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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings PowerPoint ® Lecture Slides prepared by Stephen Gehnrich, Salisbury University 5 C H A P T E R Cellular Movement
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Sponges (phylum Porifera) Cnidarians MedusaHydra Ctenophores Sea walnut Sea gooseberries
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Flatworms Nematodes Annelids Annelids – Internal structure
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Internal structure of a crayfish (lateral view).
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Cytoskeleton and Motor Proteins All physiological processes depend on movement Intracellular transport Changes in cell shape Cell motility Animal locomotion
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Cytoskeleton and Motor Proteins All movement is due to the same cellular “machinery” Cytoskeleton Protein-based intracellular network Motor proteins Enzymes that use energy from ATP to move
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Use of Cytoskeleton for Movement Cytoskeleton elements Microtubules Microfilaments
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Cytoskeleton “road” and motor protein carriers
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Reorganizing the cytoskeletal network A macrophage of a mouse stretching its arms to engulf two particles, possibly pathogens
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Motor proteins pull on the cytoskeletal “rope”
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Cytoskeleton and Motor Protein Diversity Structural and functional diversity Multiple isoforms Various ways of organizing Alteration of function
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Microtubules Are tubelike polymers of the protein tubulin Similar protein in diverse animal groups Multiple isoforms Are anchored at both ends Microtubule-organization center (MTOC) (–) near the nucleus Attached to integral proteins (+) in the plasma membrane
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Function of Microtubules Motor proteins can transport subcellular components along microtubules Motor proteins kinesin and dynein For example, rapid change in skin color
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Microtubules: Composition and Formation Microtubules are polymers of the protein tubulin Tubulin is a dimer of -tubulin and -tubulin Tubulin forms spontaneously For example, does not require an enzyme Polarity The two ends of the microtubule are different Minus (–) end Plus (+) end
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Microtubule Assembly Activation of tubulin monomers by GTP Monomers join to form tubulin dimer Dimers form a single-stranded protofilament Many protofilaments form a sheet Sheet rolls up to form a tubule Dimers can be added or removed from the ends of the tubule Asymmetrical growth Growth is faster at + end Cell regulates rates of growth and shrinkage
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Microtubule Growth and Shrinkage Growth / Shrinkage Local [tubulin] Dynamic instability MAPs Temperature Chemicals (Taxol, Colchicine) GTP hydrolysis on b-tubulin STOPsKatanin
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Microtubule Dynamics Figure 5.5
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Regulation by MAPs Figure 5.6
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Movement Along Microtubules Motor proteins move along microtubules Direction is determined by polarity and the type of motor protein Kinesin move in (+) direction Dynein moves in (–) direction Movement is fueled by hydrolysis of ATP Rate of movement is determined by the ATPase domain of motor protein and regulatory proteins Dynein is larger than kinesin and moves five times faster
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Vesicle Traffic in a Neuron Figure 5.7
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Cilia and Flagella Cilia numerous, wavelike motion. Flagella single or in pairs, whiplike movement.
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Microtubules and Physiology Table 5.1
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Microfilaments Polymers composed of the protein actin Found in all eukaryotic cells Often use the motor protein myosin Movement arises from Actin polymerization Sliding filaments using myosin More common than movement by polymerization
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Microfilament Structure and Growth G-actin monomers polymerize to form a polymer called F-actin Spontaneous growth 6–10 times faster at + end Treadmilling Assembly and disassembly occur simultaneously and overall length is constant Capping proteins Increase length by stabilizing – end and slowing disassembly
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Microfilament (Actin) Arrangement Arrangement of microfilaments in the cell Tangled neworks Microfilaments linked by filamin protein Bundles Cross-linked by fascin protein Networks and bundles of microfilaments are attached to cell membrane by dystrophin protein Maintain cell shape Can be used for movement
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Microfilament (Actin) Arrangement Figure 5.10
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Movement by Actin Polymerization Two types of amoeboid movement Filapodia are rodlike extensions of cell membrane Neural connections Microvilli of digestive epithelia Lamellapodia are sheetlike extensions of cell membrane Leukocytes Macrophages
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Actin Polymerization and Fertilization Figure 5.11
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Myosin Most actin-based movements involve the motor protein myosin Sliding filament model 17 classes of myosin (I– XVII) Multiple isoforms in each class All isoforms have a similar structure Head (ATPase activity) Tail (can bind to subcellular components) Neck (regulation of ATPase)
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Sliding Filament Model Myosin is an ATPase Converts energy from ATP to mechanical energy Sliding Filament Model Chemical reaction Myosin binds to actin (cross-bridge) Structural change Myosin bends (power stroke) Need ATP to release and reattach to actin Absence of ATP causes rigor mortis Myosin cannot release actin
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Sliding Filament Model - Cross-bridge cycle Figure 5.13 Extension Cross-bridge formation Power stroke Release
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Actino-Myosin Activity Two factors affect movement Unitary displacement Distance myosin steps during each cross-bridge cycle Depends on Myosin neck length Location of binding sites on actin Helical structure of actin Duty cycle Cross-bridge time/cross-bridge cycle time Typically ~0.5 Use of multiple myosin dimers to maintain contact
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Myosin Activity Figure 5.14
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Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Actin and Myosin Function Table 5.2
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