ArticleThe Journal of biological chemistry2011
Stalk domain of the dynamin-like MxA GTPase protein mediates membrane binding and liposome tubulation via the unstructured L4 loop.
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 43 papers.
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Who cites it
43 citing papers in PubMed, 70 citations in OpenAlex.
- Binding of Bacillus subtilis dynamin-like protein DynA to the bacterial membrane is essential for effective phage defense.The FEBS journal · 2026Article
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- Recent updates of interferon-derived myxovirus resistance protein A as a biomarker for acute viral infection.European journal of medical research · 2024Review
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- The Antiviral Activity of Equine Mx1 against Thogoto Virus Is Determined by the Molecular Structure of Its Viral Specificity Region.Journal of virology · 2023Article
- Article
- Mx genes: host determinants controlling influenza virus infection and trans-species transmission.Human genetics · 2020Review
- The anti-viral dynamin family member MxB participates in mitochondrial integrity.Nature communications · 2020Article
- Human Antiviral Protein MxA Forms Novel Metastable Membraneless Cytoplasmic Condensates Exhibiting Rapid Reversible Tonicity-Driven Phase Transitions.Journal of virology · 2019Article
- Interferon-Inducible Myxovirus Resistance Proteins: Potential Biomarkers for Differentiating Viral from Bacterial Infections.Clinical chemistry · 2019Review
- Structural Insights into the Mechanism of Dynamin Superfamily Proteins.Trends in cell biology · 2019Review
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- Article
- Porcine Mx1 Protein Inhibits Classical Swine Fever Virus Replication by Targeting Nonstructural Protein NS5B.Journal of virology · 2018Article
- Tetrahymena dynamin-related protein 6 self-assembles independent of membrane association.Journal of biosciences · 2018Article
- SMARCA2-regulated host cell factors are required for MxA restriction of influenza A viruses.Scientific reports · 2018Article
- Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET.Nature communications · 2017Article
- Mx Is Not Responsible for the Antiviral Activity of Interferon-α against Japanese Encephalitis Virus.Viruses · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human MxA protein is an interferon-induced large GTPase with antiviral activity against a wide range of viruses, including influenza viruses. Recent structural data demonstrated that MxA oligomerizes into multimeric filamentous or ring-like structures by virtue of its stalk domain. Here, we show that negatively charged lipid membranes support MxA self-assembly. Like dynamin, MxA assembled around spherical liposomes inducing liposome tubulation. Cryo-transmission electron microscopy revealed that MxA oligomers around liposomes have a "T-bar" shape similar to dynamin. Moreover, biochemical assays indicated that the unstructured L4 loop of the MxA stalk serves as the lipid-binding moiety, and mutational analysis of L4 revealed that a stretch of four lysine residues is critical for binding. The orientation of the MxA molecule within the membrane-associated oligomer is in agreement with the proposed topology of MxA oligomers based on crystallographic data. Although oligomerization of wild-type MxA around liposomes led to the creation of helically decorated tubes similar to those formed by dynamin, this lipid interaction did not stimulate GTPase activity, in sharp contrast to the assembly-stimulated nucleotide hydrolysis observed with dynamin. Moreover, MxA readily self-assembles into rings at physiological conditions, as opposed to dynamin which self-assembles only at low salt conditions or onto lipids. Thus, the present results indicate that the oligomeric structures formed by MxA critically differ from those of dynamin.
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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.