Textbook Chapter 9: Microfilaments Flashcards

1
Q

Actin filaments

A
  • solid, thinner structures, often organized into a branching network.
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2
Q

cytoskeleton (3)

Composed of+each filament is….+construction

A
  • composed of three well-defined filamentous structures—microtubules (MT), actin filaments, and intermediate filaments (IFs)—that together form an elaborate interactive and dynamic network.
  • Each of the three types of cytoskeletal filaments is a polymer of protein subunits held together by weak, noncovalent bonds.
  • This type of construction lends itself to rapid assembly and disassembly, which is dependent on complex cellular regulation
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3
Q

Microtubules (5)

The physical description+found in+Role(2)+consist of+intramolecular interaction

A
  • long, hollow, unbranched tubes composed of subunits of the protein tubulin
  • found in the cytoskeleton, the mitotic spindle, centrioles, and the core of cilia and flagella
  • Roles in cell support and movement of materials within a cell
  • microtubules are seen to consist of 13 protofilaments aligned side by side to form a tubel.
  • Noncovalent interactions between adjacent protofilaments are thought to play an important role in maintaining microtubule structure.
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4
Q

Intermediate filaments

A
  • tough, ropelike fibers composed of a variety of related proteins.
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5
Q

Five function of cytoskeleton:

A
  1. Structural support (cell shape, resisting forces)
  2. Transport of materials and organelles within a cell
  3. Contraction and motility
  4. Spatial organization (hold secretory lysosome ontop)
  5. Cell division
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6
Q

Each protofilament is assembled from dimeric building blocks consisting of one —— and one —– subunit. The two types of globular tubulin subunits have a similar threedimensional structure and fit tightly together. The tubulin dimers are organized in ———. Because each assembly unit contains two nonidentical components (a heterodimer), the protofilament is asymmetric. All of the protofilaments of a microtubule have ——. Consequently, the entire polymer has —–. One end of a microtubule is known as the plus end and is terminated by a row of ——–. The opposite end is the minus end and is terminated by a row of ——-.

A
  • α-tubulin
  • β-tubulin
  • in a linear array along the length of each protofilament
  • the same polarity
  • polarity
  • β-tubulin subunits
  • α-tubulin subunits
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7
Q

Microtubule-associated proteins (or MAPs) (2)

What they do+ controlled by

A
  • increase the stability of microtubules and promote their assembly by linking tubulin subunits together, making it harder for them to fall apart.
  • activity of some MAPs is controlled by the addition and removal of phosphate groups from particular amino acid residues
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8
Q

Structures and materials traveling from the cell body toward the terminals of a neuron are said to move in ——- direction

A

an anterograde direction

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9
Q

Microtubules as structural supports (3):

What+ help determine+maintains

A
  • Microtubules provide mecanical support: Are stiff enough to resist compression or bending forces
  • Help determine the shape of a cell
  • Maintains intracellular location of organelles
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10
Q

Microtubules as agents of intracellular motility (2)

Two types of stuff it transports

A
  • Transport of membrane vesicles from one membrane compartment to another
  • Transport non membrane bound cargos (RNAs, ribosomes, cytoskeletal elements)
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11
Q

How do the motor proteins of a cell generate force?

A

convert chemical energy (stored in ATP) into mechanical energy, which is used to generate force, as occurs when a muscle cell contracts, or to move cellular cargo attached to the motor

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12
Q

Collectively, motor proteins can be grouped into three
broad superfamilies:

A

kinesins, dyneins, and myosins

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13
Q

Kinesins and dyneins move along ——, whereas myosins move along —–

A
  • microtubules
  • actin filaments
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14
Q

No motor protein is known that uses intermediate filament tracks. This is not surprising considering that intermediate filaments are ……

A

not polarized and thus would not provide directional cues to the motor.

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15
Q

Kinesins (4)

Family+constructed from+head+tail

A
  • kinesin will refer only to members of the kinesin-1 family
  • Each kinesin-1 molecule is a tetramer constructed from two identical heavy chains and two identical light chains
  • a pair of globular heads that bind a microtubule and act as ATP-hydrolyzing, force-generating “engines.”
  • Each head (or motor domain) is connected to a neck, a rodlike stalk, and a fanshaped tail that binds cargo to be hauled
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16
Q

The motor portions of all KRPs have related amino acid sequences, reflecting their common evolutionary ancestry and their similar role in moving along microtubules. In contrast, the tails of KRPs have ——, reflecting the ——-. A number of different proteins
have been identified as potential adaptors that link specific KRPs and their cargoes. Surprisingly, the motor domains of kinesins are strikingly similar in structure to those of myosins, despite the fact that kinesins are much smaller proteins and the two types of motors operate over different tracks. Kinesins and myosins almost certainly evolved from a common ancestral protein present in a primitive eukaryotic cell.

A
  • diverse sequences
  • variety of cargo these motors haul
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17
Q

In an axon, where all of the microtubules are oriented with their minus ends facing the cell body, kinesin transports vesicles and other cargo toward —–

A

the synaptic terminals

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18
Q

A single kinesin molecule moves along a single —– of a microtubule at a velocity ——

A
  • protofilament
  • proportional to the ATP concentration
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19
Q

Each step of the kinesin molecule is approximately —- in length, which is also the length of ——-, and requires the hydrolysis of —– ATP molecule

A
  • 8 nm
  • one tubulin dimer in a protofilament
  • a single
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20
Q

The movement of kinesin molecules, both in vitro and in vivo, is highly processive, meaning that——. This is because……

A
  • the motor protein tends to move along an individual microtubule for considerable distances (over 1 µm) without falling off.
  • A two-headed kinesin molecule can accomplish this
    feat because at least one of the heads is attached to the microtubule at all times
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21
Q

Explain the kinesin movement:

A
  • Leading head binds one ATP: Hydrolysis and release of ADP + Pi = powerstroke that swings trailing head forward
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22
Q

members of the kinesin superfamily tend to move vesicles and organelles (e.g., peroxisomes and mitochondria) in an outward direction toward the cell’s —–

A

plasma membrane

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23
Q

Dynein (6)

what it is responsible for+ composed of chains+structure+head function+stalk+projection

A
  • the protein responsible for the movement of cilia and flagella
  • a huge protein composed of two identical heavy chains and a variety of intermediate and light chains
  • Each dynein heavy chain consists of a large globular head with an elongated projection (stalk)
  • The dynein head, which is larger than a kinesin head, acts as a force-generating engine.
  • Each stalk contains the all-important microtubule-binding site situated at its tip.
  • The longer projection, known as the stem (or tail), binds the intermediate and light chains
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24
Q

Dyein moves towards

A
  • moving toward the minus end of the track
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25
Q

Both motor proteins are attached to the vesicle membrane by an intermediary:

A
  • kinesin can be attached to vesicles by a variety of integral and peripheral membrane proteins
  • dynein by a protein complex called dynactin
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26
Q

A body of evidence suggests at least two well-studied roles for cytoplasmic dynein:

A
  1. Positioning the spindle and moving chromosomes during mitosis
  2. Positioning organelles and moving vesicles
27
Q

In nerve cells, cytoplasmic dynein has been implicated in the —- movement of membranous organelles and the —- movement of microtubules.

A
  • retrograde
  • anterograde
28
Q

In fibroblasts and other nonneural cells, cytoplasmic dynein is thought to transport membranous organelles
from — locations toward the —- of the cell

A
  • peripheral
  • center
29
Q

centrosome

A
  • a complex structure that contains two barrel-shaped centrioles surrounded by shapeless, electron-dense pericentriolar material (or PCM)
  • Centrioles are cylindrical structures about 0.2 µm in diameter and typically about twice as long.
30
Q

the microtubules of the cytoskeleton are typically initiated by the —-

A

centrosome

31
Q

When centrosomes replicate (2)

PCM+Centrioles

A
  • Centrioles recruit PCM to form a new centrosome with centrioles embedded in a cloud of PCM
  • New centrioles typically form adjacent to, and at right angles with, preexisting centrioles.This process of centriole duplication means that most cells contain a pair of connected centrioles in which one termed the mother, is at least one cell cycle older than the other, which is termed the daughter.
32
Q

Centrosomes are microtubule organizing centers, they (any MTOC) dictate (4):

A
  • the number of microtubules
  • their polarity
  • the number of protofilaments that make up their walls
  • the time and location of their assembly.
33
Q

Explain the interaction beween microtubules and the centrosome

A

Close examination shows that the microtubules do not actually penetrate into the centrosome and make contact with the centrioles but terminate in the dense PCM that resides at the centrosome periphery. (microtubules are initiated in the PCM)

34
Q

Microtubules are nucleated at the centrosome and grow at their —- ends, while the —- ends remain anchored at the centrosome.

A
  • plus
  • minus
35
Q

In addition, all MTOCs share a common protein component—a type of tubulin called—–

A

γ-tubulin

36
Q

γ-tubulin is a critical component in —-

A

microtubule nucleation

37
Q

The number of protofilaments in the microtubule is apparently dictated by —–. In this model, only the —–tubulin of the heterodimer can bind to a ring of γ-tubulin subunits. Thus, the—- determines the polarity of the entire microtubule and also forms a cap at its minus end, preventing the gain or loss of tubulin subunits.

A
  • the number of γ-tubulins around the ring
  • α
  • γ-TuRC (Tubulin ring complex)
38
Q

How are microtubule initiated?

A
  • γ-TuRC is a helical array of γ-tubulin (brown)
    subunits, each bound with a set of accessory proteins. This provides a place for microtubules to assemble and speeds it up.
39
Q

PCM contains: y-TuRC (2)

A
  • y-tubulin
  • Non tubulin proteins in a ring (accessory)
40
Q

These differences in microtubule stability are determined by microtubule-interacting proteins including … (3)

A
  1. MAPs, which stabilize microtubules
  2. proteins known as +TIPs, which bind to the plus end of growing microtubules
  3. Temperature (cold = dissassembly)
41
Q

Assembly of tubulin dimers requires that a GTP molecule be bound to the —-tubulin subunit. As it turns out, β-tubulin is not only a structural protein, it is also —-, a GTPase. GTP hydrolysis is not required for ——. Rather, the GTP is hydrolyzed to GDP shortly after ——, and the resulting GDP ——-. After a dimer is released from a microtubule during disassembly and enters the soluble pool, the GDP is replaced by a new GTP. This nucleotide exchange “recharges” the dimer, allowing it to serve once again as a building block for polymerization.

A
  • β
  • an enzyme
  • the actual incorporation of the dimer onto the end of a microtubule
  • the dimer is incorporated into a microtubule
  • remains bound to the assembled polymer
42
Q

GTP is not hydrolyzed by

A

α-tubulin

43
Q

Thus, it would appear that GTP hydrolysis is a fundamental component of the dynamic quality of microtubules because….

A

The strain energy stored in a microtubule as a result of GTP hydrolysis makes the microtubule inherently unstable and—in the absence of other stabilizing factors such as MAPs—capable of disassembling soon after its formation. Which is why b-tubulin becaomes hydrolyzed to GDP.

44
Q

dynamic instability steps of what happens:

A
  1. the tip consists of an open sheet containing tubulin-GTP subunits
  2. The tube has begun to close, because of the hydrolysis of the bound GTP
  3. The tube has closed to its end, leaving only tubulin-GDP
    subunits. GDP-tubulin subunits have a curved conformation compared to their GTP-bound counterparts, which makes them less able to fit into a the
    microtubule lattice. The strain resulting from the presence of GDP-tubulin subunits at the plus end of the microtubule is released as the protofilaments curl outward from the tubule and undergo catastrophic shrinkage
45
Q

+TIPs

A
  1. bind to the dynamic plus ends of microtubules and regulate the rate of the microtubule’s growth or shrinkage
  2. mediate the attachment of the plus end of the microtubule to a specific cellular structure, such as the kinetochore of a mitotic chromosome during cell division or the actin cytoskeleton of the cortex during vesicle transport
46
Q

—– of a microtubule can push on an attached object, whereas —– of a microtubule can pull on an attached object

A
  • Polymerization
  • depolymerization
47
Q

Cilia

Motile cilia+ what they do in organisms (multicell)

A
  • Motile cilia tend to occur in large numbers on a cell’s surface, and their beating activity is
    usually coordinated
  • In multicellular organisms, cilia move fluid and particulate material through various tracts
48
Q

Flagella

A
  • typically occur singly or in pairs and exhibit a variety of different beating patterns (waveforms), depending on the cell type.
49
Q

The entire ciliary or flagellar projection is covered by ——

A

a membrane that is continuous with the plasma membrane of the cell.

50
Q

The core of the cilium, called the —–, contains an array of ——- through the
entire organelle.

A
  • axoneme
  • microtubules that run longitudinally
51
Q

All microtubules of the axoneme have the same polarity: Their plus ends are at the —- and their minus ends are at the —-.

A
  • tip of the projection
  • base
52
Q

Structure of the axoneme (2)

Structural+dynein

A
  • 9 peripheral doublet microtubules around a central pair of single microtubules (9+2 array)
  • dynein tails are anchored to one of the tubules in each pair (A tubules, dark blue)
53
Q

Doublets in the axoneme are connected to eachother via ….. which acts to ….

A

Nexin: a linker between neighboring doublet microtubules, acts to stabilize the axonemal core structure

54
Q

Actin is the most —- protein in most cells

A

abundant

55
Q

Actin filaments are composed of

A

gobular subunits (G-actin)

56
Q

Inidividual G-actin monomer have —- and are added to the filament in a ——

A
  • directionality
  • particular orientation
57
Q

Actin filaments are a —– and ——

strands

A
  • double stranded helix
  • oriented in the same directioin
58
Q

The + end of actin is known as the —– and the - end is known as the ——

A
  • barbed
  • pointed
59
Q

Before it is incorporated into a filament, an actin monomer binds a —–. The —– associated with the actin monomer is hydrolyzed to —- at some time after ——. As a consequence, the bulk of an actin filament consists of ——.

A
  • molecule of ATP
  • ATP
  • ADP
  • it is incorporated into the end of a growing actin filament
  • ADP–actin subunits
60
Q

The barbed and pointed ends require different minimal concentrations of ATP-actin monomers in order to elongate, a measure known as the critical concentration. The critical concentration of the barbed end is much —- than that of the pointed end, meaning that the barbed end can continue to elongate at —- ATP-actin concentrations than the pointed end can.

A
  • lower
  • lower
61
Q

All myosins except type —- move towards the + barbed end

A

VI

62
Q

Unconventional Myosin Type V

A
  • take very large steps (36 nm)
  • a two-headed unconventional myosin involved in organelle transport
  • tail bond to a vesicle via adaptors (Rab 27a)
63
Q

As discussed later, the motor activity of myosin moves its head groups along the actin filament in the direction of the —- end

A

plus