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Cytoskeleton Flashcards

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1
Q

Cytoskeleton

A

A dense network of protein filaments that crisscrosses the cytosol and provides support to cell membranes. It helps the cell to maintain its shape and move around

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2
Q

What is the cytoskeleton made of?

A

Protein filaments. Each type of protein filament is assembled from certain subunits reversibly so that cells can assemble or disassemble the filaments if they need to. The filaments are polymers whose assembly is regulated.

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3
Q

How can the cytoskeleton be visualized? (2 ways)

A
  1. Electron microscopy. Detergents are used to make the plasma membrane and organelles soluble and to release the cytoplasm
  2. Immunofluorescence microscopy. Provides colored networks of each type of protein
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4
Q

3 protein filament systems of the cytoskeleton

A
  1. Microfilaments
  2. Microtubules
  3. Intermediate filaments
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5
Q

Microfilaments

A

Polymers of actin that are organized into networks by actin binding proteins. Form rigid gels and linear bundles as well. They organize the plasma membrane and give support to surface structures like microvilli. They also serve as tracks for motor proteins and work with myosin to provide contractile function, like a muscle

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6
Q

Microtubules

A

Rigid tubes formed from the protein tubulin, organized by microtubule associated proteins. They make up the mitotic spindle that is necessary for cell division. Organize organelles and support cilia. Motor proteins (kinesins and dyneins) transport cargo along microtubules for long range transport of organelles.

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7
Q

Motor proteins

A

Proteins that use ATP hydrolysis to generate linear or rotational motion. They use microfilaments as tracks and use microtubules to transport cargo.

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8
Q

Intermediate filaments

A

Polymers made from tissue-specific subunits and assembled into pre-existing filaments. Located on the inside of the nucleus. They give support to the cell membrane and give structural integrity to cells in tissues. They have structural and barrier forming functions in hair, skin, and nails. They are not used as tracks by motor proteins and are less dynamic that microtubules and microfilaments.

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9
Q

Actin filaments and epithelial cells

A

Actin filaments are found on epithelial cells and can be visualized on microvilli. The apical and basal domains of epithelial cells are responsible for transporting nutrients. Nutrients are moved from the lumen at the apical surface through the basal surface to the bloodstream. Therefore, the apical and basal domains of epithelial cells require multiple transport proteins to function correctly.

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10
Q

How do cells use actin filaments? (2)

A
  1. Dynamic bursts of actin filament assembly power the movement of endocytic vesicles away from the plasma membrane
  2. During mitosis when organelles have been duplicated and segregated, actin forms a contractile ring to constrict and generate 2 daughter cells
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11
Q

How are microfilaments arranged in the cell?

A

There can be multiple arrangements of microfilaments within a single cell.

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12
Q

Actin

A

An abundant intracellular protein in eukaryotic cells. Their abundance depends on their location in the cell or tissue. Actins have been classified into alpha, beta, and gamma categories based on their charge.

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13
Q

G-actin

A

A globular monomer of actin. G-actin is separated into 2 lobes by a cleft. There is a site for ATP and magnesium to bind at the base of the cleft, called the ATPase fold. When ATP or ADP bind to G-actin, the nucleotide changes the conformation of the molecule. G-actin can polymerize to form F-actin in a reversible reaction.

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14
Q

F-actin

A

A filamentous polymer of actin, which is a linear chain of actin subunits. F-actin is a major component of microfilaments.

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15
Q

Polarity of actin filaments

A

All subunits in an actin filament are oriented the same way, so the filament exhibits polarity (one end is different from the other). The positive end is where actin subunits are added, which is also where the ATP binding cleft of the terminal actin subunit comes in contact with the neighboring subunit. The negative end is where subunits are removed.

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16
Q

Which electron micrography finding demonstrates the polarity of actin subunits?

A

The myosin S1 head domains bind to actin subunits in a specific manner. When bound to all the subunits in a filament, S1 looks like it’s spiraling around the filament, forming arrowhead-like decorations. The negative end is pointed and the positive end is barbed

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17
Q

3 phases of G-actin polymerization in vitro

A
  1. Nucleation phase
  2. Elongation phase
  3. Steady-state phase
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18
Q

Nucleation phase of actin polymerization

A

There is a lag period in which G-actin subunits combine into an oligomer of 2-3 subunits. Once the oligomer gets to 3 subunits, it can act as a seed for the next phase.

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19
Q

Elongation phase of actin polymerization

A

The short oligomer rapidly increases in length as actin monomers are added to each of its ends. As the F-actin filaments grow, the concentration of G-actin filaments decreases until there is equilibrium between the filaments and monomers. The system reaches a steady state

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20
Q

Steady-state phase of actin polymerization

A

G-actin monomers exchange with subunits at the filament ends, but there’s no net change in the total length of the filaments

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21
Q

Treadmilling

A

The two ends of a myosin decorated actin filament grow at different rates. Treadmilling occurs when ATP-actin subunits are added faster at the positive end than the negative end of the actin filament. This causes a lower critical concentration at the positive end and treadmilling at a steady state. Once the molecule gets to a steady state, subunits are now added to the positive end and the negative end has a low concentration- this is treadmilling. Only occurs in a test tube, not in situ cells. Can occur in microtubules as well.

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22
Q

Cytochalasin D

A

A fugal product that poisons actin by depolymerizing actin filaments. It binds to the positive end of F-actin and inhibits addition of subunits. The actin cytoskeleton will disassemble and cell movements like locomotion and cytokinesis are inhibited.

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23
Q

Phalloidin

A

Used to localize F-actin in fluorescence microscopy. It is a mushroom toxin that binds at the interface between subunits in F-actin, which locks the subunits together and prevents actin filaments from depolymerizing. Many processes depend on actin filament turnover, so phalloidin causes these systems to no longer work and the cell dies.

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24
Q

Rate limiting step of actin polymerization

A

The formation of an initial actin nucleus from which a filament can grow. This step is a control point in cells, which determines where actin filaments are assembled and what type of actin structures can be generated

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25
Q

Formin

A

A protein that regulates actin assembly through signal transduction pathways. Formin leads to the assembly of long actin filaments. The FH2 formin domain forms a donut shaped complex to bind two actin subunits. It holds the subunits so that the positive end of the newly synthesized filament is pointing toward the FH2 domain. The filament will grow at this end with the FH2 domain still attached.

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26
Q

Profilin

A

Profilin can exchange the ADP nucleotide on G actin for ATP to generate profilin-ATP-actin. The FH1 domain of formin acts as a landing site for profilin-ATP-actin to increase the concentration of these complexes. The actin from the profilin-actin complexes is fed into the FH2 domain to add actin to the positive end of the filament, and profilin is released. Studied using optical tweezers

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27
Q

Thymosin

A

Cells typically have a very large amount of G-actin, but the actin does not polymerize. This is because of thymosin. It binds to ATP-G-actin, which inhibits addition of the actin subunit to either side of the filament. It acts as a buffer of unpolymerized actin, making ATP-actin subunits available as needed.

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28
Q

Capping proteins

A

Cells can regulate treadmilling and actin filament dynamics using capping proteins that bind to filament ends. There are 2 classes- one that binds positive ends and one that binds negative ends. Without capping proteins, the filaments would continue to grow and disassemble in an uncontrolled manner

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29
Q

CapZ

A

A capping protein that binds with high affinity to the positive end of the actin filament. It inhibits subunit addition or loss. Its activity can be inhibited with regulatory phospholipid PI(4,5)P2. Also, some regulatory proteins are able to bind the positive end and protect it from CapZ, while still allowing assembly there if necessary.

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30
Q

Tropomodulin

A

A regulatory protein that inhibits filament assembly and disassembly by binding to the negative end of an actin filament. Found in cells (like RBCs) where actin filaments have to be stabilized for long periods of time. It works with tropomyosin to stabilize the filaments

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31
Q

Severing proteins

A

Proteins that sever actin filaments. One protein, gelsolin, is regulated by calcium concentration. Once it binds calcium, gelsolin undergoes a conformational change and inserts itself between the subunits of the actin helix, breaking the filament. It caps the positive end, creating a new negative end that can disassemble

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32
Q

Actin nucleation

A

This is accomplished by the formin FH2 domain. Its forms a dimer and nucleates filament assembly. The dimer binds two actin subunits, and by rocking back and forth, it can allow additional subunits to be inserted between the FH2 domain and the positive end of the growing filament. FH2 protects the filament’s positive end from being capped by capping proteins

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33
Q

Optical traps

A

Used to study molecular motor proteins such as myosin.

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34
Q

Listeria

A

Hijacks normal cell motility processes- if actin filaments become immobilized in the network of the cytoskeleton, it binds to an rides on the positive ends to be transported across the cell. The transportation is powered by massive local polymerization of actin. The polymerization is also used to push listeria through the plasma membrane into the next cell. Listeria is a food borne pathogen that causes gastrointestinal symptoms.

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35
Q

How does listeria move around the cell?

A

Listeria has a surface protein called ActA, which has an actin binding site and an acidic region which activates the Arp 2/3 complex. When 4 proteins are added (Arp 2/3, cofilin, CapZ, and ATP-G-actin) listeria is able to move. Due to CapZ function, assembly of actin occurs adjacent to the bacteria, where ActA is stimulating the Arp 2/3 complex

36
Q

Cofilin

A

Cofilin is necessary to accelerate the disassembly of the negative region of the actin filament, which regenerates free actin to keep the polymerization cycle going

37
Q

ARP 2/3 dependent actin assembly during endocytosis

A

Studied using endosomes that had taken up fluorescently labeled transferrin. Endocytosis assembly factors recruit NPFs that activate the ARP 2/3 complex. Driven by F-actin like listeria. A burst of ARP 2/3 actin assembly drives the movement of endocytic vesicles away from the plasma membrane

38
Q

Phagocytosis and actin dynamics

A

Actin assembly and contraction drives the phagocytosis of particles. When a bacterium invades, it is coated by antibodies specific to a cell-surface protein in a process called opsonization.

39
Q

Opsonization steps (4)

A
  1. As the fab region of the antibody interacts with the antigen, another domain on the antibody (the Fc domain) is exposed.
  2. The Fc domain of the antibody is displayed on the surface of the bacteria it’s bound to. It is recognized by the Fc receptor on the leukocyte surface
  3. This interaction tells the cell to assemble a contractile actin structure that results in the bacteria being engulfed
  4. The bacteria is internalized into a phagosome and is killed and degraded by lysosomes
40
Q

Lamellipodia

A

Membrane protrusions located at the front of the cell. They play a role in cell motility and are made of cytoskeletal actin proteins.

41
Q

Substratum

A

A surface that a cell attaches to when moving or growing

42
Q

Steps in cell locomotion (4)

A
  1. Lamellipodia extend from the leading edge (front) of the cell
  2. Lamellipodia adhere to the substratum by focal adhesions
  3. The rear part of the cell contracts, causing the majority of the cytoplasm to move forward
  4. The trailing edge of the cell remains attached to the substratum, but it will eventually retract into the cell body. The membranes and integrins at the back of the cell are internalized and recycled to make new adhesions
43
Q

Which actin based structures are involved in cell locomotion? (4)

A
  1. There is a network of actin filaments in the leading edge that moves the cell forward
  2. Stress fibers attached to focal adhesions pull up the cell body as rear adhesions are released
  3. Focal adhesions involve attaching stress fibers to the ECM using integrins
  4. There is a dynamic actin network in the leading edge, nucleated by the ARP 2/3 complex
44
Q

Diaphanous gene

A

Linked to sensorineural hearing loss. Actin polymerization involves proteins known to interact with diaphanous protein in Drosophila and mouse. It has therefore been speculated that this gene may have a role in the regulation of actin polymerization in hair cells of the inner ear.

45
Q

Structure of intermediate filaments

A

IF proteins forms parallel, coiled dimers. It has globular heads and tails that are variable in length. Tetramers are formed by two antiparallel, staggered dimers.

46
Q

Assembly of intermediate filaments

A

A mature filament consists of 4 protofibrils (groups of tetramers). Globular domains form beaded clusters on the surface.

47
Q

5 types of intermediate filaments

A
  1. Acidic keratins
  2. Basic keratins
  3. Desmin
  4. Neurofilaments
  5. Lamins
48
Q

Keratins

A

There are acidic and basic keratins, which are found in epithelial cells. There are also hard keratins that make up hair and nails. They provide tissue strength and integrity

49
Q

Soft keratins

A

The type of keratin found in epithelial cells. They make up the skin. The basal layer of the skin cells is in contact with the basal lamina and proliferates constantly, making keratinocytes. Keratinocytes differentiate to make cytokeratins as they leave the basal layer. Cytokeratins make attachment sites between cells to help them withstand abrasion. When the cells die, they leave a cytokeratin network without organelles- the network protects against water evaporation.

50
Q

Desmin, GFAP, and vimentin

A

Found in muscle (desmin), glial cells (GFAP), and mesenchymal cells (vimentin). Function- sarcomere organization and integrity

51
Q

Desmin

A

In smooth muscle, desmin filaments link cytoplasmic dense bodies to the plasma membrane so the cells don’t overstretch. In skeletal muscle, a lattice of desmin filaments surrounds the sarcomere. Desmin plays a structural role in maintaining the integrity of the muscle

52
Q

Neurofilaments

A

NFL, NFM, and NFH make up the neurofilaments found in the axons of neurons. They establish the correct diameter of axons, which determines the rate at which action potentials move down the axon

53
Q

Lamins

A

Most widespread of the intermediate filament proteins. They are components of the network called the nuclear lamina (between the nuclear envelope and the chromatin of the nucleus). There are 3 genes that encode lamins- A, B, and C.

54
Q

Epidermolysis bullosa

A

Keratin associates with desmosomes and hemidesmosomes, to link cells together or to link cells to the extracellular matrix. Therefore, keratin gives structural integrity to epithelial tissue. In epidermolysis bullosa, a mutation in a keratin gene (K14) results in fragile basal cells that can be damaged just from regular movement. The damaged basal cells cause the more superficial layers of the epidermis to blister.

55
Q

Ortec

A

Founded in 1991, was formed to commercialize the technology developed by Dr. Mark Eisenberg, an Australian general practitioner, to treat his son for Epidermolysis Bullosa (EB). To prevent his son from having to undergo additional
surgeries, Dr. Eisenberg discovered that he could create a substitute skin using cells from infant foreskins and delivering these in a collagen matrix. In 1987, Dr. Eisenberg successfully applied the technology he discovered, now known as OrCel®, on his son

56
Q

Nuclear lamina

A

Two dimensional mesh that is located between the nuclear envelope and the chromatin of the nucleus. Made up of lamins. LINC complexes attach lamins to the cytoskeleton through 2 nuclear membranes.

57
Q

Intermediate filament associated proteins

A

The plakin family is one example, which attaches intermediate filaments to other structures. They also link keratin filaments to desmosomes and hemidesmosomes. Plectin is a plakin that connects intermediate filaments to microtubules

58
Q

Desmosomes

A

Junctions between epithelial cells that provide stability to a tissue

59
Q

Hemidesmosomes

A

Located at regions of the plasma membrane where intermediate filaments are linked to the ECM

60
Q

MTOCs

A

Microtubule organizing centers- this is where microtubules are assembled. The MOTC is called a centrosome in an interphase cell and spindle poles in mitotic cells.

61
Q

Protofilaments

A

Microtubules are made up 13 longitudinal repeating units called protofilaments. In tubulin, the dimers are aligned into protofilaments, which form the wall of the microtubulin.

62
Q

Singlet, doublet, and triplet microtubules

A

A singlet microtubule is most typical, and is a tube made of 13 protofilaments, found in cytoplasm. In a doublet, there are 10 additional protofilaments forming another tube, found in cilia and flagella. In a triplet, a tubule of a doublet microtubule forms another tubule, making a triplet structure. These are found in basal bodies and centrioles

63
Q

Dynamic instability

A

Most microtubules will disassemble at 4C and reassemble when cells are warmed to 37C. This method was used to isolate microtubule associated proteins and study their behavior. Microtubules also undergo periods of growth and shrinkage.

64
Q

How does microtubule assembly occur?

A

The alpha beta tubulin concentration must be above the critical concentration. Once the tubulin concentrations are higher than the critical concentration, tubulin dimers are added to the positive end more quickly than the negative end. The positive end is where beta tubulin is exposed.

65
Q

Graphical representation of microtubule assembly

A

When tubulin is warmed to induce polymerization, nucleation, elongation, and steady states (level slope) are seen. When individual microtubules in an assembling population have their lengths plotted at different times, we can see them grow and shrink, demonstrating dynamic instability. The graph looks more jagged in this case. Assembly and disassembly proceed at uniform rates, but shortening of a microtubule is much more rapid than growth

66
Q

Dynamic instability depends on

A

The presence of a GTP beta tubulin cap. The end of a growing microtubule is blunt, while the end of a shrinking microtubule curls like horns. A microtubule with GTP beta tubulin dimers at the end of its protofilaments is strongly favored to grow, but these microtubules also form highly curved protofilaments and will undergo rapid disassembly. The microtubule will switch between growing and shrinking phases (rescues and catastrophes), causing dynamic instability

67
Q

Microtubule pigment cell experiments

A

Studied using fish or frog melanophores. Melanophores are used to change skin color of fishes and frogs to help with camouflage and social interaction. The changes are mediated by neurotransmitters, and the movement of melanosomes are mediated by changes in intracellular cAMP and is dependent on microtubules. Studies have demonstrated that melanosome dispersion requires kinesin-2 and melanosome aggregation requires cytoplasmic dynein-dynactin. Dynactin might coordinate the activity of these 2 motors

68
Q

Melanophores

A

Skin cells that contain hundreds of melanin filled pigment granules called melanosomes. When melanophores have dispersed melanosomes, the skin is darker, when the melanosomes are aggregated at the cell center, the skin is paler.

69
Q

Microtubule-associated proteins

A

Associated with tubulin and help mediate the assembly, dynamics, and function of microtubules

70
Q

Tau

A

Helps to stabilize the cytoskeleton of neurons. It is a microtubule associated protein. In Alzheimer’s and Parkinson’s Disease, tau proteins aggregate inside the neurons and interfere with brain function

71
Q

Kinesin-13

A

Kinesins are motor proteins that mediate transport along microtubules. However, kinesin-13 is not motile. It destabilizes microtubule ends using ATP hydrolysis

72
Q

Stathmin

A

Proteins that play critically important roles in the regulation of the microtubule cytoskeleton. Stathmin regulates microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.

73
Q

Katanin

A

Microtubule associated protein that forms a 6 membered ring that severs a microtubule by pulling subunits out of the microtubule- results in its destabilization and severing. This causes more rapid depolymerization of the microtubule, or the microtubule is repaired with GTP tubulin to make a new growing end. It severs longer microtubules during neuronal development

74
Q

Microtubule polarity

A

Tubulin dimers in a protofilament are oriented the same way, so each filament has an alpha subunit on one end and a beta subunit at the other, demonstrating intrinsic polarity. Subunits are added at the beta end. All laterally associated protofilaments have the same polarity, so the microtubule has an overall polarity.

75
Q

How is the rate of axonal transport determined in vivo?

A

Through radiolabeling and gel electrophoresis. Radioactive amino acids are injected into the dorsal root ganglia of the sciatic nerve, where the cell bodies of the nerve are located. The amino acids are incorporated into new proteins, which travel down the axon to the synapse. The sciatic nerve is cut to see how far the proteins have been transported.

76
Q

DIC microscopy of vesicle transport

A

DIC microscopy demonstrates microtubule-based vesicle transport in vivo. An ATP buffer was added to the cytoplasm from a squid axon. DIC microscopy showed that two organelles attached to microtubules move in opposite directions along the same filament, pass each other, and then continue in their original direction. Showed that there must be ATP dependent motors that move cargo along microtubules in anterograde and retrograde directions

77
Q

Microtubule dyneins and kinesins

A

Dyneins in the cytoplasm mediate retrograde transport of organelles toward the negative end of the microtubule. Kinesins mediate anterograde transport toward the positive ends. Most organelles have one or more microtubule based motors

78
Q

Colchicine

A

Binds tubulin dimers so they can’t form microtubules. It is able to treat gout because it reduces the microtubule dynamics of white blood cells. Therefore, the white blood cells are unable to migrate and cause inflammation

79
Q

Taxol

A

Binds microtubules and stabilizes them against depolymerization. This inhibits mitosis by disrupting the mitotic spindle, so Taxol can be used to treat some cancers. It triggers dividing cells to commit to apoptosis, and it blocks Bcl-2.

80
Q

Kinesin-1 catalyzed vesicle transport

A

Kinesin-1 is located outside of the microtubule and is attached to receptors on the vesicle surface. It transports the vesicles from the negative to positive end of a microtubule. ATP is required for movement

81
Q

Structure and function of the kinesin superfamily

A

Some of these proteins are involved in the transport of organelles, mRNA, and chromosomes, as well as microtubule sliding and microtubule depolymerization. In these proteins, the conserved motor domain is fused to a variety of class-specific nonmotor domains

82
Q

How does kinesin-1 walk down the microtubule?

A

This process uses ATP. After kinesin has taken a step, the leading head is in the nucleotide-free state and tightly bound to the microtubule, while the trailing head is weakly bound to the microtubule. The leading head then binds ATP, which causes the region linking the kinesin heads to swing forward and dock in its associated head domain. This thrusts the trailing head forward. The new leading head finds a binding site to weakly bind. The leading head releases ATP, and binds tightly to the microtubule. The trailing head hydrolyzes ATP to make ADP and Pi, and releases Pi. The trailing head is converted to a weak binding state

83
Q

How is kinesin-1 regulated?

A

The head of Kinesin-1 folds back and interacts with the tail. This interaction inhibits the ATPase activity of kinesin-1. When the motor encounters an appropriate receptor, it unfolds and transports the cargo toward the positive end of the microtubule.

84
Q

The power stroke of dynein

A

Dynein can’t mediate cargo transport by itself. It requires a large protein complex (dynactin) to link dynein to its cargo. Upon ATP binding, dynein dissociates from the microtubule and the linker becomes bent. The linker crosses between the second and third AAA ATPase repeats (pre-stroke). Interaction with the microtubule, hydrolysis of ATP, and release of Pi causes the linker to straighten. The straightening is the power stroke that moves the cargo toward the negative end of the microtubule.

85
Q

Kartagener’s Syndrome

A

Ciliary dyskinesia, a defect in the dynein arms in cilia. It causes thick mucus that blocks the respiratory tract

Cell Biology (12 decks)

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