CHAPTER

5
Cellular Movement
and Muscles

PowerPoint® Lecture Slides prepared by

Stephen Gehnrich, Salisbury University

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 Cytoskeleton and Motor Proteins

 All physiological processes depend on movement

 Intracellular transport
 Changes in cell shape
 Cell motility
 Animal locomotion

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 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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 Use of Cytoskeleton for Movement

 Cytoskeleton elements
 Microtubules
 Microfilaments
 Three ways to use the
cytoskeleton for
movement
 Cytoskeleton “road”
and motor protein
carriers
 To reorganize the
cytoskeletal network
 Motor proteins pull on
the cytoskeletal “rope”
Figure 5.1
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 Cytoskeleton and Motor Protein Diversity

 Structural and functional diversity

 Multiple isoforms of cytoskeletal and motor proteins
 Various ways of organizing cytoskeletal elements
 Alteration of cytoskeletal and motor protein function

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 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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 Microtubules

Figure 5.2
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 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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 Movement of Pigment Granules

Figure 5.3
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 Microtubules: Composition and Formation

 Microtubules are polymers of the protein tubulin

 Tubulin is a dimer of a-tubulin and b-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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 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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 Microtubule Assembly

Figure 5.4
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 Microtubule Growth and Shrinkage

 Factors affecting growth/shrinkage are

 Local concentrations of tubulin
 High [tubulin] promotes growth
 Dynamic instability
 GTP hydrolysis on b-tubulin causes disassembly
 Microtubule-associated proteins (MAPs)
 Temperature
 Low temperature causes disassembly
 Chemicals that disrupt the dynamics
 For example, plant poisons such as taxol and colchicine

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 Microtubule Dynamics

Figure 5.5
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 Regulation by MAPs

Figure 5.6
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 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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 Vesicle Traffic in a Neuron

Figure 5.7
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 Cilia and Flagella

 Cilia
 Numerous, wavelike motion
 Flagella
 Single or in pairs, whiplike movement
 Composed of microtubules arranged into axoneme
 Bundle of parallel microtubules
 Nine pairs of microtubules around a central pair
 “Nine-plus-two”
 Asymmetric activation of dynein causes movement

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 Cilia and Flagella

Figure 5.8
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 Microtubules and Physiology

Table 5.1
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 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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 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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 Microfilament Structure and Growth

Figure 5.9
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 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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 Microfilament (Actin) Arrangement

Figure 5.10
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 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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 Actin Polymerization and Fertilization

Figure 5.11
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 Myosin

 Most actin-based movements involve the motor

protein myosin
 Sliding filament model
 Myosin is an ATPase
 Converts energy from ATP to mechanical energy
 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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 Myosin

Figure 5.12
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 Sliding Filament Model

 Analogous to pulling yourself along a rope

 Actin – the rope
 Myosin – your arm
 Alternating cycle of grasp, pull, and release
 Your hand grasps the rope
 Your muscle contracts to pull rope
 Your hand releases, extends, and grabs further along
the rope

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 Sliding Filament Model

 Two processes
 Chemical reaction
 Myosin binds to actin (cross-bridge)
 Structural change
 Myosin bends (power stroke)
 Cross-bridge cycle
 Formation of cross-bridge, power stroke, release, and
extension
 Need ATP to release and reattach to actin
 Absence of ATP causes rigor mortis
 Myosin cannot release actin

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 Sliding Filament Model

Figure 5.13
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 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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 Myosin Activity

Figure 5.14
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 Actin and Myosin Function

Table 5.2
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 Muscle Cells (Myocytes)

 Myocytes (muscle cells)

 Contractile cell unique to animals
 Contractile elements within myocytes
 Thick filaments
 Polymers of myosin
 ~300 myosin II hexamers
 Thin filaments
 Polymers of a-actin
 Ends capped by tropomodulin and CapZ to stabilize
 Proteins troponin and tropomyosin on outer surface

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 Thick and Thin Filaments

Figure 5.15
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 Muscle Cells

 Two main types of muscle cells are based on the

arrangement of actin and myosin
 Striated (striped appearance)
 Skeletal and cardiac muscle
 Actin and myosin arranged in parallel
 Smooth (do not appear striped)
 Actin and myosin are not arranged in any particular way

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 Striated and Smooth Muscle

Figure 5.16
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 Striated Muscle Types

Table 5.3
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 Striated Muscle Cell Structure

 Thick and thin filaments arranged into sarcomeres

 Repeated in parallel and in series
 Side-by-side across myocyte
 Causes striated appearance
 End-to-end along myocyte

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 Sarcomeres

 Structural features of sarcomeres

 Z-disk
 Forms border of each sarcomere
 Thin filaments are attached to the Z-disk and extend from
it towards the middle of the sarcomere
 A-band (anisotropic band)
 Middle region of sarcomere occupied by thick filaments
 I-band (isotropic band)
 Located on either side of Z-disk
 Occupied by thin filament

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 Sarcomeres

 Thin and thick filaments overlap in two regions of

each sarcomere
 Each thick filament is surrounded by six thin
filaments
 Three-dimensional organization of thin and thick
filaments is maintained by other proteins
 Nebulin
 Along length of thin filament
 Titin
 Keeps thick filament centered in sarcomere
 Attaches thick filament to Z-disk

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 Sarcomeres

Figure 5.17
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 Three-Dimensional Structure of Sarcomere

Figure 5.18
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 Muscle Actinomyosin Activity is Unique

 Myosin II cannot drift away from actin

 Structure of sarcomere
 Duty cycle of myosin II is 0.05 (not 0.5)
 Each head is attached for a short time
 Does not impede other myosins from pulling the thin
filament
 Unitary displacement is short
 Small amount of filament sliding with each movement
of the myosin head

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 Contractile Force

 Contractile force depends on overlap of thick and

thin filaments
 More overlap allows for more force
 Amount of overlap depends on sarcomere length as
measured by distance between Z-disks
 Maximal force occurs at optimal length
 Decreased force is generated at shorter or longer
lengths

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 Length–Force Relationship

Figure 5.19
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 Myofibril

 In muscle cells, sarcomeres are arranged into

myofibrils
 Single, linear continuous stretch of interconnected
sarcomeres (i.e., in series)
 Extends the length of the muscle cell
 Have parallel arrangement in the cell
 More myofibrils in parallel can generate more force

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 Myofibrils in Muscle Cells

Figure 5.20
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 Regulation of Contraction

Excitation-contraction coupling (EC coupling)

 Depolarization of the muscle plasma membrane
(sarcolemma)
 Elevation of intracellular Ca2+
 Contraction
 Sliding filaments

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 Ca2+ Allows Myosin to Bind to Actin

 At rest, cytoplasmic [Ca2+] is low

 Troponin-tropomyosin cover myosin binding sites on
actin
 As cytoplasmic [Ca2+] increases
 Ca2+ binds to TnC (calcium binding site on troponin)
 Troponin-tropomyosin moves, exposing myosin-
binding site on actin
 Myosin binds to actin and cross-bridge cycle begins
 Cycles continue as long as Ca2+ is present
 Cell relaxes when the sarcolemma repolarizes and
intracellular Ca2+ returns to resting levels

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 Troponin and Tropomyosin

Figure 5.21
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 Regulation of Contraction by Ca2+

Figure 5.22
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 Ionic Events in Muscle Contraction

Figure 5.23
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 Troponin–Tropomyosin Isoforms

 Properties of isoforms affect contraction

 For example, fTnC has a higher affinity for Ca2+ than
s/cTnC
 Muscle cells with the fTnC isoform respond to smaller
increases in cytoplasmic [Ca2+]
 Isoforms differ in the affect of temperature and pH

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 Myosin Isoforms

 Properties of isoforms affect contraction

 Multiple isoforms of myosin II in muscle
 Isoforms can change over time

Table 5.4
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 Excitation of Vertebrate Striated Muscle

 Skeletal muscle and cardiac muscle differ in

mechanism of excitation and EC coupling
 Differences include
 Initial cause of depolarization
 Time course of the change in membrane potential
(action potential)
 Propagation of the action potential along the
sarcolemma
 Cellular origins of Ca2+

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 Action Potentials

 APs along sarcolemma signal contraction

 Na+ enters cell when Na+ channels open
 Depolarization
 Voltage-gated Ca2+ channel open
 Increase in cytoplasmic [Ca2+]
 Na+ channels close
 K+ leave cell when K+ channels open
 Repolarization
 Reestablishment of ion gradients by Na+/K+ ATPase
and Ca2+ ATPase

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 Time Course of Depolarization

Figure 5.24
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 Initial Cause of Depolarization

 Myogenic (“beginning in the muscle”)

 Spontaneous
 For example, vertebrate heart
 Pacemaker cells
 Cells that depolarize fastest
 Unstable resting membrane potential
 Neurogenic (“beginning in the nerve”)
 Excited by neurotransmitters from motor nerves
 For example, vertebrate skeletal muscle
 Can have multiple (tonic) or single (twitch)
innervation sites

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 Neurogenic Muscle

Figure 5.25
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 T-Tubules and Sarcoplasmic Reticulum

 Transverse tubules (T-tubules)

 Invaginations of sarcolemma
 Enhance penetration of action potential into myocyte
 More developed in larger, faster twitching muscles
 Less developed in cardiac muscle
 Sarcoplasmic reticulum (SR)
 Stores Ca2+ bound to protein sequestrin
 Terminal cisternae increase storage
 T-tubules and terminal cisternae are adjacent to one
another

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 T-Tubules and SR

Figure 5.28
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 Ca2+ Channels and Transporters

 Channels allow Ca2+ to enter cytoplasm

 Ca2+ channels in cell membrane
 Dihydropyridine receptor (DHPR)
 Ca2+ channels in the SR membrane
 Ryanodine receptor (RyR)
 Transporters remove Ca2+ from cytoplasm
 Ca2+ transporters in cell membrane
 Ca2+ ATPase
 Na+/Ca2+ exchanger (NaCaX)
 Ca2+ transporters in SR membrane
 Ca2+ ATPase (SERCA)

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 Ca2+ Channels and Transporters

Figure 5.27
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 Induction of Ca2+ Release From SR

 AP along sarcolemma conducted down T-tubules

 Depolarization opens DHPR
 Ca2+ enters cell from extracellular fluid
 In heart,  [Ca2+] causes RyR to open, allowing release of
Ca2+ from SR
 “Ca2+ induced Ca2+ release”
 In skeletal muscle, change in DHPR shape causes RyR to
open, allowing release of Ca2+ from SR
 “Depolarization induced Ca2+ release”

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 Ca2+ Induced Ca2+ Release

Figure 5.29
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 Depolarization Induced Ca2+ Release

Figure 5.30
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 Relaxation

 Repolarization of sarcolemma
 Remove Ca2+ from cytoplasm
 Ca2+ ATPase in sarcolemma and SR
 Na+/Ca2+ exchanger (NaCaX) in sarcolemma
 Parvalbumin
 Cytosolic Ca2+ binding protein buffers Ca2+
 Ca2+ dissociates from troponin
 Tropomyosin blocks myosin binding sites
 Myosin can no longer bind to actin

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 Relaxation

Figure 5.27
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 Summary of Striated Muscles

Table 5.5
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 Smooth Muscle

 Slow, prolonged contractions

 Often found in the wall of “tubes” in the body
 Blood vessels, intestine, airway, etc.

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 Smooth Muscle

 Key differences from skeletal muscle

 No sarcomeres (no striations)
 Thick and thin filaments are scattered in the cell
 Attached to cell membrane at adhesion plaques
 No T-tubules and minimal SR
 Often connected by gap junctions
 Function as a single unit
 Contract in all dimensions
 Different mechanism of EC coupling

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 Smooth Muscle

Figure 5.31
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 Control of Smooth Muscle Contraction

 Regulated by nerves, hormones, and physical

conditions (e.g., stretch)
 At rest, the protein caldesmon is bound to actin and
blocks myosin binding
 Smooth muscle does not have troponin
 Stimulation of cell increases intracellular Ca2+
 Ca2+ binds to calmodulin
 Calmodulin binds caldesmon and removes it from actin
 Cross-bridges form and contraction occurs
 Calmodulin also causes phosphorylation of myosin
 Increase in myosin ATPase activity

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 Control of Smooth Muscle Contraction

Figure 5.32
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 Diversity of Muscle Fibers

 Different protein isoforms affect EC coupling

 Ion channels
 Ion pumps
 Ca2+-binding proteins
 Speed of myosin ATPase
 Variation in other properties of muscle cells
 Myoglobin content
 Number of mitochondria
 Skeletal muscle cells can be classified as “fast,”
“slow,” “white,” “red,” “oxidative,” “glycolytic”

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 Changing Fiber Types

 Developmental (from embryo to adult)

 Increased proportion of fast muscle isoforms
 Physiological response
 For example, exercise
 Can change both cardiac and skeletal muscle

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 Changing Fiber Types

 Changes due to hormonal and nonhormonal

mechanisms
 For example, thyroid hormones repress expression of
b-myosin II gene and induce a-myosin II gene
 a-myosin II exhibits the fastest actino-myosin ATPase
rates
 For example, direct stimulation of cell can alter gene
expression

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 Nonhormonal Mechanisms

Figure 5.33
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 Trans-Differentiation of Muscle Cells

 Trans-differentiation
 Cells used for novel functions
 For example, heater organs of billfish eye
 Specialized muscle cells
 Few myofibrils (little actin and myosin)
 Abundant SR and mitochondria
 Futile cycle of Ca2+ in and out of the SR
 High rate of ATP synthesis and consumption
 Electric organs

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 Heater Organ

Figure 5.34
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 Invertebrate Muscles

 Variation in
contraction force due
to graded excitatory
postsynaptic potentials
(EPSP)
 Innervation by
multiple neurons
 EPSPs can summate
to give stronger
contraction
 Some nerve signals
can be inhibitory
Figure 5.35
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 Asynchronous Insect Flight Muscles

Wing beats: 250–1000 Hz

 Fastest vertebrate contraction ≈ 100 Hz (toadfish
sonic muscle)

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 Asynchronous Insect Flight Muscles

Asynchronous muscle contractions

 Contraction is not synchronized to nerve stimulation
 Stretch-activation
 Sensitivity of the myofibril to Ca2+ changes during
contraction/relaxation cycle
 Intracellular [Ca2+] remains high
 Contracted muscle is Ca2+ insensitive
 Muscle relaxes
 Stretched muscle is Ca2+ sensitive
 Muscle contracts

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 Asynchronous Insect Flight Muscles

Figure 5.36
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 Mollusc (Bivalve) Catch Muscle

 Muscle that holds shell closed

 Capable of long duration contractions with little
energy consumption
 Protein twitchin may stablilize actin-myosin cross-
bridges
 Cross-bridges do not continue to cycle
 Phosphorylation/dephophorylation of twitchin regulates
its function

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 Mollusc (Bivalve) Catch Muscle

Figure 5.37
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