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UCI SOM Liu

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