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Cell Biology 222

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2
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Lecture10

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3
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Cytoskeleton

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Created by Dr. Najah AL-Baqami

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5
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1/16/2025 1

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6
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➢ The cytoskeleton is a network of different protein fibers that provides many

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7
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functions: it maintains or changes the shape of the cell; it secures some organelles in

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8
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specific positions; it enables movement of cytoplasm and vesicles within the cell;

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9
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and it enables the cell to move in response to stimuli.

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10
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➢ There are three types of fibers within the cytoskeleton: microfilaments,

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11
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intermediate filaments, and microtubules. Some of the cytoskeletal fibers work in

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12
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conjunction with molecular motors which move along the fibers within the cell to

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13
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carry out a diverse set of functions. There are two main families of cytoskeletally-

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14
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associated molecular motors: dyneines and kinesins.

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15
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1/16/2025 2

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16
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➢ The cytoskeleton is a highly dynamic

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17
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structure that is continuously

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18
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reorganized as a cell changes shape,

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19
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divides, and responds to its

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20
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environment.

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21
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➢ The cytoskeleton controls the location

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22
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of the organelles that conduct these

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23
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specialized functions.

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24
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➢ It is also responsible for the segregation

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of chromosomes into daughter cells and
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the pinching apart of cells at cell
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division.
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➢ The cytoskeleton is built on a framework of three types
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of protein filaments: intermediate filaments,
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microtubules, and actin filaments.
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➢ Each type of filament has distinct mechanical
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properties and is formed from a different protein
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subunit
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➢ Intermediate filaments strengthen animal cells (epithelial cells )
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➢ Intermediate filaments are particularly prominent in the cytoplasm of cells that are
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subject to mechanical stress. They are present in large numbers, for example, along
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the length of nerve cell axons by stretching and distributing the effect of locally
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applied forces, keep cells and their membranes from breaking in response to
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mechanical shear.
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➢ The nuclear envelope is supported by a meshwork of Intermediate Filaments.
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Figure 17–7 Intermediate filaments support and strengthen the nuclear envelope.
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(A) Schematic cross section through the nuclear envelope. The intermediate filaments of
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the nuclear lamina line the inner face of the nuclear envelope and are thought to provide
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attachment sites for the DNA-containing chromatin. Page574-576
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Figure 17–4 Intermediate filaments
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strengthen animal cells. If a sheet of
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epithelial cells is stretched by external
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forces (due to the growth or
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movements of the surrounding tissues,
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for example), then the network of
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intermediate filaments and
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desmosomal junctions that extends
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through the sheet develops tension
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and limits the extent of stretching. If
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the junctions alone were present, then
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the same forces would cause a major
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deformation of the cells, even to the
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extent of causing their plasma
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membranes to rupture.
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➢ Microtubules usually grow out of an organizing structure (a centrosome,
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spindle pole, the basal body of a cilium).
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➢ The centrosome is the major microtubule-organizing center in animal
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cells.
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➢ Microtubules are maintained by a balance of assembly and disassembly.
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➢ Microtubules organize the interior of the cell.
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➢ Motor Proteins drive intracellular transport.
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➢ Organelles move along microtubules.
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Figure 17–8 Microtubules usually grow out of an organizing structure. Unlike
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intermediate filaments, microtubules (dark green) extend from an organizing center such as
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(A) a centrosome, (B) a spindle pole, or (C) the basal body of a cilium. Page 577-584
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Figure 17–10 Tubulin
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polymerizes from nucleation
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sites on a centrosome. (A)
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Schematic drawing showing that
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a centrosome consists of an
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amorphous matrix of protein
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containing the -tubulin rings
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that nucleate microtubule
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growth. In animal cells, the
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centrosome contains a pair of
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centrioles, each made up of a
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cylindrical array of short
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microtubules.
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(B) A centrosome with attached microtubules. The minus end of each microtubule is embedded in the centrosome, having
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grown from a nucleating ring, whereas the plus end of each microtubule is free in the cytoplasm. (C) A reconstructed image
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shows a dense thicket of microtubules emanating from the centrosome of a C. elegans cell. (C, from E.T. O’Toole et al., J. Cell Biol. 163:451–
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456, 2003. With permission from The Rockefeller University Press.)
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Figure 17–13 The selective
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stabilization of microtubules can
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polarize a cell. A newly formed
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microtubule will persist only if both
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its ends are protected from
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depolymerization. In cells, the minus
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ends of microtubules are generally
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protected by the organizing centers
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from which the filaments grow. The
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plus ends are initially free but can be
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stabilized by other proteins.
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Here, for example, a nonpolarized cell is depicted in (A) with new microtubules growing from and shrinking
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back to a centrosome in many directions randomly. Some of these microtubules happen by chance to encounter
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proteins (capping proteins) in a specific region of the cell cortex that can bind to and stabilize the free plus ends
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of microtubules (B). This selective stabilization will lead to a rapid reorientation of the microtubule arrays (C)
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and convert the cell to a strongly polarized form (D). Page 577-584
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Figure 17–14 Microtubules transport
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cargo along a nerve cell axon. In nerve
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cells, all the microtubules in the axon
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point in the same direction, with their
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plus ends toward the axon terminal. The
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oriented microtubules serve as tracks for
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the directional transport of materials
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synthesized in the cell body but required
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at the axon terminal (such as membrane
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proteins required for growth).
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For an axon passing from your spinal cord to a muscle in your shoulder, say, the journey takes about two days.
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In addition to this outward traffic of material (red circles) driven by one set of motor proteins, there is inward
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traffic (blue circles) in the reverse direction driven by another set of motor proteins. The inward traffic carries
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materials ingested by the tip of the axon or produced by the breakdown of proteins and other molecules back
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toward the cell body.
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Figure 17–16 Motor proteins move along
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microtubules using their globular heads. (A)
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Kinesins and cytoplasmic dyneins are
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microtubule motor proteins that generally move
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in opposite directions along a microtubule. Each
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of these proteins (drawn here to scale) is a dimer
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composed of two identical molecules. Each
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protein has two globular heads that interact with
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microtubules at one end and a single tail at the
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other. (B) Schematic diagram of a motor protein
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showing ATP-dependent “walking” along a
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filament.
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Figure 17–17 Different motor proteins transport cargo along microtubules. Most kinesins move toward the
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plus end of a microtubule, whereas dyneins move toward the minus end. Both types of microtubule motor
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proteins exist in many forms, each of which is thought to transport a different cargo. The tail of the motor
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protein determines what cargo the protein transports.
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➢ Actin filaments can grow by the addition of actin monomers at either end.
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➢ ATP hydrolysis decreases the stability of the actin polymer.
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➢ Forces generated in the actin-rich cortex move a cell forward.
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➢ Actin associates with myosin to Form contractile structures.
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Figure 17–28 Actin filaments allow eucaryotic cells to adopt a variety of shapes and perform a variety
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of functions. Various actin-containing structures are shown here in red: (A) microvilli; (B) contractile
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bundles in the cytoplasm; (C) sheetlike (lamellipodia) and fingerlike (filopodia) protrusions from the
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leading edge of a moving cell; (D) contractile ring during cell division. Page 590-597
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Figure 18–33 The contractile ring divides the cell in two. (A) Scanning electron
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micrograph of an animal cell in culture in the last stages of cytokinesis. (B) Schematic
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diagram of the midregion of a similar cell showing the contractile ring beneath the plasma
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membrane and the remains of the two sets of interpolar microtubules.
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Figure 17–30 ATP hydrolysis
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decreases the stability of the
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actin polymer. Actin monomers in
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the cytosol carry ATP, which is
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hydrolyzed to ADP soon after
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assembly into a growing filament.
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The ADP molecules remain
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trapped within the actin filament,
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unable to exchange with ATP until
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the actin monomer that carries
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them dissociates from the filament.
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Figure 17–32 Forces generated in the actin-rich
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cortex move a cell forward. In this proposed
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mechanism for cell movement, actin polymerization at
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the leading edge of the cell pushes the plasma membrane
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forward (protrusion) and forms new regions of actin
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cortex, shown here in red. New points of anchorage are
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made between the actin filaments and the surface on
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which the cell is crawling (attachment). Contraction at
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the rear of the cell then draws the body of the cell
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forward (traction). New anchorage points are established
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at the front, and old ones are released at the back as the
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cell crawls forward. The same cycle is repeated over and
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over again, moving the cell forward in a stepwise
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fashion.
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Figure 17–36 The short tail of a
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myosin-I molecule contains sites
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that bind to various components of
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the cell, including membranes. (A)
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Myosin-I has a single globular head
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and a tail that attaches to another
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molecule or organelle in the cell. This
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arrangement allows the head domain
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to move a vesicle relative to an actin
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filament (B), or an actin filament and
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the plasma membrane relative to each
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other (C). Note that the head group of
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the myosin always walks toward the
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plus end of the actin filament it
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contacts.
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