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Essential Cell Biology 5th edition

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600 CHAPTER 17 Cytoskeleton

Figure 17–37 Myosin-I is the simplest

myosin. (A) Myosin-I has a single globular

head that attaches to an actin filament and

a tail that attaches to another molecule or

organelle in the cell. (B) This arrangement

allows the head domain to move a vesicle

relative to an actin filament, which in this

case is anchored to the plasma membrane.

(C) Myosin-I can also bind to an actin

filament in the cell cortex, ultimately pulling

the plasma membrane into a new shape.

Note that the head group always walks

toward the plus end of the actin filament.

(A)

(B)

myosin-I

plus end

70 nm

head

domain

plasma

membrane

tail

myosin-l

vesicle

minus end

(C)

minus end

plus end

myosin-l

plasma membrane

MUSCLE CONTRACTION

Muscle contraction ECB5 is the E17.36/17.37

best understood of animal cell movements. In

vertebrates, running, walking, swimming, and flying all depend on the

ability of skeletal muscle to contract strongly and move various bones.

Involuntary movements such as heart pumping and gut peristalsis

depend on cardiac muscle and smooth muscle, respectively, which are

formed from muscle cells that differ in structure from skeletal muscle but

use actin and myosin in a similar way to contract. Much of our understanding

of the mechanisms of cell movement originated from studies of

muscle cell contraction. In this section, we discuss how actin and myosin

interact to produce this contraction.

Muscle Contraction Depends on Interacting Filaments

of Actin and Myosin

Muscle myosin belongs to the myosin-II subfamily of myosins. These

proteins are dimers, with two globular ATPase heads at one end and a

single coiled-coil tail at the other (Figure 17–38A). Clusters of myosin-II

molecules bind to each other through their coiled-coil tails, forming a

bipolar myosin filament from which the heads project (Figure 17–38B).

Figure 17–38 Myosin-II molecules

can associate with one another

to form myosin filaments. (A) A

molecule of myosin-II contains two

identical heavy chains, each with

a globular head and an extended

tail. (It also contains two light chains

bound to each head, but these are

not shown.) The tails of the two heavy

chains form a single coiled-coil tail.

(B) The coiled-coil tails of myosin-II

molecules associate with one another

to form a bipolar myosin filament in

which the heads project outward from

the middle in opposite directions.

The bare region in the middle of the

filament consists of tails only.

(A)

(B)

myosin-II molecule

head

150 nm

myosin-II filament

tail

bare region

(myosin tails only)

1 µm

myosin heads

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