ArticleMethods in molecular biology (Clifton, N.J.)2020
Affinity Purification and Functional Characterization of Dynamin-Related Protein 1.
Article in Methods in molecular biology (Clifton, N.J.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- DRP1 mutations associated with EMPF1 encephalopathy perturb the transcriptional profile and maturation of cortical neurons.Journal of neurodevelopmental disorders · 2026Article
- The Structure of the Drp1 Lattice on Membrane.Journal of molecular biology · 2025Article
- Structural basis for regulated assembly of the mitochondrial fission GTPase Drp1.Nature communications · 2024Article
- Allosteric control of dynamin-related protein 1 through a disordered C-terminal Short Linear Motif.Nature communications · 2024Article
- The AAA-ATPase Yta4/ATAD1 interacts with the mitochondrial divisome to inhibit mitochondrial fission.PLoS biology · 2023Article
- Targeting an allosteric site in dynamin-related protein 1 to inhibit Fis1-mediated mitochondrial dysfunction.Nature communications · 2023Article
- Disease-associated mutations in Drp1 have fundamentally different effects on the mitochondrial fission machinery.Human molecular genetics · 2023Article
- NovelLife science alliance · 2022Article
- Blocked O-GlcNAc cycling alters mitochondrial morphology, function, and mass.Scientific reports · 2021Article
- In vitro and in vivo assays for mitochondrial fission and fusion.Methods in cell biology · 2020Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Purification of dynamin-related proteins is complicated by their oligomeric tendencies. In this chapter, we describe an established purification regime to isolate the mitochondrial fission protein Drp1 using bacterial expression. Key attributes of dynamins include their ability to hydrolyze GTP and self-assemble into larger polymers under specific conditions. Therefore, the GTPase activity of Drp1 should be examined to confirm isolation of functional protein, and we describe a conventional colorimetric assay to assess enzyme activity. To determine the ability of Drp1 to self-assemble, we induce Drp1 polymerization through addition of a non-hydrolyzable GTP analogue. A sedimentation assay provides a quantitative measure of polymerization that complements a qualitative assessment through visualization of Drp1 oligomers using negative-stain electron microscopy (EM). Importantly, we highlight the caveats of affinity tags and the influence that these peptide sequences can have on Drp1 function given their proximity to functional domains.
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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.