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what are the three types of filaments?
IF
actin
MT
describe IF
strong to combat mechanical stress
describe the sturcture of IF’s
each monomerhas a pair of globular terminal domains seperated by long fibrous alpha helical region that is polar
pairs of monomers are parallel
monomers form dimers
dimers form non polar tetramers
tetramers form 8unit lengths IF filament
what are the types and functions of IF?
cytoplasmic; keratin, neurofilaments, vimentin filaments.
nuclear; nuclear filaments
explain what keratin filaments serve to do?
act as the structural protein of epithelial cells
radiate through cytoplasm thethered to nuclear envelope anchored to outer edge of cell. and also connect to MT and F actin via plecton
e
explain neurofilaments
bundles of IF located in cytoplasm of mature neurons, parallel to axon for sztrength and stability.
describe the assembly and disassembly of IF
doesnt directly require ATP/GTP
assembly is controlled by subunit phosphorylation and dephosphorylation.
once assembeled subunits are not incorporated end to end just along.
what is the function of linker proteins?
cross links other IF and desmosomes for reinforcment and stabilization. each plectin dimer has two binding sites for its respective filament binding.
what are actin filaments for?
maintain cell shape movement and cell division
what is the sturcture of actin filaments?
thin flexible helicla filament made of actin monomers free form in the ctyoplasm
F-actin; polar filament for higher order structure.
describe the assembly and disassembly of actin filaments
grow by the addition of actin at both ends but fvaster at positive end. ATP is hydrolyzed to ADP is encorporated into growing end that is dedpolymerizing ( if conc of atp-actin monomers is very high subunits are added to both ends).
at the point where addition=loss the actin filament doesnt grow.
treadmilling is the addition of monomers at olne end with equal loss at the other, generating movement.
what are the actin binding proteins?
nucleating; to form seeds
monomer-sequestering; binding individual actin to prevent spontaneous assembly
bundleling;pushes cell forward
cargo movement
end blocking; stops hrowth
cross linking; gives stren gth
filament severing; stop smovement
actin filament depolymerization
describe cell motility
cell sends out protrusions at its front edge by actin polymerization.
protrusions adhere to surface over which the cell is crawling by formation of focal adhesions.
the rest of the cell drags behind deploymerization olf focal adhesion
what are myosins described as?
motors of f actin
what are the two types of mysosin?
unconventional-myosin 1
conventional myosin 2
how do the two types of myosin work?
1- hand a repetitive cylce of binding, release, reattachment
2- muscle contraction, sliding filamentmodel.
what are the three layers of mucle fibers?
muscle fibers→myofibrils→sarcomeres
describe the sliding filament model steps
attachment
release
cocked
rebinding/power stroke
what are MT’s functions?
cell shape, cell division, cell motility, provide tracks
describe the structure of MT
tubular structures alpha tubulin(-) and beta tubulin(+) form a polar heterodimer.
explain the assembly of MT
each tubulin dimer contains GTP tightly bound to beta tubulin.
added to + end of MT
GTP is hydrolyzed= GDP
GDP remains bound to beta tubulin
if tubulin dimers are added faster than it is hydrolyzed the MT grows
how is MT disassembled?
if the GDP bounds less tightly it tips in favour of disaszsembly.
what are the MAPs?
nucleation
branching
link other MTs
polymerization
stability
severing
motor proteins
intracellular motility
requies ATP through motor proteins
list the three motor proteins included in intracellular motility
myosins; actin filaments move to + end
kinesins; MT move to + end
dyneins; MT move to negative end
all move unidirecionally
how do kinesis move?
hand over hand model
how do dyneins move?
pull the golgi inwardly along the MT and towards centrosomes
what is the mechanism of ciliary/flagellar locomotion
?
the dynein anchored along the tubule attached to an adjacent binding site and flexible linker proteins cause bending when the tubules power stroke.