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BI220 E1 L45

lecture 4&5 slides

QuestionAnswer
cytoskeleton complex fiber network. cell structure, facilitating motility, mediating intracellular transport of materials
dynamic instability constant assembly and disassembly - changes cell structure and function
intermediate filament protein examples keratin (cytoplasmic, epithelial cells). vimentin, desmin (cytoplasmic, connective tissue & muscles). neurofilaments, nestin (cytoplasmic, neurons). lamins (nuclei of animal cells).
plectins protein class - crosslink & connect all 3 main components of cytoskeleton
intermediate filaments function provide mechanical strength to cells, resist stretching forces, form scaffold structure in cells for anchoring cytoskeleton. NO MOTILITY
epidemolysis bullosa (EB) butterfly skin - connective tissue disorder causing blistering of the skin due to minimal touch
EB cause issues with anchoring between epidermis & dermis. often caused by mutations in keratin or plectin
nuclear lamina responsible for assembly & disassembly of nucleus during cell division. composed of lamins forming meshwork of the inner membrane
progeria (HGPS) premature aging due to point mutation in LMNA gene = failure to produce lamin A. cell division greatly limited --> premature aging --> death.
cell structures comprised of microtubules centrioles, centrosomes, mitotic spindle fibers, flagella, cilia
microtubules key roles intracellular trafficking, organelle positioning, cell locomotion (cilia, flagella), nuclear division, structural support
microtubules composed of? tubulin dimers (alpha & beta monomers)
plus end of microtubules exposed beta monomers (faster addition as tube grows)
minus end of microtubules exposed alpha monomers (slower addition as tube grows)
MTOC microtubule formation site
MTOC functions 1. organize microtubules for motility structures (flagella, cilia) 2. organize mitotic spindle during cell div
gamma tubulin rings nucleation sites for building new microtubules
MTOC structure centrosome. inside are 2 centrioles. made of 9 sets of microtubule triplets. surrounded by pericentriolar material (PCM).
PCM contains gamma-tubulin, pericentrin, ninein.
GTP guanosine triphosphate. energy source for polymerization of microtubules
capping proteins prevent changes to structure and length of microtubules. centrosome & MTOCs cap - end. membrane-associated proteins cap + end.
cell polarization capping microtubules on one end. creates distinct poles of the cell
microtubule motor proteins intracellular transport of substances
anterograde motion movement of substances AWAY from cell nucleus. typically involves motion toward + end of microtubules
retrograde motion movement of substances TOWARD cell nucleus. typically involves motion toward - end of microtubules
dyneins microtubule motor protein. - end of microtubule. retrograde
kinesins microtubule motor protein. + end of microtubule. anterograde
head portion of motor protein ATPase activity - utilizes ATP to facilitate motion via ATP hydrolysis & binds to microtubules
tail portion of motor protein binds specific cargo
motor protein cargo examples proteins, vesicles, organelles
how do motor proteins cause motion? proteins (i.e. dynein) apply forces on cross linked microtubules, causing bending & thus motion
microfilament-associated cell processes chemotaxis, phago/pinocytosis, microvilli, stress fiber formation, lamelli/filopodia, cleavage furrow / contractile ring
motor proteins that provide pulling forces within cell actin & myosin
treadmilling adding subunits at barbed end & losing subunits at pointed end --> no net change in length
ATP bound actin polymerizes at ____ end +
ATP hydrolyzed to ADP effect actin monomers become more fragile --> more likely dissociate from - end
amoeboid movement extending a portion of plasma membrane & forming contact & pulling cell forward
pseudopodia aspects lamellipodia (flattened extension) & filopodia (pointy extension)
myosin does ________ contractile forces for pulling
myosin bind to and "walk" along microfilaments toward + end of structures, consuming ATP. carries loads (i.e. vesicles) like dyneins and kinesins on microtubules. myosin i & ii are common in humans
sliding filament theory actin & myosin are responsible for forces generated. filaments slide against one another
myosin thick filament
actin thin filament. contains 2 types of bound proteins which are important in contraction
tropomyosin cable which covers myosin binding sites
troponin calcium binding molecule, causes change in tropomyosin position
rigor mortis cause lack of ATP - locking actin & myosin
Created by: knorrod
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