Motor proteins carry cargoes
along microtubules in cells as seen in this image from an earlier study at Rice.
Rice University researchers are modeling the movement of motor
proteins along a microtubule by breaking the pathway down into its basic elements.
The axoneme's movement is accomplished via rows of motor proteins called dyneins that are
attached along the microtubules and exert force on them so the microtubules «slide» past each other, which then causes the entire axoneme and sperm tail to bend and move.
If they are dragged one
way along the microtubule it is hard to do it, while if they're dragged the other way it is easy to do it,» he says.
Miniscule carriers, the motor proteins,
slide along the microtubules with great volumes such as chromosomes, vesicles and other subcellular components — like mitochondria — latched onto them.
In fact, the researchers were surprised to find that weak repulsions led to maximum
movement along the microtubules and that motor proteins are more sensitive to attraction rather than repulsion.
Each kinesin contains two «head» subunits, and each subunit contains two binding sites — one to grip and
walk along microtubules and the other to bind ATP.
The «parts list» in these processes is similar: Microtubules, semi-rigid tubes of protein, can serve within the cell as scaffolding, roadways, and a building material for machinery; some proteins serve as fasteners, binding and releasing other materials; and motor proteins use chemical energy to push and pull
materials along microtubules, or move the microtubules themselves.
This suggests that HIV proteins probably
migrate along microtubules towards the virological synapse, which could explain why HIV particles preferentially bud there.
When the researchers administered drugs to inhibit the movement of certain «motor» proteins that transport mitochondria and other cargo within the cell by
traveling along microtubules, the mitochondria accumulated in the axon of the neuron and never made it to the synaptic terminal.
The researchers found that AS - 2 binds strongly to the kinesin motor, preventing it from sticking to a cell's monorails — that is, traveling
along microtubules.
A protein complex moves
along the microtubules — tiny tubes in the cell — leaving behind fibers that are patterned into the cell wall.
Motor proteins powered by adenosine triphosphate, which supplies chemical energy, «walk»
along microtubules to deliver cargo throughout cells and discard trash.
In research detailed last week in Cell, the Rockefeller team discovered some of these fastener proteins, known as non-motor microtubule associated proteins, or MAPs, experience different degrees of friction depending on the direction in which they are being moved
along a microtubule.
Generally, they have two motor units at one end that can «walk»
along a microtubule, dragging cargo attached to the other end of the protein.
As a graduate student at the European Molecular Biology Lab in Heidelberg he used cryo - EM to study kinesin motors, capturing snapshots that show how kinesin «walks»
along a microtubule.