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(a) Upon homodimerization, cytoplasmic dynein-1 (insets 1 and 2, yellow) and dynein-2 (insets 3 and 4, red) intrinsically adopt an autoinhibited configuration (insets 1 and 3) that can be relieved ...
A single type of dynein motor carries out all minus end-directed microtubule transport in the cytoplasm. Several multifunctional adaptors, including dynactin, LIS1, NUDE and NUDEL, Bicaudal D and ...
The new video shows that the first step to activating dynein involves Lis1 attaching to dynein’s motor subunit. Like dynein, Lis1 is also made up of two identical halves. In this first interaction, ...
Using cryo-electron tomography, researchers have uncovered details of how the dynein motor protein drives cilia to beat. Understanding this motion may help to tackle health problems that affect ...
Microtubule motor proteins move across the microtubule, transporting cellular cargo within the cell. They are responsible for mitosis, cellular transport and the movement of organelles.
Using this approach, the team discovered that HIV hitches to dynein by attaching directly to the motor protein, not via BicD2. The motor protein does not start moving right away, though.
Like many machines, cells have motors that help them carry out essential tasks. In the case of division¿a process that goes horribly awry in cancer cells¿a protein motor known as dynein plays a ...
"However, dynein ends up being a major motor protein in that direction because kinesin-14 motors lack the ability of dynein to generate persistent motility on the cytoskeleton track." ...
(2017) Exploiting molecular motors as nanomachines: the mechanisms of de novo and re-engineered cytoskeletal motors. Current Opinion in Biotechnology. 46, 20–26. Driller-Colangelo AR**, Chau KWL**, ...
A motor protein called dynein then transports the endosomes to structures called lysosomes, which use the chemicals to break down the endosomes. Dr.
Get Instant Summarized Text (Gist) HIV can attach directly to the dynein motor protein for intracellular transport, rather than relying solely on the BicD2 adapter protein as previously thought.