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Molecular cell > cytoskeleton > Flashcards

cytoskeleton Flashcards

1
Q

definition of cytoskeleton

A

cytoskeleton consist of filamentous bio-polymers (microtubules, F-actin and intermediate filaments) and oaf associated proteins that modulate the activity, dynamics and organisation of the cytoskeleton (actin binding or microtubule binding proteins, such as molecular motors)

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2
Q

filamentous bio-polymers in the cytoskeleton

A

microtubules, F-actin, intermediate filaments)

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3
Q

proteins associated with the cytoskeleton

A

actin binding or microtubule binding proteins, such as molecular motors

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4
Q

eukaryotic cytoskeleton provides

A

tracks that link the regions of the cell

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5
Q

skeleton

A

–> connects all parts of the cell–> supports motility–> helps spatial organisation

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6
Q

F actin location

A

found closest to the membrane

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7
Q

microtubules location

A

spans from the centrosome to the outside of the cell

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8
Q

intermediate filaments

A

found all around the cell

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9
Q

three classes of filaments that make up the cytoskeleton

A

f actin, microtubules, intermediate filaments

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10
Q

f actin also known as

A

microfilaments

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11
Q

F actin

A

7-9nm –> short range transport and cell migration

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12
Q

Microtubule

A

25nm –> long range transport and chromosome inheritance (mites, meioses)

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13
Q

<p>intermediate filaments</p>

A

mechanical strength

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14
Q

cytoskeleton as well as proving tracks for intracellular trafficking, also provides..

A

stability for the cell e.g. extreme example: membrane cytoskeleton of red blood cells make them stiff and strong

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15
Q

structure of F actin

A
  • made up of G actin monomers-f actin is made up of 2 photo filaments-actin exists as monomers and polymers-F actin will release G actin- cell switches between g and f actin
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16
Q

most actin in the cell is

A

G actin

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17
Q

how many different actin binding proteins ar known

A

160

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18
Q

what do actin binding proteins d

A

they modify actin organisation

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19
Q

actin forms

A

cellular protrusion e.g. sterocilia on hair cells in the inner eare.g. microvilli on an intestine epithelium

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20
Q

examples of different formations of actin

A

stabilising, capping, depolymerising, cross-linking, severing, moving, bundling

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21
Q

ordered bundling

A

microvilli, sterocilia

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22
Q

dynamic crosslinking

A

stress-fibres and muscle

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23
Q

cross linking

A

network formation

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24
Q

myosin is used in

A

actin in a ‘moving’ formation

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25
Q

firkin, alpha-actinic is used in

A

bundling and stabilising

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26
Q

filamin, spectrum are used in

A

sequestering/recycling and branching

27
Q

G actin is polymerised by

A

‘treadmilling’

28
Q

what is treadmilling

A

adding subunits at one end, losing them at the other

29
Q

without actin binding proteins

A

the cell would die e..g all the G actin would polymerise

30
Q

the bundles actin forms make it

A

a strong molecule

31
Q

single actin chains are

A

flimsy and week

32
Q

cilia are just

A

huge bundles of actin

33
Q

microtubules are made up of

A

beta and alpha tubular (tubulin dimer) and these polymerise into protofilliment (straight line) which joins to form a microtubule

34
Q

13 protofilaments

A

form a microtubule

35
Q

at one end of the microtubule there will be

A

Beta tubulin

36
Q

at the other end of the microtubule will be

A

an alpha tubule

37
Q

microtubule size

A

25nanometer diameter

38
Q

without GFP what cannot be visualised

A

microtubules –> gives out light and make it look larger than it really is

39
Q

tubular exists as..

A

dimers and polymers

40
Q

tubular is fairly dynamic and this is due to

A

polymerisation behaviour

41
Q

tubular is added and released at

A

one end of the polymer

42
Q

polymerisation of tubulin- polymerisation

A

1)polymerisation- GTP-bound tubular dimers get added to ‘plus end’. A cap of GTP tubular stabilises the growing microtubule

43
Q

polymerisation of tubulin- pausing

A

water is added to GTP tubular to form GDP tubular and phosphate. when polymerisation slows down (e..g not enough tubular available), the GTP cap disappears

44
Q

polymerisation of tubulin- depolymerisation

A

-microtubule becomes unstable and depolymerises and this moment of transition is called a CATASTROPHE

45
Q

polymerisation of tubulin- second polymerisation

A

GTP tubular can bind to the shrinking microtubule and establish a new cap.
The meant of transition is called a RESCUE EVENT

46
Q

microtubules constantly switch from

A

growing and shrinking

47
Q

growing and shrinking

A

dynamic instability

48
Q

recue event

A

moment of transition when GTP tublin begins to bind again

49
Q

GTP cap needs to be present for the

A

microtubule to grow

50
Q

what reveals the difference in dynamic behaviour of microtubules and F-actin

A

speckle microscopy

51
Q

which part of the microtubule is dynamic

A

the ends of the microtubule–> while incorporated tubular remains relatively stationary–> only change in colour at the ends of the microtubule

52
Q

which parts of F-actin are dynamic

A

actin treadmills through the actin filament meshwork–> can see flow of action–> due to tread milling of fluorescent subunit throughout the actin filament

53
Q

intermediate filaments

A

relatively unorganised and made of many different types of proteins. provide strength to organisms, since animal cells do not have a cell wall and the plasma membrane is liquid

54
Q

which types of proteins are present in intermediate filaments

A

keratin, lamina, pimentos (ends are globular)

55
Q

formation of intermediate filament

A

a coiled coil consisting of alpha-helices. made up of 2-3 helices, which wind around each other

56
Q

alpha helices in intermediate filaments are often..

A

amphipathic

57
Q

amphiphatic

A

charged at one site –> serves protein interaction

58
Q

often intermediate filaments have a structural similarity but are

A

made up of different proteins e.g. keratin or vimentin

59
Q

formation of intermediate filaments does not require

A

ATP or GTP –> self assemble into apolar filaments (not polar or dynamic)

60
Q

nuclear lamina are made out of

A

intermediate filaments

61
Q

lamins provide stability and organise the

A

nucleus

62
Q

phosphorylation leads to

A

fragmentation of lamins

63
Q

what allows cell movement

A

the intermediate filaments can be reorganised by disassembling into subunits

64
Q

which skin associated structure are formed by intermediate filaments

A

nails, hair , eye (lens)

Molecular cell (21 decks)

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