Cytoskeleton Flashcards

(43 cards)

1
Q

what 3 kinds of protein structures is the cytoskeleton made up of

A

microfilaments (actin)
intermediate filaments
microtubules

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2
Q

what does highly conserved mean

A

the chemical/molecular structure is very similar among a wide range of different organisms

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3
Q

what are the filaments of actin microfilaments organized into

A

bundles and 3D networks

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4
Q

what doe actin microfilaments bind to and how

A

bind to specific transmembrane proteins either directly or indirectly

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5
Q

how do actin microfilaments exists as

A

monomers (G-actin) and long chains (F-actin)

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6
Q

what are the 3 major varieties of actin filaments

A

alpha-actin (found in muscle tissue)
beta-actin (non muscle actin)
gamma-actin (non muscle actin)

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7
Q

what is the first step of actin polymerization

A

nucleation

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8
Q

what occurs during nucleation during actin polymerization

A

a trimer is formed

addition actin monomers can then be added to either end

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9
Q

what happens following polymerization of microfilaments

A

ATP-actin associates with the growing (plus or barbed) ends, and the ATP is hydrolyzed to ADP following polymerization

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10
Q

which end of microfilaments is the slower growing end

A

minus end (pointed or depolymerization end)

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11
Q

what doe very low concentrations of F actin favor

A

disassembly of actin filaments

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12
Q

what do intermediate concentrations of G actin favor

A

dynamic equilibrium between the minus end and the plus end (tread milling)

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13
Q

what do high concentrations of G actin favor

A

net addition at both ends and therefore growth of the actin filament

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14
Q

what does cytochalasins do

A

drug that affects actin polymerization:

binds to barbed ends, blocks elongation, can inhibit movement

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15
Q

what does phalloidin do

A

drug that affects actin polymerization
binds to actin filaments and prevents dissociation
can be labeled with fluorescent dyes to allow visualization of actin filaments

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16
Q

what are the actin binding proteins & what do they do

A
  • spectrin: (found in RBC) binds cortical cytoskeleton to the plasma membrane
  • dystrophin: binds cortical cytoskeleton to the plasma membrane
  • villin and fimbrin: cross-links in microvilli
  • calmodulin and myosin I: cross-links actin to plasma membrane in microvilli
  • alpha-actinin: cross-links stress fibers and connects actin to protein-plasma membrane complex complexes
  • filamin: cross-links actin at wide angles to form screen-like gels
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17
Q

what are the actin-binding molecules that control treadmilling

A
  • thymosin: captures actin monomers and prevents actin monomers from being polymerized
  • profilin: binds to actin monomers and prevents monomers form being polymerized, facilities exchange of bound ADP for ATP-favors polymerization
  • gelsolin: destabilizes F-actin and caps actin filaments (preventing loss and addition of G-actin)
  • cofilin: triggers depolymerization of ADP-bound actin at the minus end
  • Arp2/3: initiates growth of F actin from sides of existing filaments-causes branching
  • phalloidin: prevents depolymerization by binding to actin filaments
  • latrunculins: binds to G-actin and induces F-actin depolymerization
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18
Q

what does spectrin do?

A

(found in RBC) binds cortical cytoskeleton to the plasma membrane

19
Q

what does dystrophin do

A

binds cortical cytoskeleton to the plasma membrane

20
Q

what does villain and fimbrin do

A

cross-links in microvilli

21
Q

what does calmodulin and myosin I do

A

cross-links actin to plasma membrane in microvilli

22
Q

what does alpha-actinin do

A

cross-links stress fibers and connects actin to protein-plasma membrane complex complexes

23
Q

what does filamin do

A

cross-links actin at wide angles to form screen-like gels

24
Q

what does thymosin do?

A

(tread milling)captures actin monomers and prevents actin monomers from being polymerized

25
what does profiling do
(tread milling) binds to actin monomers and prevents monomers form being polymerized, facilities exchange of bound ADP for ATP-favors polymerization
26
what does gelsolin do
(tread milling)destabilizes F-actin and caps actin filaments (preventing loss and addition of G-actin)
27
what do cofilin do
(tread milling)triggers depolymerization of ADP-bound actin at the minus end
28
what does Arp2/3 do
(tread milling)initiates growth of F actin from sides of existing filaments-causes branching
29
what does phalloidin do
(treadmilling) prevents depolymerization by binding to actin filaments
30
what does latrunculins do
(treadmilling) binds to G-actin and induces F-actin depolymerization
31
what are characteristics of intermediate filaments
* abundant cells subject to mechanical stress * provide tensile strength in cells * strengthen epithelial cells (as desmosomes and hemidesmosomes)
32
how do tetramers assemble in intermediate filaments
end to end to form protofilaments
33
what are some intermediate filament functions
* form a cytoplasmic network in most cells | * associate with other cytoskeletal elements to form a scaffolding that organizes the internal structure of the cell
34
what is a type I intermediate filament
acidic keratins
35
what is an example of a type 2 intermediate filament
neutral to basic keratins
36
what are examples of type 3 intermediate filaments
vimentin, desmin, glial fibrillary acidic protein, peripherin
37
what is an example of type 4 intermediate filament
neurofilaments
38
what is an example of a type 5 intermediate filament
nuclear lamins
39
what is an example of a type 6 intermediate filament
nestin
40
what happens following polymerization in mircotubules
GTP is hydrolyzed to GDP and the tubulin is less stable * dimers at the minus end dissociate
41
what are some factors that inhibit microtubule polymerization
colchicines, colcemid, vincristine, vinblastin
42
what factor stabilizes microtubules
taxol (often used to treat breast cancer)
43
what are the functions of the cytoskeleton
* cell movement * support and strength for the cell * phagocytosis * mitotic spindle formation * cytokinesis * cell-to-cell and cell-to-Extracellular Matrix adherence * changes in cell shape