Motor proteins carry cargoes
along microtubules in cells as seen in this image from an earlier study at Rice.
Motor proteins carry cargoes
along microtubules in cells.
Not exact matches
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.
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.
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.
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.
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.
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.
«Motors that move
along microtubule tracks like cars on a highway do a lot of work
in cells.
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 microtubul
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 microtubul
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 microtubul
in which they are being moved
along a
microtubule.
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
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
microtubules, or move the
microtubulesmicrotubules themselves.
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.