Bacterial plasmid carrying the K18 fragment of human Tau containing four
microtubule binding repeats (a gift from M. Margittai (University of Denver, Denver, CO) was overexpressed in Bl21 (D3) Escherichia coli bacteria and purified, as previously described (Meyer et al., 2014).
Not exact matches
Normally tau
binds to
microtubules — molecular conveyor belts that move chromosomes and vesicles within cells.
However, when they then «fixed» a specific hinge region of the dynein molecule that is known to connect dynein to its
microtubule, they discovered that the dynein to spontaneously moved in its characteristic direction when force was applied at the ATP
binding site, matching the way it moves in nature.
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.
«Our study shows how EB proteins can either facilitate
microtubule assembly by
binding to sub-units of the
microtubule, essentially holding them together, or else cause a
microtubule to disassemble by promoting GTP hydrolysis that destabilizes the
microtubule lattice,» says Eva Nogales, a biophysicist with Berkeley Lab's Life Sciences Division who led this research.
Through a combination of high - resolution cryo - electron microscopy (cryo - EM) and a unique methodology for image analysis, a team of researchers with Berkeley Lab and the University of California (UC) Berkeley has produced an atomic view of
microtubules that enabled them to identify the crucial role played by a family of end -
binding (EB) proteins in regulating
microtubule dynamic instability.
They added a tubulin -
binding protein known as Tau, that connects the HyPer protein to the
microtubule structures.
His team found that, from its vantage point at the minus - end of an existing
microtubule, Kinesin - 14 attaches to a second protein that is
bound to the plus end of a growing
microtubule.
When for the protein does not
bind properly to the
microtubules that form the cell's structure, it has a tendency to clump together, she explained, forming insoluble fibers in the neuron.
This competition between strain and
binding to the
microtubule is needed to guarantee processivity of this motor.»
Since its development, lattice light - sheet microscopy has been used to image numerous important events, such as single transcription factor molecules
binding to DNA, hotspots of transcription,
microtubule instability, protein distributions in embryos, and much more.
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.
We demonstrated the technique on 20 different biological processes spanning four orders of magnitude in space and time, including the
binding kinetics of single Sox2 transcription factor molecules, 3D superresolution photoactivated localization microscopy of nuclear lamins, dynamic organelle rearrangements and 3D tracking of
microtubule plus ends during mitosis, neutrophil motility in a collagen mesh, and subcellular protein localization and dynamics during embryogenesis in Caenorhabditis elegans and Drosophila melanogaster.
For example, the protein PRC1
binds with
microtubules, creating bundles of
microtubules and cross-links between them.
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.
In addition to
binding microtubules, centromeres have other functions, including sister chromatid cohesion and preventing
microtubules from both poles attaching to the same chromatid.
The alpha and beta «tails» that protrude from the
microtubule surface are known sites for modification, which in turn, determine which motors and associated protein will
bind to the
microtubule.
Identification of proteins that
bind and control
microtubule nucleation and dynamics during mitosis (Vernos group, Current Biology 2012, 2013, Nature Comm 2014, 2015, Current Biology 2015, J Cell Sci 2016, Mol Biol Cell 2016).
Tubulin - mediated
binding of human immunodeficiency virus - 1 Tat to the cytoskeleton causes proteasomal - dependent degradation of
microtubule - associated protein 2 and neuronal damage.
GAS2 - like proteins mediate communication between
microtubules and actin through interactions with end -
binding proteins.
GCP6
binds to intermediate filaments: a novel function of keratins in the organization of
microtubules in epithelial cells.
Aurora A regulates the activity of HURP by controlling the accessibility of its
microtubule -
binding domain.
The spindle is made of
microtubules (MT), molecular motors, and MT -
binding factors, some of which show astounding complexity.
Tau is a protein that
binds to
microtubules and promotes stabilization of the cell's internal structure.