Cytoskeleton Flashcards
Families of protein filaments
- Actin filaments
- microtubules
- intermediate filaments
shape of the cell’s surface; whole-cell locomotion; pinching of one cell into two
Actin filaments
positions of membrane enclosed organelles; direct intracellular transport; from the mitotic spindle
Microtubules
mechanical strength
intermediate filaments
- underlie the plasma membrane of animal cells
- strength and shape to its thin lipid bilayer
Actin Filaments
Types Cell surface projections formed by actin filaments
- filopodia
- lamellipodia
- pseudopodia
on the surface of hair cells in the inner ear contain stable bundles of actin filaments that tilt as rigid rods in response to sound
Stereocilia
on the surface of intestinal epithelial cells vastly increase the apical cell-surface area to enhance nutrient absorption
Microvilli
Where can microtubles be found?
In cytoplasmic array that extend to cell periphery
- found in cytoplasmic array that extends to the cell periphery
- form a bipolar mitotic spindle during cell division
Microtubules
What does microtubules form?
Cilia
motile whips or sensory devices
Cilia
- line the inner face of the nuclear envelope
- protective cage for the cell’s DNA
Intermediate filaments
twisted into strong cables that can hold epithelial cells sheet together.
intermediate filaments in cytosol
An important and dramatic example of rapid reorganization of the cytoskeleton occurs during
Cell division
bipolar mitotic spindle
Interphase microtubules
crawl across the surface of the dish
Actin
belt around the middle of the cell; pinch the cell into two
Contractile ring
protrusive structure filled with newly polymerized actin filaments
Neutrophils
The cells that have achieved a stable, differentiated morphology
Mature neurons or epithelial cells
cytoskeletal-based cell surface protrusions including microvilli and cilia are able to maintain a ____ ____
constant location
use organized arrays of microtubules, actin filaments, and intermediate filaments to maintain the critical differences between the apical surface and the basolateral surface
Polarized epithelial cells
Subunits for actin filaments; ATP hydrolysis
actin subunits
subunits for microtubules; GTP hydrolysis
Microtubules
are made up of subunits that are themselves elongated and fibrous
intermediate filaments
- determine the spatial distribution and the dynamic behavior of the filaments
- bind to the filaments or their subunits to determine the sites of
assembly of new filaments - bring cytoskeletal structure under the control of extracellular and intracellular signals
- maintain a highly organized but flexible internal structure
accessory proteins
- bind to a polarized cytoskeletal filament
- energy from ATP hydrolysis to move along the filament, and the “cargo” they carry
- carry membrane enclosed organelles
- cause cytoskeletal filaments to exert tension or to slide against each other
motor proteins
tubulin homolog that forms Z-ring
FtsZ
actin homolog
MreB and Mbl
bacterial actin homolog;
encoded by a gene on certain bacterial plasmids that also carry genes responsible for antibiotic resistance
ParM
harbors a protein with significant structural similarity to intermediate filaments
Caulobacter crescentus (italicized)
a protein that forms a filamentous structure that influences the unusual crescent shape of this species
Crescentin
assembly of actin subunits
head-to-tail
types of Different ends
- Minus end
- plus end
a slower growing minus end
Pointed end
faster-growing plus end
Barbed end
the minimum length at which random thermal fluctuations are likely to cause it to bend
Persistence length
control their shape and movement
Regulation of actin filament formation
subunits assemble into an initial aggregate, or nucleus, that is
stabilized by multiple subunit–subunit
contacts and can then elongate rapidly by
addition of more subunits
nuceloation
lag period; G-actin aggregates into short, unstable oligomers; when oligomers reaches a certain length, it can act as a stable seed or nucleus
Nucleation
rapidly increases in length by the addition of actin monomers to both of its ends
Elongation
G-actin monomers exchange with subunits at the filament ends, but there is no net change in the total mass of filaments
Steady-state
called when steady-state phase has been reached, the concentration of the pool of unassembled subunits
Critical concentration, Cc
the ratio of the “on”and “off” rate constant
Dissociation constant
manifested by the different rates at which G-actin adds to the two end
Polarity of F-actin
decorated actin filaments nucleate the polymerization of G-actin
Myosin
caused by a difference in Cc values at the two ends
DIfference of elongation filament
Cc is about six times ____ for polymeration at (+) end than addition at the (-) end
lower
G-actin concentrations intermediate between the Cc values for the (+) and the (-) end
Stead-state phase
regulates the actin behavior, that bind actin monmers or filaments
Accessory proteins
a measure of how long an individual actin monomer spends in a filament as it treadmills
Filament half-life
inhibition of actin polymerization; they cannot associated with either the plus or minus ends; neither hydrolyze nor exchange their bound nucleotide
Thymosin
binds to the face of the actin monomer opposite the ATP-binding cleft, blocking the side of the monomer that would normally associate with the filament minus end
Profilin
prerequisite for cellular actin polymerization
Filament nucleation
actin-related proteins
Arp 2/3 complex
dimeric proteins that nucleate the growth of straight, unbranched filaments that can be cross-linked by other proteins to form parallel bundles
Formins
side-binding proteins; elongated protein that binds simultaneously to six or seven adjacent actin subunits
Tropomyosin
binds at the plus end; stabilizes an actin filament (inactive)
Capping protein (CapZ)
- capping long-lived actin filaments in muscle; minus end-binding
- binds tightly to the minus ends that have been coated and stabilized by tropomyosin
- reduce their elongation and depolymerization
Tropomodulin
- are activated by high levels of cytosolic Ca2+
Gelsolin superfamily
interacts with the side of the actin filament and contains subdomains that bind to two different sites
Gelsolin
- actin depolymerizing factor;
- binds along the length of the actin filament, forcing the filament to twist a little more tightl
Cofilin
cross-link actin filaments into parallel array
Bundling proteins
hold two actin filaments together at a large angle to each other, forming a looser meshwork
Gel-forming proteins
enable stress fiber and other contractile arrays to contract
- an elongated protein formed from two heavy chains and two copies of each light chains
Myosin II
close packing of actin filaments; not contractile
Fimbrin
cross-links oppositely polarized actin filaments into loose bundle; allowing the binding of myosin and formation of contractile actin bundles
α-actinin
formation of a loose and highly viscous gel; by clamping together two actin filaments roughly at right angles
Filamin
observed in migrating fibroblasts. These are filled with dense cores of filamentous actin
Lamellipodia
defect in nerve-cell migration during early embryonic development
filamin A gene mutations
periventricular region of the brain fail to migrate to the cortex and instead form nodules
Periventricular heteropia
web-forming; long, flexible protein made out of four elongated polypeptide chains
Spectrin
first motor protein identified
Skeletal muscle myosin
globular head domain at its N-terminus. contains force-generating machine
Heavy chain
– bind close to the N-terminal head
Light chains