ArticleStructure (London, England : 1993)2016
Selective Binding of AIRAPL Tandem UIMs to Lys48-Linked Tri-Ubiquitin Chains.
Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Blocking TRIM47-mediated HNF4Acta pharmaceutica Sinica. B · 2026Article
- K48- and K63-linked ubiquitin chain interactome reveals branch- and length-specific ubiquitin interactors.Life science alliance · 2024Article
- The role of RNF149 in the pre-emptive quality control substrate ubiquitination.Communications biology · 2023Article
- Promoter Methylation-Regulated Differentially Expressed Genes in Breast Cancer.Breast cancer (Dove Medical Press) · 2023Article
- Panel of Engineered Ubiquitin Variants Targeting the Family of Human Ubiquitin Interacting Motifs.ACS chemical biology · 2022Article
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- The Proteasome and Its Network: Engineering for Adaptability.Cold Spring Harbor perspectives in biology · 2020Review
- Structural insights into ubiquitin recognition and Ufd1 interaction of Npl4.Nature communications · 2019Article
- Tandem UIMs confer Lys48 ubiquitin chain substrate preference to deubiquitinase USP25.Scientific reports · 2017Article
- A single MIU motif of MINDY-1 recognizes K48-linked polyubiquitin chains.EMBO reports · 2017Article
- A Mighty "Protein Extractor" of the Cell: Structure and Function of the p97/CDC48 ATPase.Frontiers in molecular biosciences · 2017Review
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 4 countries.
Funding
Abstract
Lys48-linked ubiquitin chains act as the main targeting signals for protein degradation by the proteasome. Here we report selective binding of AIRAPL, a protein that associates with the proteasome upon exposure to arsenite, to Lys48-linked tri-ubiquitin chains. AIRAPL comprises two ubiquitin-interacting motifs in tandem (tUIMs) that are linked through a flexible inter-UIM region. In the complex crystal structure UIM1 binds the proximal ubiquitin, whereas UIM2 (the double-sided UIM) binds non-symmetrically to the middle and distal ubiquitin moieties on either side of the helix. Specificity of AIRAPL for Lys48-linked ubiquitin chains is determined by UIM2, and the flexible inter-UIM linker increases avidity by placing the two UIMs in an orientation that facilitates binding of the third ubiquitin to UIM1. Unlike middle and proximal ubiquitins, distal ubiquitin binds UIM2 through a novel surface, which leaves the Ile44 hydrophobic patch accessible for binding to the proteasomal ubiquitin receptors.
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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.