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• W4243817179 abstract "Dynactin might sound like a vitamin supplement, or maybe the latest exercise craze, but it’s a complex structure that is crucial for the function of the microtubule ‘motor’ — cytoplasmic dynein. Well, it consists of 11 different subunits (see Figure). A dimer of p150Glued sticks out to interact with cytoplasmic dynein and microtubules. It’s part of the molecular machinery that drives a whole host of movements within the cell. Almost every organelle that moves towards the slow-growing ends of microtubules uses cytoplasmic dynein, and so also needs dynactin. Cargoes include the Golgi apparatus, ER–Golgi traffic, most endocytic organelles, nuclei and material for retrograde axonal transport. More unusual cargoes include lipid droplets and viral capsids. No. Microtubules are also ‘cargo’. For instance, dynein–dynactin is needed to keep microtubules associated with the centrosome, and contributes to centrosome separation during cell division. Indeed. Dynein and dynactin have vital roles in spindle assembly, where they help to focus microtubules at the spindle poles and keep the poles apart. They also help attach chromosomes to the spindle via kinetochores. And dynactin and dynein localised to cortical sites apparently pull on the microtubule network, so ensuring correct spindle orientation and contributing to pole separation in anaphase B. Yes, rather mysteriously, dynactin binds to microtubule tips. It could be waiting to grab nearby organelles and activate their movement, or it might be binding regulatory and signalling components, so concentrating them at microtubule ends. One such molecule could be the tumour suppressor adenomatous polyposis coli (APC) protein, which associates with EB1, which in turn interacts with dynactin and cytoplasmic dynein. The whole gamut of molecular, genetic, biochemical and cell biological approaches has been used to study dynactin in organisms including yeast, flies, worms and man. One particularly effective tool is dynamitin (surely, one of the corniest names in biology), a component of dynactin that blows the complex into several pieces when present in excess. Somehow or other, dynactin increases the distance that cytoplasmic dynein moves along a microtubule before falling off. It might also be part of a ‘cargo receptor’ to which dynein binds. Dynein can bind to membranes lacking dynactin, but they won’t move without it. It’s also possible that certain other cargoes are transported by dynein on its own. This is one of the least understood aspects of dynactin. To bind to microtubule ends, dynactin needs another protein, CLIP170. Targeting to kinetochores may depend on the interaction of dynamitin with ZW10 protein. Binding to the Golgi apparatus might occur by means of Arp1 binding to a Golgi-specific spectrin. How dynactin associates with other organelles is completely obscure. More potential partners for dynactin and dynein are being reported all the time (such as EB1, pericentrin, NuMA, Eg5, spectrin, protein 4.1, Huntingtin-associated protein and viral proteins). We must wait to see how many of these interactions will stand the test of time. Probably not. A complete loss of dynactin (or cytoplasmic dynein) function is lethal in many animals, probably because of the catastrophic effects on pronuclear migration and cell division. Some dynactin mutations are tolerated (for example, Glued in Drosophila). Fungi can get away without it — under cushy laboratory conditions, at least. Karki S, Holzbaur E: Cytoplasmic dynein and dynactin in cell division and intracellular transport.Curr Opin Cell Biol 1999, 11:45-53. Eckley DM, Gill SR, Melkonian KA, Bingham JB, Goodson HV, Heuser JE, Schroer TA: Analysis of dynactin subcomplexes reveals a novel actin-related protein associated with the Arp1 minifilament pointed end.J Cell Biol 1999, 147:307-319. Schroer T: Structure and function of dynactin.Semin Cell Dev Biol 1996, 7:321-328. Vallee RB, Sheetz MP: Targeting of motor proteins.Science 1996, 271:1539-1544." @default.
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• W4243817179 date "2000-06-01" @default.
• W4243817179 modified "2023-10-13" @default.
• W4243817179 title "Dynactin" @default.
• W4243817179 doi "https://doi.org/10.1016/s0960-9822(00)00550-9" @default.
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