ArticleNature communications2019
Mycobacterial dynamin-like protein IniA mediates membrane fission.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 47 citations in OpenAlex.
- A Pilot Proteomics Analysis ofInternational journal of molecular sciences · 2026Article
- The Cyclic Di-GMP Receptor HpoR Modulates Mycobacterial Multidrug Susceptibility by Regulating IniBAC-Mediated Envelope Permeability.Microorganisms · 2026Article
- Extracellular Vesicles of Mycobacterium tuberculosis Serve as a Virulence Factor - Current Research Applications.Current microbiology · 2026Review
- Binding of Bacillus subtilis dynamin-like protein DynA to the bacterial membrane is essential for effective phage defense.The FEBS journal · 2026Article
- A special latch in yeast mitofusin guarantees mitochondrial fusion by stabilizing self-assembly.Nature communications · 2025Article
- Risk factors associated with morbidity and unfavorable treatment outcome in drug-resistant pulmonary tuberculosis: a case-control study.Precision clinical medicine · 2025Article
- Article
- Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025Review
- Identification of gene targets that potentiate the action of rifampicin onMicrobiology (Reading, England) · 2024Article
- A dynamin superfamily-like pseudoenzyme coordinates with MICOS to promote cristae architecture.Current biology : CB · 2024Article
- Review
- Transcriptomic responses to antibiotic exposure inAntimicrobial agents and chemotherapy · 2024Article
- Nanoenzymes: A Radiant Hope for the Early Diagnosis and Effective Treatment of Breast and Ovarian Cancers.International journal of nanomedicine · 2024Review
- A DRP-like pseudoenzyme coordinates with MICOS to promote cristae architecture.bioRxiv : the preprint server for biology · 2023Article
- Dynamin-like proteins mediate extracellular vesicle secretion in Mycobacterium tuberculosis.EMBO reports · 2023Article
- SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features.Nature communications · 2023Article
- Cyanobacterial membrane dynamics in the light of eukaryotic principles.Bioscience reports · 2023Article
- DosR's multifaceted role onFrontiers in cellular and infection microbiology · 2023Article
- Fusion activators enhance mitochondrial function.Mitochondrial communications · 2023Article
- Molecular Insight intoPharmaceuticals (Basel, Switzerland) · 2022Article
Corrections and comments
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Authors and funding
13 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycobacterium tuberculosis infection remains a major threat to human health worldwide. Drug treatments against tuberculosis (TB) induce expression of several mycobacterial proteins, including IniA, but its structure and function remain poorly understood. Here, we report the structures of Mycobacterium smegmatis IniA in both the nucleotide-free and GTP-bound states. The structures reveal that IniA folds as a bacterial dynamin-like protein (BDLP) with a canonical GTPase domain followed by two helix-bundles (HBs), named Neck and Trunk. The distal end of its Trunk domain exists as a lipid-interacting (LI) loop, which binds to negatively charged lipids for membrane attachment. IniA does not form detectable nucleotide-dependent dimers in solution. However, lipid tethering indicates nucleotide-independent association of IniA on the membrane. IniA also deforms membranes and exhibits GTP-hydrolyzing dependent membrane fission. These results confirm the membrane remodeling activity of BDLP and suggest that IniA mediates TB drug-resistance through fission activity to maintain plasma membrane integrity.
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Registered trials
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.