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Articles by Steven M. Markus
Roles of microtubules and LIS1 in dynein transport machinery assembly - Nature
Abstract Cytoplasmic dynein-1, a microtubule (MT)-based motor protein, requires dynactin and a coiled-coil adaptor to form the processive dynein–dynactin–adaptor (DDA) complex1,2. The roles of MTs and dynein regulator lissencephaly-1 (LIS1) in DDA assembly have remained elusive. Here we use cryo-electron microscopy to determine the structural basis of MT- and LIS1-mediated DDA assembly.
The mechanochemical cycle of reactive full-length human dynein 1 - Nature Structural & Molecular Biology
Abstract Dynein-driven cargo transport has a pivotal role in diverse cellular activities, central to which is dynein’s mechanochemical cycle. Here, we performed a systematic cryo-electron microscopic investigation of the conformational landscape of full-length human dynein 1 in reaction, in various nucleotide conditions, on and off microtubules.
Microtubule motors of opposite polarity cooperate rather than compete in cargo transport - Nature Structural & Molecular Biology
Microtubule-based cargo transport relies on the actions of dynein and kinesins, motors that walk in opposite directions yet act together to ensure appropriate distribution of cargos in cells. Research now provides mechanistic insights into how these seemingly antagonistic motors collaborate, rather than compete, to promote each other’s activities.
Cryo-EM Reveals the Mechanochemical Cycle of Reactive Full-length Human Dynein-1
Abstract Dynein-mediated cargo transport plays pivotal roles in a variety of essential cellular activities, including vesicle trafficking, organelle and nucleus positioning, mitosis and morphogenesis. Central to all these cellular processes is dynein's ATP-dependent mechanochemical cycle.
Conserved roles for the dynein intermediate chain and Ndel1 in assembly and activation of dynein - Nature Communications
Abstract Processive transport by the microtubule motor cytoplasmic dynein requires the regulated assembly of a dynein-dynactin-adapter complex. Interactions between dynein and dynactin were initially ascribed to the dynein intermediate chain N-terminus and the dynactin subunit p150Glued. However, recent cryo-EM structures have not resolved this interaction, questioning its importance. The intermediate chain also interacts with Nde1/Ndel1, which compete with p150Glued for binding.
Pac1/LIS1 stabilizes an uninhibited conformation of dynein to coordinate its localization and activity
Abstract Dynein is a microtubule motor that transports many different cargos in various cell types and contexts. How dynein is regulated to perform these activities with spatial and temporal precision remains unclear. Human dynein is regulated by autoinhibition, whereby intermolecular contacts limit motor activity. Whether this mechanism is conserved throughout evolution, whether it can be affected by extrinsic factors, and its role in regulating dynein function remain unclear.
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