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What are motor proteins?
Proteins that bind to a cytoskeletal filament and use energy from ATP
hydrolysis to move along it.
What direction do myosin motor proteins move along F-actin?
Towards the barbed
(+) end
What are the two classes of myosin?
Conventional myosin (e.g., Myosin II) and unconventional
myosins (at least 17 classes, e.g., Myosin V).
What is the structure of myosin motor proteins?
Composed of one pair of heavy chains and
two pairs of light chains.
What is the function of the head domain of myosin?
It contains the ATP-hydrolysis domain
for power generation and the actin binding region.
What happens to myosin heads in the resting state?
They are bent backwards and
sterically interfere with each other, resulting in inactivity.
How does myosin generate force?
Through coupled ATP hydrolysis and conformational changes
during each cycle of binding, hydrolysis, and release.
What is a sarcomere?
The contractile unit of muscle, consisting of an array of ordered thick and thin
filaments.
Thin filaments (actin) and thick filaments (myosin
II) with overlapping regions.
Actin and myosin slide past each other without
shortening.
It interferes with actin
binding to myosin heads.
An increase in cytosolic Ca2+ concentrations.
It is a Ca2+ binding protein that, when
bound to Ca2+, changes tropomyosin's conformation to allow myosin heads to contact actin.
It is required for cell motility and
cytokinesis during cell division.
They have either one head or two
and are involved in intracellular transport.
It has two heads and a long neck region, allowing it to take long
strides on actin without letting go.
Essential for embryo development,
blood vessel formation, wound healing, and movement of immune cells.
A specialized, thin layer of cytoplasm just under the plasma membrane.
Thin, spike-like protrusions with an actin filament core.
It positions thick filaments midway between
Z-discs and acts like a spring during contraction and relaxation.
The location of proteins linking adjacent Myosin II proteins.
They are
greatly reduced in size.
They stabilize and cap
the actin filaments.
It releases the myosin head from the actin
filament.
It generates force
and restores the myosin head to its original conformation.
It is free of myosin head
domains, allowing for efficient sliding of actin filaments.
Flattened, sheet-like protrusions supported by a meshwork of actin filaments
that drive forward movement of migrating cells.
3D protrusions that are thicker than lamellipodia.
A 3D protrusion where the plasma membrane detaches from actin, and cytoplasm
pushes the membrane forward.
Actin polymerization generates
the protrusion and forward pulling forces.
Myosin II generates retraction forces at the rear
of the cell.
Stimulus received on one end of the cell
activates a family of proteins in the cytosol.
Activated Arp2/3 proteins serve as a nucleating site for new actin filaments.
Older filaments are
disassembled by proteins like Cofilin
Rho-GTP activates Formin proteins
to create actin bundles and inactivate destabilizing proteins.
Dynein moves towards the negative
end of microtubules, facilitating retrograde transport.
Kinesin moves towards the positive end of microtubules, facilitating anterograde transport.
Dynein is composed of two heavy chains and several intermediate
and light chains.
Dynein uses a 'linker-swing,
dynein-winch' mechanism for movement along microtubules.
Head (ATPase and binds MTs), Neck (direction of
movement), Stalk (flexibility/movement), Tail (binds cargo).
The inner core of cilia or flagella that bends to produce movement, consisting
of 9 doublets of microtubules and a central pair.
Dyneins move along adjacent
doublets of microtubules, causing them to bend relative to each other.
A complex network of proteins and polysaccharide
chains that cells secrete.
Cells can be linked by direct interactions,
such as binding of integral membrane proteins, to form tissues and organs.
Adaptor
proteins mediate binding to cargo for both Dynein and Kinesin.
WAVE proteins stimulate
Arp2/3 proteins to nucleate branched actin filaments and drive protrusion of the leading edge.
Cdc42 proteins help
establish polarity in the cell, influencing directionality of movement.
Some pathogens like Listeria monocytogenes use actin tails for propulsion by activating Arp2/3 to polymerize actin.
Connective tissues, like bone or tendon, are
formed from ECM and have very few cells that bear mechanical stress.
A thin mat-like structure that is part of the ECM, acting as a basement
membrane.
Apical surface (exposed to lumen), basal
surface (attached to basal lamina), and lateral surfaces (where junctions occur).
They mediate cell-cell interactions and link the cytoskeleton to extracellular structures.
Integrins, selectins, and
cadherins.
Glycoproteins that join cells together and have a modular construction of extracellular domains with calcium ions.
They act like 'Velcro' to mediate strong
cell-cell interactions.
Classical
cadherins are closely related in sequence, while nonclassical cadherins are more distantly related.
Carbohydrate-binding proteins that bind specific oligosaccharides on cell surfaces.
Two noncovalently attached glycoprotein subunits (alpha and
beta).
They associate with ECM proteins or proteins on other cells and
interact with actin through adaptor proteins.
Protein complexes made up of cadherins that link two epithelial cells.
They respond to tension
inside and outside of cells, facilitating mechanotransduction.
Catenins link cadherins to the
cytoskeleton and inhibit actin-myosin fiber formation.
Structures that provide strength in tissues subjected to mechanical stress by
linking cells with cadherins.
Nonclassical cadherins, specifically
Desmoglein and Desmocollin.
Structures that seal adjacent cells to prevent the movement of molecules
between them.
Transmembrane proteins called Claudins and
Occludins.
To facilitate intercellular communication by forming
channels that allow small molecules to pass between cells.
Channels composed of six four-pass transmembrane connexin proteins that form
gap junctions.
Channels in plant cells that act like gap junctions for cell-to-cell communication.
Tight junctions form the blood-brain barrier, preventing unwanted substances from passing into the brain.
The process by which cells convert mechanical stimuli into biochemical signals.
Keratins are intermediate filaments that provide
structural support and connect to the basal lamina via hemidesmosomes.