ArticleBiochimica et biophysica acta. General subjects2019
The specificity of ubiquitin binding to ubiquilin-1 is regulated by sequences besides its UBA domain.
Article in Biochimica et biophysica acta. General subjects, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- UBQLN2 is necessary for UBE3A-mediated proteasomal degradation of the domesticated retroelement PEG10.Journal of cell science · 2025Article
- UBQLN2 in neurodegenerative disease: mechanistic insights and emerging therapeutic potential.Biochemical Society transactions · 2025Review
- UBQLN1 links proteostasis and mitochondria function to telomere maintenance in human embryonic stem cells.Stem cell research & therapy · 2024Article
- UBQLN2 undergoes a reversible temperature-induced conformational switch that regulates binding with HSPA1B: ALS/FTD mutations cripple the switch but do not destroy HSPA1B binding.Biochimica et biophysica acta. General subjects · 2023Article
- Mechanistic insights into enhancement or inhibition of phase separation by different polyubiquitin chains.EMBO reports · 2022Article
- Article
- Ubiquitin-Modulated Phase Separation of Shuttle Proteins: Does Condensate Formation Promote Protein Degradation?BioEssays : news and reviews in molecular, cellular and developmental biology · 2020Review
- Structure, dynamics and functions of UBQLNs: at the crossroads of protein quality control machinery.The Biochemical journal · 2020Review
- Ubiquilin-2 differentially regulates polyglutamine disease proteins.Human molecular genetics · 2020Article
- ALS/FTD mutations in UBQLN2 impede autophagy by reducing autophagosome acidification through loss of function.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Cell-Clearing Systems Bridging Repeat Expansion Proteotoxicity and Neuromuscular Junction Alterations in ALS and SBMA.International journal of molecular sciences · 2020Review
- Promiscuous Roles of Autophagy and Proteasome in Neurodegenerative Proteinopathies.International journal of molecular sciences · 2020Review
- Global proteomics of Ubqln2-based murine models of ALS.The Journal of biological chemistryArticle
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
UBQLN proteins regulate proteostasis by facilitating clearance of misfolded proteins through the proteasome and autophagy degradation pathways. Consistent with its proteasomal function, UBQLN proteins contain both UBL and UBA domains, which bind subunits of the proteasome, including the S5a subunit, and ubiquitin chains, respectively. Conclusions regarding the binding properties of UBQLN proteins have been derived principally through studies of its individual domains, not the full-length (FL) proteins. Here we describe the in vitro binding properties of FL-UBQLN1 with the S5a subunit of the proteasome and two different lysine-linked (K48 or K63) ubiquitin chains. We show that in contrast to its isolated UBA domain, which binds almost equally well with both K48 and K63 ubiquitin chains, FL UBQLN1 binds preferentially with K63 chains. Furthermore, we show that deletion of the UBL domain from UBQLN1 abrogates ubiquitin binding. Taken together these results suggest that sequences outside of the UBA domain in UBQLN1 function to regulate the specificity and binding with different ubiquitin moieties. We also show that the UBL domain of UBQLN1 is required for S5a binding and that its binding to UBQLN1, in turn, enhances K48 ubiquitin chain binding to the complex. We discuss the implications of our findings with the known function of UBQLN proteins in protein degradation.
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