Cytoskeleton Flashcards

1
Q

Width of actin filament

A

7 nM

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2
Q

Polarization of actin

A

Grow fastest at + end, depolymerize at - end

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3
Q

Polymerization of actin

A

G actin binds to ATP
Polymerizes into F-actin (mostly at + end)
ATP later hydrolyzes to ADP
Polymerization also requires K+ and Mg+

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4
Q

Structure of actin

A

G = granular, polymerizes into F (fibrillar) in presence of ATP

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5
Q

Functions of actin

A

Anchor membranes, structure (terminal web)
Contractile (shape, movement, cell separation)
Transport around cell (actin binding proteins)
Form microvilli, lamellae, filopodia

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6
Q

Actin and ATP cycling

A

Requires ATP presence to polymerize (reflects concentrations of ATP in cell)
Hydrolysis while polymerized
ADP tends to depolymerize

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7
Q

Actin binding proteins (6)

A
Myosin - motor
Tropomyosin - stabilizes
Gelsolin - breaks filaments in middle
Actin bundling proteins - fimbrin, villin, alpha actinin
Branching proteins - formin
Integrin - intermembrane, anchors to ECM
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8
Q

Actin and cell movement

A

Polymerization can move cell membrane

Myosin can be bound to organelle, vesicle or to membrane

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9
Q

Actin disrupters

A

Cytochalasins B+D - prevent polymerization (chemo)

Phalloidin - prevents depolymerization (mushroom toxin)

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10
Q

Microtubule size

A

25 nM (biggest cytoskeleton element)

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11
Q

Microtubule structure

A

Tubulin dimers (alpha and beta) in
13 chains around
hollow core
Originate from MTOC

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12
Q

Microtubule polarization

A
  • end at MTOC

+ end at periphery - growth and depolymerization at + end (MTOC caps - end)

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13
Q

Microtubules and GTP cycling

A

GTP binding promotes assembly

Depolymerizes closer to bottom

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14
Q

MTOC

A

AKA centrosome
Nine sets of triplets of MTs
Rings of gamma tubulin and capping proteins that stabilize - end of all microtubules

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15
Q

Functions of microtubules

A

Organize and transport organelles (vesicles, Golgi, ER)
Mitosis (create spindle)
Can contribute to cell movement and shape
Cilia

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16
Q

Microtubule movement

A

Kinesins to + end
Dynein to - end
Both are ATPases (bind for conformational change, hydrolisis for release and resetting)
Responsible for relative movement (ie cilia)

17
Q

Cilia structure

A

9 doublets + 2 central MTs
Dynein attach to next doublet, bend and release for movement
Basal body is 9 triplets (like MTOC)

18
Q

Microtubule disruptors

A

Vinblastine - chemo, prevents polymerization
Taxol - chemo, stabilizes (prevents mitosis)
Colchicine - gout, prevents polymerization (decreases inflammatory cell movement)

19
Q

Size of intermediate filaments

A

8-10 nm

20
Q

Intermediate filament structure

A

2 coiled dimers form tetramer

8 staggered tetramers form filament

21
Q

Characteristics of intermediate filaments

A

Non-polar (each tetramer is symmetrical)
Don’t regularly (de)polymerize
Very stable and strong

22
Q

Types of intermediate filaments (6)

A
Keratin - epithelia
Vimentin - connective tissue, mesenchyme
Desmin - skeletal muscle
Glial fibrillary acidic protein - glial cells
Neurofilaments
Lamins - all nuclei
  • Type of intermediate filament can identify cancer cell origins
  • Helical/rod domain is conserved, ends have identifiable differences
23
Q

Functions of intermediate filaments

A

Key for structure, mechanical stress (ie desmosomes)
Support other cytoskeleton elements
Lamin supports nuclear envelope