ArticleThe Journal of biological chemistry2009
Structural basis for ubiquitin recognition by a novel domain from human phospholipase A2-activating protein.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- PLAA/UFD-3 regulates P-bodies through its intrinsic disordered domain.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The UBX domain in UBXD1 organizes ubiquitin binding at the C-terminus of the VCP/p97 AAA-ATPase.Nature communications · 2023Article
- Chromatin Ubiquitination Guides DNA Double Strand Break Signaling and Repair.Frontiers in cell and developmental biology · 2022Review
- SMARCB1 Promotes Ubiquitination and Degradation of NR4A3 via Direct Interaction Driven by ROS in Vascular Endothelial Cell Injury.Oxidative medicine and cellular longevity · 2020Article
- Computational modeling of Repeat1 region of INI1/hSNF5: An evolutionary link with ubiquitin.Protein science : a publication of the Protein Society · 2016Article
- Doa1 is a MAD adaptor for Cdc48.The Journal of cell biology · 2016Article
- Doa1 targets ubiquitinated substrates for mitochondria-associated degradation.The Journal of cell biology · 2016Article
- The functional interactome landscape of the human histone deacetylase family.Molecular systems biology · 2013Article
- Ubiquitin and its binding domains.Frontiers in bioscience (Landmark edition) · 2012Review
- WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins.Molecular cell · 2010Article
- Solution structure of the N-terminal domain of DC-UbP/UBTD2 and its interaction with ubiquitin.Protein science : a publication of the Protein Society · 2010Article
- Ubiquitin-binding domains - from structures to functions.Nature reviews. Molecular cell biology · 2009Review
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ubiquitin (Ub) is an essential modifier conserved in all eukaryotes from yeast to human. Phospholipase A(2)-activating protein (PLAA), a mammalian homolog of yeast DOA1/UFD3, has been proposed to be able to bind with Ub, which plays important roles in endoplasmic reticulum-associated degradation, vesicle formation, and DNA damage response. We have identified a core domain from the PLAA family ubiquitin-binding region of human PLAA (residues 386-465, namely PFUC) that can bind Ub and elucidated its solution structure and Ub-binding mode by NMR approaches. The PFUC domain possesses equal population of two conformers in solution by cis/trans-isomerization, whereas the two isomers exhibit almost equivalent Ub binding abilities. This domain structure takes a novel fold consisting of four beta-strands and two alpha-helices, and the Ub-binding site on PFUC locates in the surface of alpha2-helix, which is to some extent analogous to those of UBA, CUE, and UIM domains. This study provides structural basis and biochemical information for Ub recognition of the novel PFU domain from a PLAA family protein that may connect ubiquitination and degradation in endoplasmic reticulum-associated degradation.
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