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Microtubules form a network of filaments in eukaryotic cells that act as railway tracks to transport organelles and vesicles by the microtubule-associated motor proteins— kinesin and dynein.
Kinesins carry mitochondria and secretory vesicles towards the cell periphery, while dyneins position the Golgi apparatus near the cell center.
In the hand-over-hand model, the two globular heads of the kinesin move alternately forward, resembling a walking movement.
ATP is bound to the kinesin, and its hydrolysis powers the forward motion of the rear globular head.
Upon binding to the microtubule, the kinesin releases the ADP, and an ATP quickly occupies the recently vacated nucleotide-binding site to power the next movement.
In contrast, the inchworm model hypothesizes that the front and rear globular heads of kinesin do not switch places during the movement. During each cycle of progressive forward movement, hydrolysis of a single ATP takes place only at one of the globular heads.
During transport, cytoplasmic dyneins associate with another large protein called dynactin, which has a short actin-like filament, Arp1. Arp1 acts as a receptor for attaching the motor protein complex to the vesicles. This attachment results in the hydrolysis of ATP, causing the complex to move.
In eukaryotic cells, cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filam…
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