 2017Article
- The 2.2-Angstrom resolution crystal structure of the carboxy-terminal region of ataxin-3.FEBS open bio · 2016Article
- Ataxin-3 phosphorylation decreases neuronal defects in spinocerebellar ataxia type 3 models.The Journal of cell biology · 2016Article
- Article
- Review
- Aggregation of polyglutamine-expanded ataxin-3 sequesters its specific interacting partners into inclusions: implication in a loss-of-function pathology.Scientific reports · 2014Article
- Ubiquitin-interacting motifs confer full catalytic activity, but not ubiquitin chain substrate specificity, to deubiquitinating enzyme USP37.The Journal of biological chemistry · 2014Article
- Zinc-dependent interaction between JAB1 and pre-S2 mutant large surface antigen of hepatitis B virus and its implications for viral hepatocarcinogenesis.Journal of virology · 2013Article
- Ataxin-3 is a multivalent ligand for the parkin Ubl domain.Biochemistry · 2013Article
- Trinucleotide repeats: a structural perspective.Frontiers in neurology · 2013Article
- Poly-small ubiquitin-like modifier (PolySUMO)-binding proteins identified through a string search.The Journal of biological chemistry · 2012Article
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Authors and funding
9 authors.
Funding
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Abstract
The ubiquitin-interacting motif (UIM) is a short peptide with dual function of binding ubiquitin (Ub) and promoting ubiquitination. We elucidated the structures and dynamics of the tandem UIMs of ataxin-3 (AT3-UIM12) both in free and Ub-bound forms. The solution structure of free AT3-UIM12 consists of two α-helices and a flexible linker, whereas that of the Ub-bound form is much more compact with hydrophobic contacts between the two helices. NMR dynamics indicates that the flexible linker becomes rigid when AT3-UIM12 binds with Ub. Isothermal titration calorimetry and NMR titration demonstrate that AT3-UIM12 binds diUb with two distinct affinities, and the linker plays a critical role in association of the two helices in diUb binding. These results provide an implication that the tandem UIM12 interacts with Ub or diUb in a cooperative manner through an allosteric effect and dynamics change of the linker region, which might be related to its recognitions with various Ub chains and ubiquitinated substrates.
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