ArticleMolecular biology of the cell2016
Septin 9 interacts with kinesin KIF17 and interferes with the mechanism of NMDA receptor cargo binding and transport.
Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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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.
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Who cites it
25 citing papers in PubMed, 36 citations in OpenAlex.
- Impaired Aggrephagy, Interrupted Vesicular Trafficking, and Cellular Stress, Lead to Protein Aggregation, and Synaptic Dysfunction in Cerebellum of Children and Adults with Idiopathic Autism.Cerebellum (London, England) · 2025Article
- The clinical and genetic spectrum of paediatric speech and language disorders.Brain : a journal of neurology · 2025Article
- Septins as membrane influencers: direct play or in association with other cytoskeleton partners.Frontiers in cell and developmental biology · 2023Review
- SEPT9 Upregulation in Satellite Glial Cells Associated with Diabetic Polyneuropathy in a Type 2 Diabetes-like Rat Model.International journal of molecular sciences · 2022Article
- Neuronal-specific septin-3 binds Atg8/LC3B, accumulates and localizes to autophagosomes during induced autophagy.Cellular and molecular life sciences : CMLS · 2022Article
- Right place, right time - Spatial guidance of neuronal morphogenesis by septin GTPases.Current opinion in neurobiology · 2022Review
- Septins guide noncentrosomal microtubules to promote focal adhesion disassembly in migrating cells.Molecular biology of the cell · 2022Article
- Effects ofFrontiers in molecular neuroscience · 2022Article
- Kinesins in Mammalian Spermatogenesis and Germ Cell Transport.Frontiers in cell and developmental biology · 2022Review
- Spatial regulation of microtubule-dependent transport by septin GTPases.Trends in cell biology · 2021Review
- Cellular functions of actin- and microtubule-associated septins.Current biology : CB · 2021Review
- A septin GTPase scaffold of dynein-dynactin motors triggers retrograde lysosome transport.The Journal of cell biology · 2021Article
- Spatial control of membrane traffic in neuronal dendrites.Molecular and cellular neurosciences · 2020Review
- A novel strategy to visualize vesicle-bound kinesins reveals the diversity of kinesin-mediated transport.Traffic (Copenhagen, Denmark) · 2019Article
- Microtubule control of functional architecture in neurons.Current opinion in neurobiology · 2019Review
- Article
- Septin filament coalignment with microtubules depends on SEPT9_i1 and tubulin polyglutamylation, and is an early feature of acquired cell resistance to paclitaxel.Cell death & disease · 2019Article
- Septins are critical regulators of osteoclastic bone resorption.Scientific reports · 2018Article
- Polarity of Neuronal Membrane Traffic Requires Sorting of Kinesin Motor Cargo during Entry into Dendrites by a Microtubule-Associated Septin.Developmental cell · 2018Article
- Network Analysis of UBE3A/E6AP-Associated Proteins Provides Connections to Several Distinct Cellular Processes.Journal of molecular biology · 2018Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Intracellular transport involves the regulation of microtubule motor interactions with cargo, but the underlying mechanisms are not well understood. Septins are membrane- and microtubule-binding proteins that assemble into filamentous, scaffold-like structures. Septins are implicated in microtubule-dependent transport, but their roles are unknown. Here we describe a novel interaction between KIF17, a kinesin 2 family motor, and septin 9 (SEPT9). We show that SEPT9 associates directly with the C-terminal tail of KIF17 and interacts preferentially with the extended cargo-binding conformation of KIF17. In developing rat hippocampal neurons, SEPT9 partially colocalizes and comigrates with KIF17. We show that SEPT9 interacts with the KIF17 tail domain that associates with mLin-10/Mint1, a cargo adaptor/scaffold protein, which underlies the mechanism of KIF17 binding to the NMDA receptor subunit 2B (NR2B). Significantly, SEPT9 interferes with binding of the PDZ1 domain of mLin-10/Mint1 to KIF17 and thereby down-regulates NR2B transport into the dendrites of hippocampal neurons. Measurements of KIF17 motility in live neurons show that SEPT9 does not affect the microtubule-dependent motility of KIF17. These results provide the first evidence of an interaction between septins and a nonmitotic kinesin and suggest that SEPT9 modulates the interactions of KIF17 with membrane cargo.
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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.