14.1 Structure and Organization of Actin Filaments Flashcards

1
Q

() in the most abundant cytoskeletal protein of most cells (5-10% of total proteins in eukaryotic cells)

A

actin

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2
Q

actin polymerizes to form () → thin, flexible fibers

A

actin filaments (microfilaments)

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3
Q

each actin monomer () has tight binding sites that mediate head-to-tail interactions with 2 other monomers → forms a trimer (nucleation)

A

globular [G] actin

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4
Q

polymerization of G actin leads to formation of ()

A

filamentous (F) actin

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5
Q

why are actin filaments polar (i.e. have plus and minus ends)?

A

all actin monomers are oriented in the same direction

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6
Q

describe “treadmilling” of actin filaments

A

ATP-actin is added to plus end while ADP-actin is dissociated from the minius end of a microfilament

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7
Q

describe the general dynamics of actin filaments

A
  1. the plus end of actin filaments elongates by the addition of ATP-actin monomers
  2. actin bound to ATP associates with plus ends, ATP is then hydrolyzed to ADP
  3. actin-ATP binds more readily to actin filaments compared to actin-ADP
  4. ADP-actin found at the - end is less tightly bound, and thus actin monomers are more readily disassociated from this end
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8
Q

actin-binding proteins regulate the ff:

A
  • assembly and disassembly of actin filaments
  • cross-linking of actin filaments into bundles and networks
  • association of actin filaments to cell structures (e.g. plasma membrane)
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9
Q

what are the principal proteins that stimulate the initiation and elongation of actin filaments?

A
  1. formin
  2. Arp2/3 complex (actin-related protein)
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10
Q

proteins involved in the nucleation, initiation, and growth of actin filaments → they move along growing filament and add new ATP-acting monomers at plus end

A

formins

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11
Q

binds actin monomers and stimulates exhange of bound ADP for ATP, increasing local concentration of ATP-actin → promotes actin polymerization

A

profilin

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12
Q

initiates growth of branched actin filaments → important in driving cell movement at the plasma membrane

A

Arp2/3 complex

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13
Q

actin-binding proteins that stabilize actin filaments by binding lengthwise along filament groove

A

tropomyosins

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14
Q

actin-binding proteins that stabilize actin by binding to the plus or minus ends

A

capping proteins

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15
Q

actin-binding proteins that associate microfilaments into bundles or networks

A

cross-linking proteins

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16
Q

() are filaments cross-linked into parallel arrays

A

actin bundles

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17
Q

() are filaments cross-linked in arrays that form 3D meshworks (have properties of semisolid gels)

A

actin networks

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18
Q

actin-binding protein that severs filaments → generates new ends which are then available for polymerization or depolymerization

A

cofilin

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19
Q

a drug that affects actin polymerization by binding to plus ends and block elongation → inhibits cell movement and even cell division

A

cytochalasins

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20
Q

a drug that affects actin polymerization by binding to actin filaments and prevents dissociation

A

phalloidin

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21
Q

network of microfilaments and associated proteins under the plasma membrane

A

cell cortex

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22
Q

member of calponin family and is the major protein that provides the structural basis for the cortical cytoskeleton; a tetramer of two polypeptides, ⍺ and β

A

spectrin

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23
Q

spectrin ends associate with short actin filaments → forms the ()

A

spectrin-actin network

24
Q

links the spectrin-actin network and the plasma membrane by binding to spectrin and band 3 (transmembrane protein)

A

ankyrin

25
Q

ankyrin binds to spectrin and ()

A

band 3 transmembrane protein

26
Q

() is another link that binds spectrin-actin junctions and glycophorin (transmembrane protein)

A

protein 4.1

27
Q

protein 4.1 binds spectrin-actin junctions and ()

A

glycophorin

28
Q

links actin filaments to transmembrane proteins that link to the extracellular matrix → maintains cell stability during muscle contraction

A

dystrophin

29
Q

what is the cause of Duchenne’s muscular dystrophy?

A

absence (complete KO) of dystrophin

30
Q

what is the cause of Becker’s muscular dystrophy?

A

abnormal expression of dystrophin

31
Q

specialized plasma membrane regions of fibroblasts that form contacts with the adjacent cells’ extracellular matrix

A

focal adhesions

32
Q

in focal adhesions, fibroblast cells attach to extracellular matrix by binding to transmembrane proteins called ()

A

integrins

33
Q

for fibroblasts, focal adhesions are also the attachment sites for large actin bundles called ()

A

stress fibers

34
Q

stress fibers are contractile fibers, cross-linked by (1) and stabilized by (2)

A
  1. alpha-actinin
  2. tropomyosin
35
Q

what proteins are involved in stress fiber binding in focal adhesions

A
  1. talin - interacts with vinculin and integrin
  2. vinculin - interacts with talin and actin filament
36
Q

cell-cell contacts in epithelial cell sheets

A

aderens junctions

37
Q

the continuous belt of cell-cell contacts around each epithelial cell in epithelial cell sheets

A

adhesion belt

38
Q

what are the proteins that are involved cell-cell contact in adherens junctions

A
  1. cadherins - transmembrane proteins that mediate cell-cell contact by binding to cytoplasmic catenins
  2. catenins - interact with actin filament and cadherins, anchoring the actin filaments to the plasma membrane
39
Q

extensions of the cell surface are usually based on (), either in permanent or transient conformations; the latter usually form in response to environmental signals

A

actin filaments

40
Q

cell surface extensions of moderate width; responsible for phagocytosis and movement of amoebas

A

pseudopodia

41
Q

broad, sheet-like extensions at the leading edge of fibroblasts

A

lamellipodia

42
Q

projections of the plasma membrane supported by actin bundles

A

filopodia

43
Q

fingerlike extensions on plasma membranes that are abundant on cell surfaces involved in absorption (e.g. epithelial cells); serve to increase surface area of the cell

A

microvilli

44
Q

in the epithelial cells lining the intestine, microvilli form a () (about 1000 microvilli per cell) on apical surface of cell

A

brush border

45
Q

intestinal microvilli contain parallel bundles of 20-30 microfilaments cross-linked by (1) and (2)

A
  1. fimbrin
  2. villin
46
Q

actin bundles of intestinal microvilli are attached to the plasma membrane by the calcium-binding protein (1), in association with (2)

A
  1. calmodulin
  2. myosin I
47
Q

how are extensions of the plasma membrane driven by branching and polymerization of underlying actin filaments

A
  • growing actin filaments push against plasma membranes and drive formation of protrusions
  • inhibition of actin polymerization blocks the formation of cell surface protrusions
48
Q

cell movement across a surface proceeds in 3 stages

A
  1. extension of leading edge
  2. attachment of leading edge to substratum
  3. retraction of trailing edge
49
Q

like other cell surface protrusions, extension of the leading edge during cell motility involves

A

branching and polymerization of actin filaments

50
Q

formation of cell surface protrusions in response to external stimuli is mediated by small (), which are activated by signals stimulating cell movement

A

GTP-binding Rho proteins

51
Q

Rho proteins promote actin polymerization by:

A
  • stimulating Arp2/3 complex (initiates growth of branched actin filaments)
  • activating formins (initiates growth of linear filaments)
  • activating WASP
52
Q

what is the role of cofilin in cell motility

A
  • by cleaving existing filaments, it creates new plus ends to support filament branching and growth
53
Q

as new actin filaments extend into the growing cell, they also provide pathways for vesicles containing ()

A

lipids and proteins needed for continued extensions

54
Q

for slow-moving cells, cell attachment to surface requires ()

A

rebuilding cell-substratum adhesions (e.g. focal adhesions)

55
Q

retraction of the trailing edge into the cell body involves the action of (1) and (2)

A
  1. small GTP-binding Arf proteins
  2. Rho proteins
56
Q

what is the role of Arf GTPases in the retraction of the trailing edge

A

control membrane endocytosis and regulate Rho proteins to modulate actin polymerization and dynamic reorganization

57
Q

what is the role of Rho GTPases in the retraction of the trailing edge

A

causing the formation of stress fibers and actomyosin contractility providing tension for the cell to retract its tail and move forward