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| http://dx.doi.org/10.1038/cr.2014.69 | DOI Listing |
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Dynein-1 is a microtubule motor responsible for the transport of cytoplasmic cargoes. Activation of motility requires it first overcome an autoinhibited state prior to its assembly with dynactin and a cargo adaptor. Studies suggest that Lis1 may relieve dynein's autoinhibited state.
View Article and Find Full Text PDFNde1 Promotes Lis1 Binding to Full-Length Autoinhibited Human Dynein-1.
bioRxiv
December 2024
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06511, USA.
Cytoplasmic dynein-1 (dynein) is the primary motor for the retrograde transport of intracellular cargoes along microtubules. The activation of the dynein transport machinery requires the opening of its autoinhibited Phi conformation by Lis1 and Nde1/Ndel1, but the underlying mechanism remains unclear. Using biochemical reconstitution and cryo-electron microscopy, we show that Nde1 significantly enhances Lis1 binding to autoinhibited dynein and facilitates the opening of Phi.
View Article and Find Full Text PDFGenome-scale requirements for dynein-based transport revealed by a high-content arrayed CRISPR screen.
J Cell Biol
May 2024
Cell Biology Division, Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.
Article Synopsis
- Dynein is an important motor protein that helps organize cells, but its production and function are not well understood.
- Researchers conducted a CRISPR screen on human cells to identify genes that affect dynein's ability to transport cellular structures, leading to the discovery of 195 relevant gene targets.
- One notable finding was that the RNA-binding protein SUGP1 enhances dynein function by supporting the activity of another protein, LIS1, which plays a role in cargo movement within cells.
Dynein and dynactin move long-range but are delivered separately to the axon tip.
J Cell Biol
May 2024
Division of Structural Studies, Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.
Axonal transport is essential for neuronal survival. This is driven by microtubule motors including dynein, which transports cargo from the axon tip back to the cell body. This function requires its cofactor dynactin and regulators LIS1 and NDEL1.
View Article and Find Full Text PDFConserved roles for the dynein intermediate chain and Ndel1 in assembly and activation of dynein.
Nat Commun
September 2023
Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA, 95616, USA.
Article Synopsis
- Microtubule motor cytoplasmic dynein requires a specific complex assembly involving dynein, dynactin, and adapter proteins for effective transport within cells.
- Initial assumptions about the interaction between dynein and dynactin have been challenged by new cryo-EM structures that did not confirm earlier findings, suggesting a more complex relationship.
- The study identifies the N-terminus of the dynein intermediate chain as a crucial site for binding both dynactin and Ndel1, indicating the importance of a sequential process in dynein activation that involves multiple proteins like LIS1.
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