ArticleProceedings of the National Academy of Sciences of the United States of America2007
Structural insights into the interaction of the evolutionarily conserved ZPR1 domain tandem with eukaryotic EF1A, receptors, and SMN complexes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 49 citations in OpenAlex.
- Survival motor neuron protein-independent amelioration of spinal muscular atrophy by pharmacological inhibition of c-Jun-NHBrain communications · 2026Article
- Structural insights into CDF1 accumulation on the CONSTANS promoter via a plant-specific DNA-binding domain.Nature plants · 2025Article
- Assessment of Reference Genes Stability in Cortical Bone of Obese and Diabetic Mice.Diabetes, metabolic syndrome and obesity : targets and therapy · 2024Article
- Role of senataxin in R-loop-mediated neurodegeneration.Brain communications · 2024Review
- A Zpr1 co-chaperone mediates folding of eukaryotic translation elongation factor 1A via a GTPase cycle.Molecular cell · 2023Article
- Zinc-finger protein Zpr1 is a bespoke chaperone essential for eEF1A biogenesis.Molecular cell · 2023Article
- Pan-Cancer Profiling and Digital Pathology Analysis Reveal Negative Prognostic Biomarker ZPR1 Associated with Immune Infiltration and Treatment Response in Hepatocellular Carcinoma.Journal of hepatocellular carcinoma · 2023Article
- Zinc finger protein ZPR1: promising survival motor neuron protein-dependent modifier for the rescue of spinal muscular atrophy.Neural regeneration research · 2022Article
- Mutation in senataxin alters the mechanism of R-loop resolution in amyotrophic lateral sclerosis 4.Brain : a journal of neurology · 2022Article
- The phospho-landscape of the survival of motoneuron protein (SMN) protein: relevance for spinal muscular atrophy (SMA).Cellular and molecular life sciences : CMLS · 2022Review
- Article
- R-loop Mediated DNA Damage and Impaired DNA Repair in Spinal Muscular Atrophy.Frontiers in cellular neuroscience · 2022Review
- Localization and Functional Roles of Components of the Translation Apparatus in the Eukaryotic Cell Nucleus.Cells · 2021Review
- On the Need to Tell Apart Fraternal Twins eEF1A1 and eEF1A2, and Their Respective Outfits.International journal of molecular sciences · 2021Review
- High-fat diet-associated cognitive decline: Is zinc finger protein 1 (ZPR1) the molecular connection?Current research in physiology · 2021Review
- ZPR1 prevents R-loop accumulation, upregulates SMN2 expression and rescues spinal muscular atrophy.Brain : a journal of neurology · 2020Article
- ZPR1-Dependent Neurodegeneration Is Mediated by the JNK Signaling Pathway.Journal of experimental neuroscience · 2019Article
- The essential genome of the crenarchaeal model Sulfolobus islandicus.Nature communications · 2018Article
- Crystal structure of the Melampsora lini effector AvrP reveals insights into a possible nuclear function and recognition by the flax disease resistance protein P.Molecular plant pathology · 2018Article
- Deregulation of ZPR1 causes respiratory failure in spinal muscular atrophy.Scientific reports · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic genomes encode a zinc finger protein (ZPR1) with tandem ZPR1 domains. In response to growth stimuli, ZPR1 assembles into complexes with eukaryotic translation elongation factor 1A (eEF1A) and the survival motor neurons protein. To gain insight into the structural mechanisms underlying the essential function of ZPR1 in diverse organisms, we determined the crystal structure of a ZPR1 domain tandem and characterized the interaction with eEF1A. The ZPR1 domain consists of an elongation initiation factor 2-like zinc finger and a double-stranded beta helix with a helical hairpin insertion. ZPR1 binds preferentially to GDP-bound eEF1A but does not directly influence the kinetics of nucleotide exchange or GTP hydrolysis. However, ZPR1 efficiently displaces the exchange factor eEF1Balpha from preformed nucleotide-free complexes, suggesting that it may function as a negative regulator of eEF1A activation. Structure-based mutational and complementation analyses reveal a conserved binding epitope for eEF1A that is required for normal cell growth, proliferation, and cell cycle progression. Structural differences between the ZPR1 domains contribute to the observed functional divergence and provide evidence for distinct modalities of interaction with eEF1A and survival motor neuron complexes.
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