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In eukaryotic cells, some motor proteins associate with microtubules to ferry cargo to specific intracellular locations.
Microtubule-associated motor proteins are broadly classified into two superfamilies — kinesins and dyneins.
Structurally, kinesins have globular heads that extend to a rod-like stalk and connect to fan-shaped receptors.
The globular head binds to microtubules, while the fan-shaped receptor binds to the organelles and vesicles.
During interphase, kinesins move the cargos towards the cell periphery using hand-over-hand movement, where the ATP-hydrolyzing globular heads work in tandem to move across the microtubules.
The dynein superfamily consists of ATP-driven proteins that carry out all microtubule minus-end-based transport.
Cytoplasmic dyneins are made up of heavy, intermediate, light, and light-intermediate chains. The heavy chain has a globular head and a stalk responsible for energy generation and binding with the microtubules, respectively.
Cytoplasmic dynein associates with other large proteins, like dynactin, to attach to the adaptor-bound cargo. These complexes then move organelles and vesicles towards other organelles near the center of the cell.
Eukaryotic cells have different motor proteins for transporting various cargo within the cell. These motor proteins differ based on the filament they…
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