Sentences with phrase «along microtubule»

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.

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.

«Motors that move along microtubule tracks like cars on a highway do a lot of work in cells.

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.

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.

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.

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.

Motor proteins carry cargoes along microtubules in cells.

Proteins travel from one end of a neuron to the other by moving along microtubules.

Motor proteins powered by adenosine triphosphate, which supplies chemical energy, «walk» along microtubules to deliver cargo throughout cells and discard trash.

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.

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.

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.

Motor proteins carry cargoes along microtubules in cells as seen in this image from an earlier study at Rice.

Not exact matches

This interrupts the transport of cellular materials along axonal microtubules, causing these materials to accumulate at several points along the axon where they may give rise to varicosities.

We found that this distribution required sliding of microtubules toward the cell center along preexisting microtubules.

A group of LMU physicists led by Professor Erwin Frey, in collaboration with Professor Stefan Diez (Technical University of Dresden and Max Planck Institute for Molecular Cell Biology and Genetics, Dresden), has now developed a model in which the motor proteins that are responsible for the transport of cargo along protofilaments also serve to regulate microtubule lengths.

The team found changes in a gene encoding a previously unknown «dynein,» a protein that moves like a railroad locomotive along cytoskeletal fibers called microtubules, hauling other molecules as cargo.

Building from two subunits, alpha and beta tubulin, this protein assembles into microtubules that play a vital role inside cells — giving structure, pushing or pulling other things around, or providing a track on which other molecules can pull themselves along.

This dimer gives microtubules directionality, which is key to many of their other properties, such as being able to assemble or disassemble from either end, and allowing motor proteins to walk along them in a specific direction.

The study, published on October 6 in Cell, describes how two proteins work together to guide the growth of a new microtubule along an existing one.

A team of researchers led by Alipasha Vaziri, an associate professor and head of the Rockefeller's Laboratory of Neurotechnology and Biophysics, has found that a molecular motor, called Kinesin - 14, helps to guide the formation of a new microtubule along an existing one, and so directs the formation of bundles.

Experiments also revealed that as pairs of microtubules were jiggled, these proteins shuffled along them in the direction of least resistance, toward either the plus or minus end of the microtubules.

Microtubules, which can be stable for minutes or even hours, were a good first target, Kolomeisky said, because many experimentalists saw their growth, stability and dissolution as a one - way process and were hard - pressed to explain signs of shrinking along the way.

His group's paper in the Journal of Physics A: Mathematical and Theoretical describes a new theoretical approach to study the effect of intermolecular interactions on the dynamics of motor proteins that move along cytoskeletal filaments known as microtubules.

Dr Stan Burgess, at the University of Leeds» School of Molecular and Cellular Biology, who led the research team, said: «Dynein has two identical motors tied together and it moves along a molecular track called a microtubule.

As mitosis progresses, the microtubules align the chromosomes along the mid-line of the cell, then shorten and pull the chromosome pairs at their centromeres to opposite sides of the cell.