ArticleThe Journal of cell biology2019
MAP7 family proteins regulate kinesin-1 recruitment and activation.
Article in The Journal of cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.
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Who cites it
92 citing papers in PubMed.
- Microtubule-Associated Proteins: From Dynamic Regulation of Microtubules to Cellular Architecture.Cells · 2026Review
- Structural basis of kinesin-1 autoinhibition and its control of microtubule-based motility.Science advances · 2026Article
- Article
- Motor-Assisted Co-Migration of Intracellular Organelles and Microtubules as a Mechanism for Directed Cargo Transport.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Article
- Rules of the road: how to turn off kinesin motors.The Biochemical journal · 2026Review
- FBXW7 regulates MAP7 through ubiquitination to affect the phenotypic characteristics and paclitaxel sensitivity of paclitaxel-resistant lung adenocarcinoma cells.European journal of medical research · 2025Article
- Structure and mechanism of microtubule stabilization and motor regulation by MAP9.bioRxiv : the preprint server for biology · 2025Article
- Cell cycle-regulated tug-of-war between microtubule motors positions major trafficking organelles.bioRxiv : the preprint server for biology · 2025Article
- KASH proteins transform from passive tethers to dynamic conductors of motor-driven nuclear dynamics.Current opinion in cell biology · 2025Review
- Accessibility of the unstructured α-tubulin C-terminal tail is controlled by microtubule lattice conformation.bioRxiv : the preprint server for biology · 2025Article
- Modeling human retinal ganglion cell axonal outgrowth, development, and pathology using pluripotent stem cell-based microfluidic platforms.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A novel MAP7D1 mutation causes mitotic defects and RPS14 accumulation in Shwachman-Diamond syndrome patient cells.Disease models & mechanisms · 2025Article
- Motor clustering enhances kinesin-driven vesicle transport.Biophysical journal · 2025Article
- Genome wide locus-specific ancestry analysis revealed adaptive admixtures in crossbred cattle of India.Scientific reports · 2025Article
- Peripheral positioning of lysosomes supports melanoma aggressiveness.Nature communications · 2025Article
- Active microtubule-actin cross-talk mediated by a nesprin-2G-kinesin complex.Science advances · 2025Article
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Engine breakdown of lysosomes and related organelles and the resulting physiology.Frontiers in cell and developmental biology · 2025Review
- Tracking Single Kinesin in Live Cells Using MINFLUX.Methods in molecular biology (Clifton, N.J.) · 2025Article
32 more citing papers are in PubMed but not listed here.
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Authors and funding
17 authors.
Funding
Abstract
Kinesin-1 is responsible for microtubule-based transport of numerous cellular cargoes. Here, we explored the regulation of kinesin-1 by MAP7 proteins. We found that all four mammalian MAP7 family members bind to kinesin-1. In HeLa cells, MAP7, MAP7D1, and MAP7D3 act redundantly to enable kinesin-1-dependent transport and microtubule recruitment of the truncated kinesin-1 KIF5B-560, which contains the stalk but not the cargo-binding and autoregulatory regions. In vitro, purified MAP7 and MAP7D3 increase microtubule landing rate and processivity of kinesin-1 through transient association with the motor. MAP7 proteins promote binding of kinesin-1 to microtubules both directly, through the N-terminal microtubule-binding domain and unstructured linker region, and indirectly, through an allosteric effect exerted by the kinesin-binding C-terminal domain. Compared with MAP7, MAP7D3 has a higher affinity for kinesin-1 and a lower affinity for microtubules and, unlike MAP7, can be cotransported with the motor. We propose that MAP7 proteins are microtubule-tethered kinesin-1 activators, with which the motor transiently interacts as it moves along microtubules.
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