ArticleProceedings of the National Academy of Sciences of the United States of America2013
Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. 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, 66 citations in OpenAlex.
- Inter-Organelle Membrane Contact Sites as Physiological Regulatory Hubs in the Brain: From Neurons to Glial Cells.Biomolecules · 2026Review
- Tubular ER dysfunction in neurodegenerative diseases.Neurobiology of disease · 2025Review
- Article
- Visualizing ER-phagy and ER architecture in vivo.The Journal of cell biology · 2024Article
- ARL6IP1 gene delivery reduces neuroinflammation and neurodegenerative pathology in hereditary spastic paraplegia model.The Journal of experimental medicine · 2024Article
- Yeast lunapark regulates the formation ofiScience · 2023Article
- Drosophila Atlastin regulates synaptic vesicle mobilization independent of bone morphogenetic protein signaling.Biological research · 2023Article
- Protrudin-mediated ER-endosome contact sites promote phagocytosis.Cellular and molecular life sciences : CMLS · 2023Article
- ERnet: a tool for the semantic segmentation and quantitative analysis of endoplasmic reticulum topology.Nature methods · 2023Article
- The interconnection of endoplasmic reticulum and microtubule and its implication in Hereditary Spastic Paraplegia.Computational and structural biotechnology journal · 2023Review
- Evolution of factors shaping the endoplasmic reticulum.Traffic (Copenhagen, Denmark) · 2022Article
- Protrudin regulates FAK activation, endothelial cell migration and angiogenesis.Cellular and molecular life sciences : CMLS · 2022Article
- Reconstitution of human atlastin fusion activity reveals autoinhibition by the C terminus.The Journal of cell biology · 2022Article
- Exploring the eukaryotic Yip and REEP/Yop superfamily of membrane-shaping adapter proteins (MSAPs): A cacophony or harmony of structure and function?Frontiers in molecular biosciences · 2022Review
- Protein disulfide isomerase A6 promotes the repair of injured nerve through interactions with spastin.Frontiers in molecular neuroscience · 2022Article
- Molecular and cellular mechanisms of spastin in neural development and disease (Review).International journal of molecular medicine · 2021Review
- Intertwined and Finely Balanced: Endoplasmic Reticulum Morphology, Dynamics, Function, and Diseases.Cells · 2021Review
- The structure and global distribution of the endoplasmic reticulum network are actively regulated by lysosomes.Science advances · 2020Article
- Protrudin-deficient mice manifest depression-like behavior with abnormalities in activity, attention, and cued fear-conditioning.Molecular brain · 2020Article
- Protrudin functions from the endoplasmic reticulum to support axon regeneration in the adult CNS.Nature communications · 2020Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Hereditary spastic paraplegias are inherited neurological disorders characterized by progressive lower-limb spasticity and weakness. Although more than 50 genetic loci are known [spastic gait (SPG)1 to -57], over half of hereditary spastic paraplegia cases are caused by pathogenic mutations in four genes encoding proteins that function in tubular endoplasmic reticulum (ER) network formation: atlastin-1 (SPG3A), spastin (SPG4), reticulon 2 (SPG12), and receptor expression-enhancing protein 1 (SPG31). Here, we show that the SPG33 protein protrudin contains hydrophobic, intramembrane hairpin domains, interacts with tubular ER proteins, and functions in ER morphogenesis by regulating the sheet-to-tubule balance and possibly the density of tubule interconnections. Protrudin also interacts with KIF5 and harbors a Rab-binding domain, a noncanonical FYVE (Fab-1, YGL023, Vps27, and EEA1) domain, and a two phenylalanines in an acidic tract (FFAT) domain and, thus, may also function in the distribution of ER tubules via ER contacts with the plasma membrane or other organelles.
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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.