ArticleMolecular biology of the cell2010
SPG20 protein spartin is recruited to midbodies by ESCRT-III protein Ist1 and participates in cytokinesis.
Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
47 citing papers in PubMed, 84 citations in OpenAlex.
- 4-Phenylbutyric Acid Improves Gait Ability of UBAP1-Related Spastic Paraplegia Mouse Model: Therapeutic Potential for SPG80.International journal of molecular sciences · 2025Article
- A comparative analysis of paxillin and Hic-5 proximity interactomes.Cytoskeleton (Hoboken, N.J.) · 2025Article
- IST1 regulates select recycling pathways.Traffic (Copenhagen, Denmark) · 2024Article
- The mammalian midbody and midbody remnant are assembly sites for RNA and localized translation.Developmental cell · 2023Article
- The Troyer syndrome protein spartin mediates selective autophagy of lipid droplets.Nature cell biology · 2023Article
- Lipid Polarization during Cytokinesis.Cells · 2022Review
- Article
- Friction-driven membrane scission by the human ESCRT-III proteins CHMP1B and IST1.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- The Role of Spastin in Axon Biology.Frontiers in cell and developmental biology · 2022Review
- Final Exon Frameshift BiallelicBrain sciences · 2021Article
- ESCRT-III-associated proteins and spastin inhibit protrudin-dependent polarised membrane traffic.Cellular and molecular life sciences : CMLS · 2020Article
- A novel missense mutation (c.1006C>T) ofJournal of genetics · 2020Article
- Why Does the Face Predict the Brain? Neural Crest Induction, Craniofacial Morphogenesis, and Neural Circuit Development.Frontiers in physiology · 2020Review
- UBAP1 mutations cause juvenile-onset hereditary spastic paraplegias (SPG80) and impair UBAP1 targeting to endosomes.Journal of human genetics · 2019Article
- Spastin tethers lipid droplets to peroxisomes and directs fatty acid trafficking through ESCRT-III.The Journal of cell biology · 2019Article
- Spastin MIT Domain Disease-Associated Mutations Disrupt Lysosomal Function.Frontiers in neuroscience · 2019Article
- Cytokinesis defects and cancer.Nature reviews. Cancer · 2019Review
- Urine-derived cells: a promising diagnostic tool in Fabry disease patients.Scientific reports · 2018Article
- The role of TGF-β superfamily signaling in neurological disorders.Acta biochimica et biophysica Sinica · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Hereditary spastic paraplegias (HSPs, SPG1-46) are inherited neurological disorders characterized by lower extremity spastic weakness. Loss-of-function SPG20 gene mutations cause an autosomal recessive HSP known as Troyer syndrome. The SPG20 protein spartin localizes to lipid droplets and endosomes, and it interacts with tail interacting protein 47 (TIP47) as well as the ubiquitin E3 ligases atrophin-1-interacting protein (AIP)4 and AIP5. Spartin harbors a domain contained within microtubule-interacting and trafficking molecules (MIT) at its N-terminus, and most proteins with MIT domains interact with specific ESCRT-III proteins. Using yeast two-hybrid and in vitro surface plasmon resonance assays, we demonstrate that the spartin MIT domain binds with micromolar affinity to the endosomal sorting complex required for transport (ESCRT)-III protein increased sodium tolerance (Ist)1 but not to ESCRT-III proteins charged multivesicular body proteins 1-7. Spartin colocalizes with Ist1 at the midbody, and depletion of Ist1 in cells by small interfering RNA significantly decreases the number of cells where spartin is present at midbodies. Depletion of spartin does not affect Ist1 localization to midbodies but markedly impairs cytokinesis. A structure-based amino acid substitution in the spartin MIT domain (F24D) blocks the spartin-Ist1 interaction. Spartin F24D does not localize to the midbody and acts in a dominant-negative manner to impair cytokinesis. These data suggest that Ist1 interaction is important for spartin recruitment to the midbody and that spartin participates in cytokinesis.
Indexed as
Identifiers
What OpenQuestion holds
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.