ArticleThe Journal of biological chemistry2020
Structure of spastin bound to a glutamate-rich peptide implies a hand-over-hand mechanism of substrate translocation.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 53 citations in OpenAlex.
- Microtubule-Associated Proteins: From Dynamic Regulation of Microtubules to Cellular Architecture.Cells · 2026Review
- Genotype-structure-phenotype correlations define divergent natural history in early-onset spastic paraplegia type 4.Brain : a journal of neurology · 2026Article
- Expanding Hereditary Spastic Paraplegias Limits: Biallelic SPAST Variants in Cerebral Palsy Mimics.Annals of clinical and translational neurology · 2026Article
- Elastic analysis bridges structure and dynamics of an AAA+ molecular motor.PLoS computational biology · 2025Article
- A large-scale curated and filterable dataset for cryo-EM foundation model pre-training.Scientific data · 2025Article
- Role of Residues Undergoing Hereditary Spastic Paraplegias Mutations: Insights from Simulating the Spiral to Ring Transition in Katanin.Journal of chemical information and modeling · 2025Article
- Repeated Exposure to Sevoflurane in Neonatal Mice Induces Cognitive and Synaptic Impairments in a TTLL6-Mediated Tubulin Polyglutamylation Manner.CNS neuroscience & therapeutics · 2025Article
- Unraveling Isoform Complexity: The Roles of M1- and M87-Spastin in Spastic Paraplegia 4 (SPG4).Movement disorders : official journal of the Movement Disorder Society · 2025Review
- Microtubule-binding domains in Katanin p80 subunit are essential for severing activity in C. elegans.The Journal of cell biology · 2024Article
- Tau oligomerization on microtubules in health and disease.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Structure of the human ATAD2 AAA+ histone chaperone reveals mechanism of regulation and inter-subunit communication.Communications biology · 2023Article
- Visualization of the Cdc48 AAA+ ATPase protein unfolding pathway.bioRxiv : the preprint server for biology · 2023Article
- Combinatorial and antagonistic effects of tubulin glutamylation and glycylation on katanin microtubule severing.Developmental cell · 2022Article
- AAA+ protease-adaptor structures reveal altered conformations and ring specialization.Nature structural & molecular biology · 2022Article
- Article
- Multiple roles for the cytoskeleton in ALS.Experimental neurology · 2022Review
- Molecular dynamics of DNA translocation by FtsK.Nucleic acids research · 2022Article
- The force required to remove tubulin from the microtubule lattice by pulling on its α-tubulin C-terminal tail.Nature communications · 2022Article
- Active conformation of the p97-p47 unfoldase complex.Nature communications · 2022Article
- Conserved structural elements specialize ATAD1 as a membrane protein extraction machine.eLife · 2022Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Many members of the AAA+ ATPase family function as hexamers that unfold their protein substrates. These AAA unfoldases include spastin, which plays a critical role in the architecture of eukaryotic cells by driving the remodeling and severing of microtubules, which are cytoskeletal polymers of tubulin subunits. Here, we demonstrate that a human spastin binds weakly to unmodified peptides from the C-terminal segment of human tubulin α1A/B. A peptide comprising alternating glutamate and tyrosine residues binds more tightly, which is consistent with the known importance of glutamylation for spastin microtubule severing activity. A cryo-EM structure of the spastin-peptide complex at 4.2 Å resolution revealed an asymmetric hexamer in which five spastin subunits adopt a helical, spiral staircase configuration that binds the peptide within the central pore, whereas the sixth subunit of the hexamer is displaced from the peptide/substrate, as if transitioning from one end of the helix to the other. This configuration differs from a recently published structure of spastin from
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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.