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Cytoskeleton Liu
UCI SOM Liu
| Question | Answer |
|---|---|
| Kinetics of f-actin polymerization | nucleation is slow, elongation is fast |
| Critical concentration | minimal G-actin concentration for actin polymerization |
| Barbed end characteristics | + end, lower critical conc., higher polymerization rate, polymerizes at steady state |
| Pointed end | - end, higher critical conc., slower polymerization rate, depolymerizes at steady state |
| Actin-monomer-binding proteins | thymosin and profilin |
| Thymosin | binds actin and inhibits f-actin polymerization |
| Profilin | promotes polymerization of actin |
| Listeria monocytogenes | intracellular parasite that uses profilin |
| Arp2 and Arp3 | form ARP complex; very similar structure to plus end of actin; catalyze polymerization; starts side chains |
| Actin severing and/or capping proteins | villin (from intestine) and gelsonin (from macrophages) |
| Platelet formation | Ca2+ activates gelsonin severs actin filaments which then grow rapidly into many long actin filaments |
| f-actin cross-linking proteins | spectrin (long), fimbrin (short), alpha actinin (medium), flimanin (for cross linking f-actin), dystrophin |
| microvilli components | f-actin, villin, fimbrin, mysoin-I, calmodulin |
| how does the actin-spectrin cytoskeleton network connect to the membrane in RBCs | ankyrin connects to band3 protein, band4.1 protein and adducin connect to glycophorin, an integral membrane protein |
| how does the cortical actin network connect to the membrane in platelets | actin-spectrin network linked to an anion transporter; second- actin-filamin gel achored to glycoprotein Ib-IX |
| duchenne’s muscular dystrophy | lack dystrophin, a spectrin related protein |
| all myosins have what | head, neck, and tail domains with distinct fxns |
| muscle type of myosin | II |
| myosin II makeup | 2 heavy chains and 4 light chains |
| z disc | where the actin filaments join in anti-parallel action (end of sarcomere) |
| 3 most notable actin/myosin structures | contractile ring, stress fibers, adhesion belt |
| myosin I | move vesicles around the cell and attach to the plasma membrane |
| myosin V | vesicular transport of secretory vesicles |
| microtubules are made of what | tubulin heterodimer (alpha and beta tubulin) |
| how many protofilaments in one microtubule | 13 |
| 4 places microtubules are found | cilia/flagella, cytoplasmic microtubules in interphase cells, mitotic spindle, centrioles/MTOC |
| cilia use what form of microtubule | axoneme |
| axoneme structure | 9 doublet microtubules and 2 single microtubules |
| ciliary dynein | move toward the minus end but because of linking proteins, the cilia just bend |
| basal body structure | nine sets of triplet microtubules; same structure as centriole |
| MTOC | microtubule organization center; stimulate polymerization; positive end is away from MTOC |
| Centrosome | single major MTOC |
| Centriole | a pair in the centrosome; same structure as basal bodies; L-shaped configuration; move to different poles during mitosis |
| Gamma-tubulin | base of centrosome; alpha and beta tubulin add on top |
| In a dividing cell, the MTOC is called | spindle pole |
| GTP cap | hydrolysis lags polymerization |
| 2 classes of microtubules | ones with a GTP cap are favored for growth, those without are favored for disassembly |
| if a microtubule loses its GTP cap, what happens | catastrophic depolymerization |
| kinesin | many types, moves to the plus end (away from MTOC)=anterograde |
| dynein | moves to minus end (to MTOC)=retrograde; mitosis |
| polar microtubule | cross linking microtubules in mitosis that don’t bind chromosomes |
| kinetochore MT | MT that grab chromosomes |
| the movement of chromosomes to the poles is known as | anaphase A |
| the poles are pushed and pulled apart in what phase | anaphase B |