Chapter 11: Cytoskeleton Flashcards

1
Q

• Know the three types of cytoskeletal elements and be able to compare their structures

A
  1. micro tubules (tubule polymers): hollow tubes that have 13 columns of tubulin molecules.
  2. microfilament (actin filaments) 2 intertwined strands of actin, each polymer of actin subunits
  3. intermediate filaments: fibrous proteins supercoiled into thicker cables
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2
Q

• The general purpose of microtubules and the various functions they’re involved in

A

primarily responsible for organizing contents of the cell
- integral during mitosis by forming the mitotic spindle, provides force needed to segregate chromosomes into 2 daughter cells , critical for stable structures like cilia and flagella.

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3
Q

• How microtubules grow and where they originate from

A

• Microtubules grow from centrosome
• Sometimes called microtubule organizing center (MTOC) it’s involved in controlling location, # and orientation of microtubules
• centrioles are surrounded by matrix of proteins w/ hundreds of ring-shaped structures formed by γ-tubulin
(gamma ring)

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4
Q

• The structure of microtubules and what they’re made up of

A
  • Microtubules are made up of polymers =protofilaments
  • Protofilaments =made of dimers of alpha tubulin & beta tubulin
  • microtubule is hollow tube of 13 protofilaments aligned side by side (parallel)
  • The result is = hollow tube w/ polarity, w/ one end showing the α-tubulin (the minus end) & the other showing β-tubulin (the plus end)
  • Critical for role in directional movement w/i the cell
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5
Q

• The idea of dynamic instability and the detailed mechanism of polymerization and depolymerization of microtubules

A
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6
Q

• The function of microtubules in vesicle transport and the mechanism of how vesicles move along them

A
  • Motor proteins are what drives movement along microtubules
  • Vesicles that are trafficked from the ER/Golgi don’t just float randomly to the cell membrane or organelles
  • Each attaches to a specific microtubule and moves along it to the right organelle/location
  • Use energy from ATP hydrolysis to carry cargo along a microtubule in a single direction
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7
Q

• The structure of motor proteins

A
  • Kinesin moves toward the positive end of the microtubule (away from cell body/MTOC)
  • Dynein moves toward the negative end of the microtubule (toward cell body/MTOC)
  • Both form dimers that have 2 globular ATP-binding heads that bind the microtubule and a single tail that binds a specific cargo for transport
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8
Q

• The general structure of microfilaments and what processes they’re involved in

A
  • Microfilaments are also polymers but only single, globular protein called actin
  • Actin filaments carry out various functions in the cell by associating with other proteins
  • Depending on which proteins they interact with, they can form:
  • stiff/stable structures like microvilli (small intestine)
  • amoeboid cytoplasmic protrusions that facilitate crawling
  • contractile rings that split cells in two during cytokinesis
  • Polymerization will occur at either end of the microfilament, so if the cell wants an actin filament to grow in a certain direction, it must “cap” (block) one end
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9
Q

• The mechanism of treadmilling and how actin filaments grow/shrink

A
  • Free actin carries ATP & hydrolyzes it to ADP shortly after being added to the chain (just like tubulin & GTP)
  • If the amount of free actin is at an intermediate level, then treadmilling can occur where the filament shrinks at the minus end and grows at the plus end
  • When the rate of ATP hydrolysis at the plus end is slower than subunit addition = growth & polymerization
  • When the rate of ATP hydrolysis at the minus end is faster than subunit addition = depolymerization
  • Overall, the plus end grows and the minus end shrinks creating “treadmilling”
  • If actin concentration is really high in the cell, both ends will grow, but if its really low, both ends will shrink
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10
Q

• The purpose of thymosin and profilin

A
  • Thymosin binds monomers to prevent polymerization

* Profilin binds monomers and helps them associate to speed polymerization

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11
Q

• The structure of myosin and what proteins make up a sarcomere

A

dimers that have globular head connected to long alpha helix
• Myosin uses atp
• Sarcomere = myosin and actin
• Sarcomeres are repeating units- make up myofibrils

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12
Q

• The detailed powerstroke mechanism involved in muscle contraction

A
  • The myosin heads are locked onto the actin filament when bound to ADP; they push inward toward the midline of the sarcomere
  • Binding of ATP to the myosin head causes a conformational change that reduces its affinity for actin
  • Hydrolysis of ATP triggers the myosin head to pivot & change positions
  • the myosin head is still bound to ADP and Pi
  • Weak interactions with actin at this new site cause the myosin head to release Pi
  • This release causes the myosin head to tightly bind the actin
  • Release of ADP causes the powerstroke mechanism
  • Powerstroke = pivoting of the myosin head back into its original position causes the actin filament to move inward and muscle contraction to happen
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13
Q

• The role of tropomyosin and troponin and how Ca stimulates a muscle contraction

A

• Troponin = a calcium sensitive protein complex that interacts with tropomysosin
• Tropomyosin = rod shaped protein that binds to actin and covers myosin binding sites
• When Ca2+ binds troponin, it causes a conformational change in troponin which, in turn, changes the position of
tropomyosin
• This opens up the myosin binding site and allows for a muscle contraction

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14
Q

• The structure of intermediate filaments and the four different classes

A

• surround nucleus & extend into pm of cell where they anchor to pm at cell-cell junctions
• They be found w/i nuc where they support nuc mem. by forming nuclear lamina network
• Less dynamic than microtubules or actin filaments (don’t polymerize and depolymerize frequently)
1. keratin filaments
2. vimentum and vimentum containing filaments
3. neurofilaments
4. nuclear lamins

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15
Q

• The purpose of keratin and its function in multicellular organisms

A
  • Keratin filaments provide mechanical strength to these cells by anchoring to sites of cell-to-cell contact called desmosomes
  • This allows strong cables of these filaments to exist throughout the epithelium like that of our skin
  • As our skin stretches, these filaments distribute the stress and prevent our skin cells from rupturing
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16
Q

• The purpose of nuclear lamins and the function of plectin (& how its broken down and rebuilt during cell division)

A

nuclear lamins: form tough meshwork
• Provides strength to the nuclear envelope
• With each cell division, kinases phosphorylate the lamins causing the meshwork to deconstruct
• Dephosphorylation of the lamins after division cause the nuclear lamina to rebuild
• Plectin, an accessory protein, crosslinks the intermediate filaments to the desmosomes, microtubules and actin filaments within the cytoplasm and nuclear lamina in nucleus

17
Q

• The basis of different cytoskeletal element diseases

A
  • Epidermolysis bullosa simplex – mutations in keratin make epithelial tissues vulnerable to pressure causing cell rupturing and blistering of the skin
  • Mutations in neurofilament genes cause axons to become weaker leading to nervous system impairment, axon degeneration and muscle weakness (Lou Gehrig’s disease & ALS)
  • Mutations in nuclear lamins cause individuals to age prematurely (progeria)
  • Diseases where plectin is mutated include muscular dystrophy neurodegeneration due to disruption of intermediate filaments in muscle and disruption of neurofilaments in neurons