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Cell Bio Final Exam > Cytoskeleton Pt 2 > Flashcards

Cytoskeleton Pt 2 Flashcards

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Biology 101 flashcards
1
Q

Functions of Actin

A

Provide strength and shape to plasma membrane

Cell surface projections (filopodia) used to explore territory and move around

Muscle contraction (association with myosin(motor protein))

Microvilli (intestinal epithelial cells): enhance nutrient absorption

Whole cell locomotion (movement)

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2
Q

Cell cortex is

A

the area under the plasma membrane that interacts with actin

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3
Q

Cytoskeletal changes in cell division

A

Crawling fibroblast-dynamic actin cytoskeleton

Leading edge: site of actin assembly at filopodia

Cell division-rearrangement of MT

Actin-contractile ring (also myosin filaments)

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4
Q

The Actin subunit is

A

asymmetric (Globular Actin or G-actin)

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5
Q

G-actin is

A

bound to ATP or ADP

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6
Q

F-actin is

A

Actin subunits assemble head to tail to form a tight right handed helix (8nm wide)

called Filamentous or F-actin

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7
Q

___ end favors elongation

A

plus

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8
Q

flexibility of actin subunit

A

more flexible than microtubule

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9
Q

Arrowhead appearance of the plus end is due to

A

interaction between actin and motor protein myosin.

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10
Q

The rate limiting step of actin formation is

A

Nucleation

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11
Q

The regulation of actin filament formation is how cells control

A

their shape and movement

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12
Q

Nucleation of actin

A

Small oligomers (3 monomers - trimer - stable enough to promote growth) of actin subunits can assemble spontaneously (but unstable)

Actin subunits can spontaneously bind one another, but the association is unstable until subunits assemble into an initial, oligomer, or nucleus, that is stabilized by multiple subunit–subunit contacts and can then elongate rapidly by addition of more subunits.

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13
Q

Critical Concentration

A

Cc=As the polymer grows, subunits are used up. Concentration (C) of subunits is observed to drop until it reaches a constant value (Cc).

At this concentration, rate of subunit addition =rate of subunit loss

for C > Cc, both ends grow; for C < Cc, both ends shrink.

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14
Q

The lag phase (nucleation) of actin formation can be eliminated with

A

preformed filament (crosslinked actin)

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15
Q

Actin can catalyze

A

ATP hydrolysis (Occurs slowly in free subunits, faster in filaments)

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16
Q

T and D forms of actin

A

T form (bound ATP)
D form (bound ADP)

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17
Q

Nucleotide hydrolyzed (energy stored in polymer), with free energy change for dissociation of _____ form polymer more negative than ____ form

A

D
T
(D form polymers will therefore shrink, T form polymers grow)

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18
Q

The critical concentration (Cc) marks the level at which G-actin monomers are

A

in equilibrium with the actin filaments.

Actin filaments are only formed at monomer concentrations above theCc

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19
Q

Actin filaments are only formed at monomer concentrations

A

above theCc

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20
Q

Actin filament at Equilibrium

A

Rate of subunit addition=Rate of subunit loss

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21
Q

Treadmilling occurs when

A

the rate of addition is faster than hydrolysis at plus end, but slower than hydrolysis at minus end.

Plus end will be in T form, Minus end in D form.

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22
Q

During treadmilling the plus end is in ___ form and the minus end is in ____ form

A

Plus end will be in T form,
Minus end in D form.

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23
Q

Plus and minus ends in actin are determined by

A

growing rate

the fast-growing end is called the plus end, whereas the slow-growing end is called the minus end

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24
Q

During treadmilling the Polymer maintains a

A

constant length, even though there is a net flux of subunits through the polymer

25
Q

Cc at plus and minus end

A

CcD> CcT

CcD is higher because D promotes shrinkage - subunits are removed (not added)

26
Q

During treadmilling, the __ end grows and the ___ end shrinks

This requires___

A

Plus end grows while minus end shrinks (at same rate)

Requires a constant consumption of energy in the form of ATP hydrolysis

27
Q

Actin Inhibitors

A

Cytochalasins
Latrunculin
Phalloidins

28
Q

Cytochalasins

A

Fungal products that prevent actin polymerization (bind to plus end). (promotes depolarization)

Application: Can change cellular morphology, induce apoptosis, inhibit cell division. potential use to treat cancer

29
Q

Latrunculin

A

Prevent actin polymerization (bind to actin subunits), from sponges

30
Q

Phalloidins

A

toxins isolated from Amanita mushroom,

bind tightly to side of filament, stabilize against depolymerization, imaging application (can no longer depolymerize)

31
Q

Sequestering monomers

A

Profilin and Thymosin

32
Q

Nucleation and Elongation

A

Arp 2/3 complex, Formin

33
Q

F actin crosslinking protein

A

Filamin

34
Q

Profilin

A

binds to actin causing a conformational change that promotes addition

35
Q

Thymosin

A

locks actin so it can’t associate with + end, preventing growth, “locking it in place”

36
Q

Arp 2/3 complex causes

A

a caping so there is no growth at the minus end

this accelerates polymerization

37
Q

ARP2/3 Complex as Microfilament Nucleator:

A
  • Caps Pointed (associate with minus end)
  • Analogous to GammaTRC for MTs
38
Q

The Arp 2/3 complex can bind to the side of a filament causing

A

pointed nucleation or branched actin

39
Q

Formins have a __ that attaches to ___

A

dimer attaches to the plus (barbed) end of a growing filament -> promoting nucleation and additional growth

(there is no branching)

40
Q

Filamin

A

is a dimer, cross linking actin, loos arraignment causes a gel like state

is important for membrane extensions ex. filopodia

clamps together pairs of actin filaments roughly at right angles, thereby promoting the formation of a loose and highly viscous gel.

41
Q

How does Listeria use actin to infect a cell

A

Has receptors for Arp2/3, nucleates actin, tail is then like a motor, is mobile through a cell, then infects another cell

42
Q

Myosin is a ___, using ___

A

is a motor protein, ATPasse

uses energy from ATP hydrolysis to move (very similar to transport proteins)

43
Q

Myosin II is composed of

A

two heads with a long tail.

Composed of 2 heavy chains (green) and four light chains (blue)

The heavy chains form coiled coils

44
Q

In Myosin II ___ binds to ATP

A

the head domains, is the area of conformation change (what binds to ATP)

45
Q

Tail-tail interactions of myosin form

A

large, bipolar thick filaments, with several hundred myosin heads

The head domains are pointed outward - bind to actin

46
Q

The bare zone of the myosin II bipolar thick filament is composed of

A

myosin tails

47
Q

Each myosin head binds to and hydrolyzes ATP, causing it to walks towards ___

A

the plus end of actin filament

inches towards end, actin slides in opposite direction

48
Q

Steps of the myosin actin cycle

A
  1. Myosin (lacks bound nucleotide)-binds tightly to actin
  2. ATP binds to myosin (conformational change in actin binding site, reduced binding affinity of myosin head to actin)
  3. Bound ATP triggers movement of lever arm (myosin head displaced along actin filament). ATP hydrolysis
  4. Weak binding of myosin head to new site on actin causes release of Pi, myosin head binds tightly to actin.
  5. Release of Pi triggers power stroke (release of ADP)-original conformation of myosin head

(4/5 - same step)

49
Q

Skeletal muscle cells (muscle fibers) anatomy

A

Huge, multinucleated cells (formed by fusion of many muscle cell precursors).

Myofibrils: cylindrical structure found in cytoplasm (consists of contractile units called sarcomeres)

50
Q

Dynamics of the sarcomere

A

not as much dynamics because it is capted at both sides

51
Q

Thin vs thick filaments of sarcomere

A

Thin filaments: actin and associated proteins, attached to Z disc (+ end). Capped (- end) of actin extend towards middle of sarcomere (overlap with thick filaments)

Thick filaments: bipolar assemblies of myosin II

52
Q

Organization of accessory proteins in a sarcomere

A

(Image)
Z disk end of actin - Plus end
Capted end of actin- Minus end
M line - myosin

53
Q

Muscle cell features make rapid contraction possible

A
  1. Myosin motor heads spend a fraction of ATP cycle time bound to thin filament, which allows many myosin heads to act in rapid succession on same actin (not interfere with each other)
  2. Specialized membrane system relays signal rapidly throughout cell

(during contraction - overlap but actin and myosin did not changed in length)

54
Q

Neuromuscular junction activation and Ca2+ Channels

A

VGCa 2+ channel - close to Ca 2+ release channel -

55
Q

T tubules and the sarcoplasmic reticulum

A

The T tubules are formed from an invagenation of the plasma membrane - they cover the myofibril - they allow for rapid contraction

56
Q

Calcium dependence of skeletal muscle contraction is due to

A

accessory proteins that are closely associated with the actin thin filaments

57
Q

Ca in muscle contraction

A

Ca2+ floods into cytosol, initiating contraction of each myofibril.

Increase in calcium is short-lived, Ca2+ pump actively transports calcium ions back to SR (restored concentrations within 30ms, allowing myofibrils to relax)

Two energy requiring steps: ATPase of myosin motor domain and Ca2+ pump

58
Q

troponin

A

three polypeptide chains that are Ca sensitive

binding of Ca causes a change in tropomyosin, causing it to move away from binding sites so they can bind to actin

Cell Bio Final Exam (5 decks)

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