Cytoskeleton Flashcards

(60 cards)

0
Q

Microtubules are?

A

25 nm in diameter. Major component is tubulin. Much more rigid than actin.

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1
Q

Microfilaments are?

A

6 nm in diameter. Major component is actin. G-actin is globular. F-actin is filament

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2
Q

Function of actin?

A

Associated with plasma membrane to determine the topology and is connected with the cellular functions of the membrane

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3
Q

4 examples of actin filaments

A

Microvilli
Stress fibers
Lamellipodia and filopodia for moving cell
Contractile ring during cell division

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4
Q

What form is actin in at low concentration?

A

Globular G-actin

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5
Q

In presence of ATP or ADP, as you increase actin concentration what happens?

A

Polymerizes into actin filament with a + and - end

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6
Q

Three phases of actin polymerization

A
Slow nucleation (just + nuclei)
Fast elongation (both nuclei)
Steady state
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7
Q

T or F: ATP is absolutely necessary for actin polymerization

A

F, can work in presence of ADP too just different kinetics

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8
Q

What is the actin critical concentration?

A

Minimal G-actin concentration needed for polymerization to occur. Above this concentration, you get mix of polymers and free subunits, below just free subunits.

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9
Q

Which end of actin grows faster?

A

Grow faster at + end than the - end. Critical concentration is lower at the + end than the - end. Can lead to a process known as treadmilling

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10
Q

Example of actin treadmilling

A

Leading edge of moving cells

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11
Q

What is an actin-monomer binding protein?

A

Regulates actin polymerization by binding to free actin molecules

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12
Q

What is thymosin? Profilin?

A

Thymosin is a actin-monomer binding protein. Profilin is antagonist to thymosin and promotes actin polymerization

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13
Q

How does listeria monocytogenes move inside a cell?

A

Recruits actin in the cell and polymerizes behind itself. Pushes the bacterium around using profilin. Can move fast enough to make a microvilli out of the host cell.

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14
Q

What are Arp 2/3?

A

Two actin related proteins that can catalyze the nucleation and polymerization of actin. Similar to the + end of actin. Binds to the minus end and encourages elongation at the + end of polymer.

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15
Q

What is gelsonin?

A

Caps the plus end of actin and severs it. Ca+2 mediated. From macrophages

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16
Q

What is villin?

A

Ca+2 activated F-actin severing protein. From intestine

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17
Q

What are capping proteins?

A

Cap actin to prevent degredation

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18
Q

How do platelets change shape to clot blood?

A

Drastically increase amounts of F-actin after stimulation

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19
Q

Describe platelet activation

A

Controlled sequence of actin filament severing, uncapping, elongation, recapping, and cross-linking of actin (mediated by Ca+2 and PIP2)

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20
Q

What are the general characteristics of F-actin cross linking proteins?

A

Two F-actin binding sites. The length and flexibility of the crosslinking protein determines whether bundles or networks are formed

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21
Q

Name 5 actin cross linking proteins

A

Spectrin, alpha-actinin, filamin, fimbrin, dystrophin

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22
Q

Alpha-actinin forms what?

A

Contractile bundles (muscle)

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23
Q

Fimbrin forms?

A

Parallel bundles that are tight (no myosin)

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24
Filamin forms?
Crossed actin fibers
25
Microvilli use what actin cross-linking proteins?
Villin or fimbrin. plus end is at tip of microvillus
26
Platelets attach actin to clots via?
Filamin
27
Actin is connected to muscle ECM by?
Dystrophin
28
What type of myosin is in muscle?
Myosin II
29
Describe general structure of myosin
Head, neck, tail domains. Tail domain provides myosin with distinct function
30
Detail myosin and actin relationship
Myosin heads walk down the actin filament towards the + end using ATP for each step.
31
Structure of myosin II
Two heavy chains and four light chains. Heavy chains have heads with ATPase activity Dimerization occurs into a coil-coil structure of two alpha-helical tails.
32
T or F: The polarity of the myosin filament is reversed at the M-line in the sarcomere
T (in order for the myosin to walk toward the plus ends of the actin at the z-disk)
33
Functions of actin and myosin II outside of muscle?
Contractile ring, stress fibers in fibroblasts, adhesion belts in epithelial cells.
34
What determines the type of myosin?
The tail domain
35
Function and description of myosin I?
One headed, moves vesicles around the cell, attaches to plasma membrane. Links with actin bundles in microvilli.
36
Function of myosin V?
Vesicular transport of secretory vesicles
37
What is tubulin?
Heterodimer of two closely related subunits. Alpha and beta tubulin.
38
Structure of microtubules
Tubulin heterodimers packed around central core. 13 protofilaments aligned in parallel making the structure polar. Fast growing + end and slow growing - end.
39
Tubulin will polymerize in the presence of?
37 degrees C, Mg, GTP
40
Describe the dynamic instability of microtubules
GTP on beta-tubulin causes for the formation of straight filament polymers. GTP hydrolysis weakens the bond in the polymer and can lead to depolymerization in order to exchange GDP for GTP
41
T or F: GTP hydrolysis lags behind polymerization in microtubule formation
T, two classes those with GTP caps or ones that are all GDP
42
Two classes of microtubules
GTP cap - growth GDP - disassembly Capping proteins can be used to prevent GDP destabilization
43
Examples of microtubule function
Cytoplasmic microtubules in interphase Mitotic spindle Structure microtubules in cilia and flagella
44
What are cilia?
Hair like appendages with bundles of microtubules at core. Contain the axoneme.
45
Describe axoneme
9+2 model. 9 doublets, one complete ring and one partial, 11 subunits. 2 center full 13 subunit microtubules
46
What is ciliary dyenin?
Drives bending motion in the axoneme. Walks toward the minus end of tubule.
47
What are basal bodies?
Lower portion of the axoneme. Composed of 9 sets of triplet microtubules (1 full, 2 incomplete). Centriole have same form as the basal body.
48
What is the MTOC?
Polymerization centers. Nested minus end and plus end growing out.
49
What is the centrosome?
A MTOC with many copies of gamma-tubulin in a ring complex, template for the 13 protofilaments. Shaped in L-shape configuration. Duplicate and split to opposite sides of cell when mitosis begins
50
Function of gamma-tubulin
Associates with the alpha-tubulin to form ring. Template for the microtubule 13 protofilaments
51
What is the spindle pole?
The MTOC for mitotic spindle (- ends all there)
52
Kinesin motion?
From minus end to plus end of microtubule
53
Dynein motion?
From plus end to the minus end of the microtubule
54
ER is located where? Golgi?
Align with microtubules and extend almost to end of cell, requires kinesin Golgi near the centrosome, requires dyenin
55
What are polar microtubules?
Microtubules from opposite poles that form the spindle
56
What are Kinetochore microtubules?
From centrosome to the kinetochore o the chromosomes
57
What is anaphase A movement?
Movement of chromosomes to opposite poles (maybe dynein mediatied)
58
What is anaphase B movement?
Sliding of polar microtubules against each other to separate the poles (kinesin mediated)
59
How is polar separation achieved via microtubules?
Four headed kinesin walks toward plus end of tubules and pushes apart the two spindle poles. Dynein walks along the cell cortex from the plus to minus end of astral microtubules