29 - Cytoskeleton Flashcards

1
Q

Do you know?

A

review

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What are the functions of the cytoskeleton?

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What are the 3 types of cytoskeletal proteins?

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What is the structure of a microtubule and its subunit?

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What is the centrosome?

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

How is a microtubule formed and elongated? What provides the energy needed to catayluze this process? How does this process work kinetically?

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

How do microtubules depolymerize? How are they held together?

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Why is having multiple protofilaments in a microtubule advantageous?

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Describe the process of microtubule filament treadmilling.

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Where are microtubules used in cellular motion? What are the charecteristics of this motion?

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

How do microtubules organize in an axoneme?

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What are some mutations that disrupt cilia and flagella? What diseases are associated with these mutations?

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What role does the cytoskeleton play in changes in cell shape?

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

How are microtubules organized in cells?

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What are the functions of microtubule associated proteins (MAPs)?

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What are molecular motor proteins?

A
17
Q

Describe kinesin motor protein domains.

A
18
Q

Describe the dynein family of motor proteins.

A
19
Q

Describe intraflagella transport (turnaround zones).

A
20
Q

Describe the assembly of intermediate filaments.

A
21
Q

What is the distribution of intermediate filament proteins?

A
22
Q

Describe actin and its structure, function, and subumit.

A
23
Q

How does a cell “crawl forward”?

A
24
Q

What are the mechanical properties of actin, tubulin, and intermediate filament proteins?

A
25
Q

How is actin organized in microvilli?

A
26
Q

What are the types of actin filament bundles?

A
27
Q

What are the 4 actin cross-linking proteins?

A
28
Q

What happens when a mutant keratin gene causes improper filament network formation?

A
29
Q

How does taxol affect microtubule polymerization?

A

Taxol affects microtubule polymerization by stabilizing microtubules. Taxol binding stabilizes microtubules by inhibiting depolymerization (shrinkage) and promoting polymerization (growth) of microtubules.

30
Q

What is phalloidin?What does it do?

A
31
Q

What is cytochalasin? What does it do?

A

Actin-specific drug. caps the filament’s plus (+) end

32
Q

How is actin polymerized?

A

Actin polymerization is the process by which actin monomers assemble into long, filamentous structures called actin filaments or microfilaments. Actin filaments are a crucial component of the cell’s cytoskeleton, and they play essential roles in various cellular processes, including cell motility, muscle contraction, and cell division. Here’s an overview of actin polymerization:

Actin Monomers (G-Actin):
    Actin polymerization begins with individual actin monomers, often referred to as G-actin (globular actin). G-actin molecules are globular in shape and are typically found in a soluble form within the cytoplasm of the cell.

Nucleation:
    The first step in actin polymerization is nucleation, during which a small number of G-actin molecules come together to form the nucleus of the actin filament. Nucleation is a critical and rate-limiting step in the process.
    Nucleation can be spontaneous but is often facilitated by nucleating proteins called actin nucleators. These nucleators help G-actin molecules assemble into the initial nucleus.

Elongation:
    Once the nucleus is formed, additional G-actin monomers rapidly add to the ends of the growing filament. Actin filaments have two distinct ends:
        (+) End: This is the fast-growing end where G-actin subunits are added more quickly.
        (-) End: This is the slow-growing end.

Treadmilling:
    Actin filaments can exhibit a phenomenon known as treadmilling, where subunits are simultaneously added at the (+) end and removed from the (-) end.
    This dynamic behavior allows actin filaments to continuously remodel and adapt to the cell's needs.

Stabilization and Binding Proteins:
    Various proteins interact with actin filaments to regulate their polymerization and stability. For example:
        Tropomyosin: Tropomyosin molecules lie along the length of actin filaments and help stabilize them.
        Capping Proteins: Capping proteins bind to the ends of actin filaments, preventing further polymerization or depolymerization.
        Severing Proteins: Severing proteins can cut actin filaments into smaller fragments, influencing their dynamics.

Function in Cells:
    Actin filaments are involved in a wide range of cellular processes, including cell motility (e.g., cell crawling, muscle contraction), cell division (e.g., cytokinesis), and the maintenance of cell shape.
    In muscle cells, actin filaments interact with myosin to generate the force required for muscle contraction.
    In non-muscle cells, actin filaments form networks and bundles that provide mechanical support and facilitate cell movement and shape changes.

Regulation:
    Actin polymerization is tightly regulated by various signaling pathways and cellular cues. Cells can rapidly modulate actin dynamics in response to external stimuli or intracellular signals.

In summary, actin polymerization is a highly dynamic and regulated process that involves the assembly of actin monomers into long filaments. These filaments serve as critical structural and functional components of the cell’s cytoskeleton, allowing cells to perform various essential functions, from cell motility to cell division. The dynamic nature of actin filaments, with ongoing assembly and disassembly, enables cells to adapt and respond to their ever-changing environment.

33
Q

What is swinholide? What does it do?

A

actin specific drug. severs filaments.

34
Q

What is lantrunculin? What does it do?

A

actin specific drug. binds subunits and prevents polymerization. truncates by stopping polymerization.

35
Q

What is taxol? What does it do?

A
36
Q

What is colchicine/colcemid? What does it do?

A

microtubule specific drug. binds subunits and prevents their polymerization.

37
Q

What is vinblastine/vincristine? What does it do?

A

microtubule specific drug. binds subunits and prevents their polymerization.

38
Q

What is nocodazole? What does it do?

A

microtubule specific drug. binds subunits and prevents their polymerization.