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 during cell division
microtubules
mechanical strength; protective cage for the cell’s DNA; form tough appendages (hair and fingernails)
intermediate filaments
cell-surface projections class of actin filaments
lamellipodia and filopodia
motile whips or sensory devices of cells
cilia
belt around the middle of the cell; pinches the cell into two identical sister cells
contractile ring
protrusive structure filled with newly polymerized actin filaments
neutrophils
specialized epithelial cells in the intestines and lungs
microvilli and cilia
present in the apical surface and the basolateral surface; maintain strong adhesive contacts with one another to enable this single layer of cells to serve as an effective physical barrier
polarized epithelial cells
actin filaments are made of ________ using ATP hydrolysis
actin subunits
microtubules are made from clusters of _________ through __________ hydrolysis
tubulin subunits, GTP
polarized structural proteins; asymmetrical form; polarized
actin filaments and microtubules subunits
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
accessory proteins
bind to a polarized cytoskeletal filament; energy from ATP hydrolysis to move along the filament, and the “cargo” they carry
motor proteins
tubulin homolog; generate a bending force that drives the membrane invagination and site for localization of enzymes
FtsZ
actin homolog; scaffold to direct the synthesis of the peptidoglycan cell wall
MreB and Mbl
abnormalities in cell shape and defects in chromosomes segregation
mutations
bacterial actin homolog; encoded by a gene on certain bacterial plasmids that also carry genes responsible for antibiotic resistance
ParM
homolog of intermediate filaments
Caulobacter crescentus – crescentin
structural proteins present in muscle cells
α-Actin
almost non-muscle cells
β- and γ-actins
faster-growing; barbed end
plus end
pointed end; slower-growing
minus end
the minimum length at which random thermal fluctuations are likely to cause it to bend
persistence length
assembly of actin subunits
head-to-tail → tight, subunits right-handed helix
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
nucleation
G-actin proceeds in three sequential phases:
nucleation, elongation, steady-state
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
when steady-state phase has been reached, the concentration of the pool of unassembled subunits is called
critical concentration, Cc
the ratio of the “on” and “off” rate constant; measures the concentration of G-actin where the addition of subunits is balanced by the dissociation of subunits
dissociation constant
manifested by the different rates at which G-actin adds to the two ends
polarity of F-actin
difference in elongation rates at the opposite ends of an actin filament is caused by a ______________________at the two ends
difference in Cc values
actin can only elongate in the _________
minus end
actin can only elongate in the __________ when the minus end is blocked
plus end
G-actin concentration below Cc+, there is:
no filament growth
G-actin concentrations between Cc+ and Cc-
growth is only at the (+) end
G-actin concentration above
no growth at both ends
G-actin concentrations intermediate between the Cc values for the (+) and the (-) ends, subunits continue to be added at the (+) end and lost from the (-) end
steady-state phase
newly added subunits traveling through the filament, as if on a
treadmill
actin behavior is regulated by _____________ that bind actin monomers 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, while leaving exposed the site on the monomer that binds to the plus end
profilin
prerequisite for cellular actin polymerization
filament nucleation
actin-related proteins; nucleates actin filament growth from the minus end, allowing rapid elongation at the plus end
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
Formin-dependent actin filament growth is strongly enhanced by the association of actin monomers with
profilin
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
tropomodulin
coats the filament completely and present in high amounts
side-binding
affect filament dynamics
end-binding
proteins that break an actin filament into many smaller filaments; generating new filament ends
severing proteins
activated by high levels of cytosolic Ca2+; interacts with the side of the actin filament and contains subdomains that bind to two different sites
gelsolin superfamily
actin depolymerizing factor; binds along the length of the actin filament, forcing the filament to twist a little more tightly
cofilin
actin filament types of arrays
dendritic networks, bundles networks, weblike (gel-like) networks
made of the long, straight filaments produced by formins
bundles networks
Arp 2/3 complex
dendritic networks
diff. actin networks depends on:
specialized accessory proteins
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
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; form actin filament webs or gels
filamin
cytoskeletal protein actin projection on the leading edge of the cell; determines cell movement direction by protrusive force that arises from the actin network
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 heterotopia
web-forming; long, flexible protein made out of four elongated polypeptide chains; allows RBC to “spring back” to shape
spectrin
first motor protein identified; generates force for muscle contraction
myosin
an elongated protein formed from two heavy chains and two copies of each light chains
myosin II
globular head domain at its N-terminus; contains force-generating machine
heavy chain
bind close to the N-terminal head of myosin
light chains
MYOSIN: SLIDING FILAMENT THEORY
- myosin head binds and hydrolyzes ATP
- it then uses the energy from ATP hydrolysis to walk toward the plus end of an actin filament
[opposing orientation of the heads makes the filament efficient at sliding] - ATP-driven sliding of actin filaments results in a powerful contraction
each step of the movement along actin is generated by the swinging of an:
8.5nm long α-helix – lever arm
a piston-like helix that connects movements at the ATP-binding cleft in the head to small rotations
converter domain
changes in the conformation of the myosin are coupled to changes in its:
binding affinity for actin
a cylindrical structure 1-2 μm in diameter that is often as long as the muscle cell itself
myofibril
myofibrils is made up of a long, repeated chain of tiny contractile units called _________, which gives the vertebrate myofibril its striated appearance
sarcomeres
parallel and partly overlapping thin and thick filaments
sarcomeres
myosin filaments sliding past the actin thin filaments, with no change in the
length of either type of filament causes:
sarcomere shortening