ArticleThe Journal of biological chemistry2011
Structure and function of the N-terminal nucleolin binding domain of nuclear valosin-containing protein-like 2 (NVL2) harboring a nucleolar localization signal.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 22 citations in OpenAlex.
- Article
- New Functional Motifs for the Targeted Localization of Proteins to the Nucleolus inInternational journal of molecular sciences · 2024Article
- Identification of nuclear valosin-containing-protein-like as a target of anti-nuclear autoantibodies in systemic sclerosis.Frontiers in medicine · 2024Article
- Structural Integrity of Nucleolin Is Required to Suppress TDP-43-Mediated Cytotoxicity in Yeast and Human Cell Models.International journal of molecular sciences · 2023Article
- Communication network within the essential AAA-ATPase Rix7 drives ribosome assembly.PNAS nexus · 2022Article
- Reciprocal Inhibition of Immunogenic Performance in Mice of Two Potent DNA Immunogens Targeting HCV-Related Liver Cancer.Microorganisms · 2021Article
- Shaping the Nascent Ribosome: AAA-ATPases in Eukaryotic Ribosome Biogenesis.Biomolecules · 2019Review
- The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs.Nature communications · 2019Article
- Cryo-EM structure of the essential ribosome assembly AAA-ATPase Rix7.Nature communications · 2019Article
- A peptidylic inhibitor for neutralizing expandedRNA (New York, N.Y.) · 2018Article
- A brain-targeting lipidated peptide for neutralizing RNA-mediated toxicity in Polyglutamine Diseases.Scientific reports · 2017Article
- Structural Analysis Reveals Features of Ribosome Assembly Factor Nsa1/WDR74 Important for Localization and Interaction with Rix7/NVL2.Structure (London, England : 1993) · 2017Article
- Nucleocytoplasmic shuttling of valosin-containing protein (VCP/p97) regulated by its N domain and C-terminal region.Biochimica et biophysica acta · 2015Article
- A nucleolar AAA-NTPase is required for parasite division.Molecular microbiology · 2013Article
- The power of AAA-ATPases on the road of pre-60S ribosome maturation--molecular machines that strip pre-ribosomal particles.Biochimica et biophysica acta · 2012Review
- A repeated triple lysine motif anchors complexes containing bone sialoprotein and the type XI collagen A1 chain involved in bone mineralization.The Journal of biological chemistryArticle
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7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The N-terminal regions of AAA-ATPases (ATPase associated with various cellular activities) often contain a domain that defines the distinct functions of the enzymes, such as substrate specificity and subcellular localization. As described herein, we have determined the solution structure of an N-terminal unique domain isolated from nuclear valosin-containing protein (VCP)-like protein 2 (NVL2(UD)). NVL2(UD) contains three α helices with an organization resembling that of a winged helix motif, whereas a pair of β-strands is missing. The structure is unique and distinct from those of other known type II AAA-ATPases, such as VCP. Consequently, we identified nucleolin from a HeLa cell extract as a binding partner of this domain. Nucleolin contains a long (∼300 amino acids) intrinsically unstructured region, followed by the four tandem RNA recognition motifs and the C-terminal glycine/arginine-rich domain. Binding analyses revealed that NVL2(UD) potentially binds to any of the combinations of two successive RNA binding domains in the presence of RNA. Furthermore, NVL2(UD) has a characteristic loop, in which the key basic residues RRKR are exposed to the solvent at the edge of the molecule. The mutation study showed that these residues are necessary and sufficient for nucleolin-RNA complex binding as well as nucleolar localization. Based on the observations presented above, we propose that NVL2 serves as an unfoldase for the nucleolin-RNA complex. As inferred from its RNA dependence and its ATPase activity, NVL2 might facilitate the dissociation and recycling of nucleolin, thereby promoting efficient ribosome biogenesis.
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