Chapter 15

Beyond the Cell: Cell Adhesions,

Cell Junctions, and Extracellular
Structures
1
Many kinds of cells spend all their lives linked to neighboring cells;
the organization of cells into tissues that allows multicellular
organisms to adopt complex structures.

The adhesions animal cells make with one another; the junctions
that characterize these adhesions; how animal cells interact with
the extracellular matrix; the walls that surround plant cells; the
specialized structures that allow direct cell-to-cell communication
between plant cells.

2
 In a polarized epithelium, cells are connected together by cell-cell adhesions.
● The apical surfaces of these cells are very different from the basal surfaces,
which lie on top of an extracellular matrix known as a basal lamina基底板.
3
In a connective tissue, such as the dermis of the skin, loosely organized cells
are embedded in extracellular matrix fibers.

4
 Cell-cell junctions

Multicellular organisms have specific means of joining cells

in long-term associations to form tissues and organs.

Such associations usually involve specialized modifications

of the plasma membrane at the point where two cells come
together.

● These specialized structures are called cell-cell junctions.

● In animals, the three most common kinds of cell junctions
are adhesive junctions黏著連接, tight junctions緊密連接, and
gap junctions間隙連接.

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➢ Adhesive junctions link adjoining cells

Adhesive junctions link cells together into tissues, enabling the

cells to function as a unit.

All junctions in this category anchor the cytoskeleton to the cell

surface.

● The resulting interconnected cytoskeletal network helps

maintain tissue integrity and to withstand mechanical stress.

7
 Adhesive junctions rely on specialized adhesion proteins.

Many of these adhesion proteins are transmembrane proteins,

which means the extracellular portion of these proteins can
interact with the extracellular portion of similar proteins on the
surface of a neighboring cell.

● In some cases, cells interact with identical molecules on the surface

of the cell to which they adhere; such interactions are said to be
homophilic interactions.

● In other cases, a cell adhesion receptor on one cell interacts with a

different molecule on the surface of the cell to which it attaches;
such interactions are said to be heterophilic interactions.

8
 Many transmembrane adhesion proteins attach to the cytoskeleton
via linker proteins, which differ depending on the class of molecule
and its location within the cell.

Cells can dynamically assemble and disassemble adhesions in response

to a variety of events.

● Many adhesion proteins are continuously recycled: protein at the cell

surface is internalized by endocytosis, and new protein is deposited
at the surface via exocytosis.

● Adhesion proteins serve as key sites for assembly of signaling

complexes in cells and for dynamically assembling cytoskeletal
structures at sites of cell adhesion.

● Cell adhesion is coordinated with cell signaling, cell movement, cell

proliferation, and cell survival.
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 The two main kinds of cell-cell adhesive junctions are adherens
jnuctions and desmosomes胞橋體.

Despite structural and functional differences, these two

adhesive junctions both rely on:

● intracellular attachment proteins, which link the junction to the

appropriate cytoskeletal filaments on the inside of the plasma
membrane, and

● cadherins鈣黏蛋白, transmembrane proteins that protrude on the

outer surface of the membrane and bind cells to each other.

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 Adherens junctions

● Cadherin-mediated adhesive junctions that interact with actin

are called adherens junctions.

● At adherens junctions, the space between the adjacent

membranes is about 20-25 nm.

● Adherins junctions are especially prominent in epithelial cells.

✓ They are found in many epithelial cell types, such as cells lining
the intestine, kidney cells, and epidermal cells.

✓ In these cells adherens junctions form a continuous belt that

encircles the cell near the apical end of the lateral membrane.

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● Adherens junctions rely on cadherins and their associated
proteins to confer adhesion between cells.

● Cadherins are characterized by :

✓ a series of structurally similar domains (or repeats) in their
extracellular domain that vary from protein to protein;

✓ a transmembrane domain;

✓ Widely varying cytosolic ends.

13
● The best-characterized cadherin, E-cadherin (E is for “epithelial”.
✓ E-cadherin associate as pairs (homodimers) in the plasma membrane and
interact with homodimers in the neighboring cell through their extracellular
domains; Ca2+ binds to and stabilizes the extracellular region of cadherins.
✓ Their cytosolic tail binds to the linker protein b-catenin; b-catenin in turn
binds a-catenin, which recruits actin to the junction.
14
● Vertebrates have many different types of cadherins, and different
cadherins are found on the surfaces of cells in specific tissues; the
amount and types of cadherin molecules on cell surfaces help to
separate cells into specific tissues.

15
● Cadherins have especially important roles during embryonic development.
✓ For example, when frog embryos are depleted of mRNA for the main
type of cadherin found in the early embryo, they lose their normal
organization.
● Cancer cells often stop expressing cadherins; these cells spread to other
parts of the body by a process known as metastasis.

16
 Desmosomes

● Desmosomes are button-like points of strong adhesion between

adjacent cells in a tissue.

● Desmosomes give the tissue structural integrity, enabling cells

to function as a unit and to resist stress.

● Desmosomes are found in many tissues but are especially

abundant in cells that experience mechanical stress, such as
skin, heart muscle, and the uterus.

● Like adherens junctions, desmosomes rely on cadherins.

✓ The cadherins in desmosomes are called desmocollins橋粒芯膠蛋白
and desmogleins橋粒芯糖蛋白.

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● The plasma membranes of the two adjacent cells are aligned
in parallel, separated by a space of about 25-35 nm.

✓ The extracellular space between the two membranes is called

the desmosome core.

✓ The desmosome core between the two membranes is filled

with cadherins (desmocollins and desmogleins).

✓ The plaque on the cytosolic side of the membrane contains

desmoplakins橋粒斑蛋白, which bind intermediate filaments,
plakoglobin斑珠蛋白, and plakophilin親斑蛋白.

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 Transient cell-cell adhesions are important for many cellular
events

In addition to cadherins, there are many other molecules that

are involved in cell-cell adhesion and cell recognition.

Lectins凝集素: carbohydrate-binding proteins, secreted by many

animal and plant cells.

● Lectins promote cell-cell adhesion by binding to a specific sugar

or sequence of sugars exposed at the outer cell surface.

● Because lectins usually have more than one carbohydrate-binding

site, they can bind to carbohydrate groups on two different cells,
thereby linking the cells together.

21
 Cell adhesion molecules細胞黏著分子(CAMs)

● CAMs are members of the immunoglobulin superfamily (IgSF).

● They contain domains, characterized by well-organized loops,
that are similar to those in the immunoglobulin subunits that
constitute antibodies.

● CAMs on one cell can interact homophilically with CAMs on an

adjacent cell or can interact heterophilically with their ligands.

22
 Selectins and leukocyte adhesion

● Cell adhesion also plays an important role during the interactions

of leukocytes with endothelial cells lining blood vessels.

● Cell surface glycoproteins, selectins, mediate these interactions.

● A different selectin is expressed by each cell type; L-selectin on
leukocytes, E-selectin on the endothelial cells of blood vessels,
and P-selectin on platelets and endothelial cells.

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➢ Tight junctions prevent the movement of molecules across
cell layers

A key feature of epithelial tissues is that they form barriers

between the internal cells of the body and the outside world.

For example, intestinal cells must seal off the fluids that pass
through the digestive tract from the internal fluids of the
body.

Epithelial cells need specialized structures that serve to seal

them tightly together.

Tight junctions serve this function

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 Role of tight junctions in sealing epithelia

The tight junctions between adjacent form a continuous band

around the apical ends of the lateral surfaces of each cell.

● These bands together form a formidable barrier that only lets

selected ions and molecules pass between cells, so that many
molecules must cross the cell layer by passing through the cells
themselves via specialized transporter proteins.

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 Tight junctions are especially prominent in:

● intestinal epithelial cells;

● they are also abundant in the ducts and cavities of glands that
connect with the digestive tract, such as liver and pancreas;

● the urinary bladder, where they ensure that the urine stored in
the bladder does not seep out between cells;

● between the endothelial cells lining the blood vessels of the

brain, thereby creating the blood-brain barrier.

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 Tight junctions are connected along sharply defined ridges.

● Each junction appears as a series of ridges that form an

interconnected network extending across the junction.

● The membranes are not actually in close contact over broad

areas; they are connected at periodic points of contact
along sharply defined ridges.

● Each ridge consists of a continuous row of tightly packed

transmembrane proteins about 3-4 nm in diameter.

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 Tight junctions contain several major transmembrane proteins.

These include a transmembrane protein known as occludin封閉蛋白

and immunoglobulin superfamily proteins known as junctional
adhesion molecules連接黏著分子(JAMs); in addition, tight junctions
contain claudins.

● Claudins have four membrane-spanning domains;

● Claudins in the plasma membrane of adjacent cells are thought to
interlock to form a tight seal.

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● Charged amino acids in the large extracellular loop of claudins
form ion-selective pores that allow passage of specific ions
through the epithelium.

✓ Because in this case ions move between cells, rather than through
them, this type of transport is termed paracellular transport.

✓ Different claudins are expressed in different epithelial tissues

and are thought to confer on these tissues different permeability
properties.

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Charged amino acids (red)
34
 Role of tight junctions in blocking lateral movement of membrane
proteins

Tight junctions act like “gates”, preventing the movement of fluids,

ions, and molecules across a sheet of cells.

In addition, tight junctions like “fences”, blocking the lateral

movement of lipids and proteins within cell membranes.

● Lipid movement is blocked in the outer monolayer only.

● The movement of integral membrane proteins is also blocked;
different kinds of integral membrane proteins can be maintained in
the region of plasma membrane surrounded by a tight junction belt.

35
➢ Gap junctions allow direct electrical and chemical communication
between cells

A gap junction is a region where the plasma membranes of two cells

are aligned and brought into intimate contact, with a gap of only 2-3
nm in between, spanned by small molecular “pipelines”; through which
ions and small molecules can pass.

At a gap junction, the two plasma membranes from adjacent cells

are joined by tightly packed, hollow cylinders called connexons連接子.

A single gap junction may consist of just a few or as many as

thousands of clustered connexons.

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● In vertebrates, each connexon is a circular assembly of six
subunits of the protein connexin連接蛋白.

● Invertebrates produce proteins called innexins that appear to

serve the same function.

● More than a dozen types of connexins are found in different

tissues, but each one functions similarly in forming connexons.

● The assembly spans the membrane and protrudes into the space
between the two cells.

37
 Each connexon has a diameter of about 7 nm and a hollow center that
forms a very thin hydrophilic channel through the membrane.

● The channel is about 3 nm in diameter at its narrowest point; just

large enough to allow the passage of ions and small molecules but too
small to allow proteins, nucleic acids, and organelles through.

● Gap junctions allow the passage of solutes with molecular weights up

to about 1200, such as single sugars, amino acids, and nucleotides.

● Gap junctions are especially abundant in tissues such as muscle and

nerve, where extremely rapid communication between cells is
required.

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The extracellular matrix of animal cells
Tissues are not simply composed of cells; cells interact with
extracellular materials that are crucial for tissue structure
and function.
In animal cells, this extracellular matrix (ECM) takes on a
remarkable variety of forms in different tissues.

40
 Despite the diversity of function, the ECM of animal cells almost
always consists of the same three classes of molecules:

1. Structural proteins such as collagens膠原蛋白 and elastins彈力蛋白,

which give the ECM its strength and flexibility;

2. Protein-polysaccharide complexes called proteoglycans蛋白聚糖

that provide the matrix in which the structural molecules are
embedded;

3. Adhesive glycoproteins such as fibronectins纖維結合素 and

laminins層黏蛋白, which allow cells to attach to the ECM.

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➢ Collagens are responsible for the strength of the extracellular
matrix

The most abundant component of the ECM in animals is a large

family of closely related proteins celled collagens.

Collagens form fibers with high tensile strength and account for
much of the strength of the ECM.

● Collagen is the most abundant protein in vertebrates, accounting

for as much as 25-30% of total body protein.

● Collagen is secreted by several types of cells in connective tissues,

including fibroblasts.

● Vitamin C is an essential cofactor輔因子 for collagen synthesis.

43
Two defining characteristics are shared by all collagens:
their occurrence as a rigid triple helix of three intertwined
polypeptide chains and their unusual amino acid composition.

Specifically, collagens are high in both the common amino

acid glycine and the unusual amino acids hydroxylysine and
hydroxyproline, which rarely occur in other proteins.

The high glycine content makes the triple helix possible

because the spacing of the glycine residues places them in
the axis of the helix, and glycine is the only amino acid small
enough to fit in the interior of a triple helix.

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● Collagen fibers can be seen in bundles
throughout the extracellular matrix.

小纖維
● Each collagen fiber is composed
of numerous fibrils.

● A fibril is made up of many

collagen molecules.

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● Collagen molecules: consisting of three polypeptides called
a-chains that are twisted together into a rigid, right-
handed triple helix.

● Collagen molecules are about 270 nm in length and 1.5 nm

in diameter and are aligned both laterally and end to end
within the fibrils.

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A precursor called procollagen forms many types of tissue-specific
collagens

47
 In the ER lumen, three a chains assemble to form a triple helix
called procollagen.

● At both ends of the triple-helical structure, short nonhelical

sequences of amino acids prevent the formation of collagen fibrils,
as long as the procollagen remains within the cell.

● Once procollagen is secreted from the cell into the intercellular

space, it is converted to collagen by procollagen peptidase, an
enzyme that removes the extra amino acids from both the N-and
C-terminal ends.

● The resulting collagen molecules spontaneously associate to form

mature collagen fibrils, which then assemble into fibers.

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 The stability of the collagen fibril is reinforced by hydrogen bonds
that involve the hydroxyl groups of hydroxyproline and hydroxylysine
residues in the a chains.

● These hydrogen bonds form crosslinks both within and between the
individual collagen molecules in a fibril.

● Vertebrates have about 25 kinds of a chains, each encoded by its own

gene and having its own unique amino acid sequence.

● These different a chains combine in various ways to form at least 15

types of collagen molecules.

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➢ Elastins impart elasticity and flexibility to the extracellular matrix

Elasticity is provided by stretchable elastic fibers present in the

ECM.

The principle constituent of elastic fibers is a family of ECM

proteins called elastins.

● Elastins are rich in the amino acids glycine and proline; however,
the proline residues are not hydroxylated, and no hydroxylysine
is present.

● Elastin molecules are crosslinked to one another by covalent bonds

between lysine residues.

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● Over time, collagens
become increasingly
crosslinked and
inflexible, and elastins
are lost from tissues
like skin.

● As a result, older
people often find that
their bones and joints
are less flexible, and
their skin becomes
wrinkled.

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➢ Collagen and elastin fibers are embedded in a matrix of
proteoglycans

The hydrated, gel-like network in which the collagen and

elastin fibrils of the ECM are enmeshed consists primarily
of proteoglycans, glycoproteins in which a large number of
glycosaminoglycans糖胺聚糖 are attached to a single protein
molecule.

Glycosaminoglycans (GAGs) are large carbohydrates,

characterized by repeating disaccharide units.

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 The three most common types of disaccharide units:

1) Chondroitin sulfate硫酸軟骨素: glucuronate葡糖醛酸(the ionized form

of glucuronic acid, GlcUA) and N-acetylgalactosamine (GalNAc).

2) Keratan sulfate硫酸角質素: galactose (Gal) and N-acetylglucosamine

(GlcNAc).

3) Hyaluronate透明質酸鹽: GlcUA and GlcNAc, contains no sulfate groups.

Because GAGs are hydrophilic molecules with many negatively

charged sulfate and carboxyl groups, they attract both water and
cations, thereby forming the hydrated, gelatinous matrix in which
collagen and elastin fibrils become embedded.

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 Most GAGs in the ECM are covalently bound to protein molecules to
form proteoglycans.

● Each proteoglycan consists of numerous GAG chains attached along

the length of a core protein.

● Proteoglycans vary greatly in size, depending on the molecular

weight of the core protein (about 10,000 to over 500,000) and the
number and length of the carbohydrate chains (1-200 per molecule,
with an average length of about 800 monosaccharide units).

● Proteoglycans are linked directly to collagen fibers to make up the

fiber/network structure of the ECM.

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● In some cases, the proteoglycans are integral components of the
plasma membrane, with their core polypeptides embedded within
the membrane.

● In other cases, proteoglycans are linked covalently to membrane

phospholipids.

● Alternatively, either proteoglycans or collagen may bind to

specific receptor proteins on the outer surface of the plasma
membrane.

● In many tissues, proteoglycans are present as individual molecules.

57
● In cartilage, numerous proteoglycans become attached to long
molecules of hyaluronate (core proteins of proteoglycans
attached via linker proteins), forming large complexes.

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➢ Free hyaluronate lubricates joints and facilitates cell migration

Hyaluronate, in addition to its role as the backbone of the

proteoglycan complex in cartilage, occurs as a free molecule
consisting of hundreds or even thousands of repeating
disaccharide units.

Hyaluronate molecules have lubricating properties and are most

abundant in places where friction must be reduced, such as the
joints between movable bones.

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➢ Adhesive glycoproteins anchor cells to the extracellular matrix

Direct links between the ECM and the plasma membrane are
reinforced by a family of adhesive glycoproteins that bind
proteoglycans and collagen molecules to each other and to
receptors on the membrane surface.

These proteins typically have multiple domains, some with

binding sites for macromolecules in the ECM and others with
binding sites for membrane receptors.

The two most common kinds of adhesive glycoproteins are the

fibronectins and laminins.

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➢ Fibronectins bind cells to the ECM and guide cellular movement

Fibronectins are a family of closely related adhesive glycoproteins

in the ECM and are widely distributed in vertebrates.

Fibronectins occur in soluble form in blood and other body fluids,

as insoluble fibrils in the extracellular matrix, and as an
intermediate form loosely associated with cell surfaces.

● These different forms of the protein are generated because the

RNA transcribed from the fibronectin gene is processed to
generate many different mRNAs.

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● A fibronectin molecule consists of
two very large polypeptide subunits
joined by two disulfide bonds near
their carboxyl ends.

● Each subunit has about 2500 amino

acids and is folded into a series of
rodlike domains connected by short,
flexible segments.

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● Several of the domains bind to one or more specific kinds of
macromolecules located in the ECM or on cell surfaces, including
several types of collagen, heparin, and the blood-clotting protein
fibrin纖維蛋白.

● Other domains recognize and bind to cell surface receptors.

✓ The receptor-binding activity of these domains has been localized
to a specific tripeptide sequence, RGD (arginine-glycine-aspartate).

✓ This RGD sequence is a common motif among extracellular adhesive

proteins and is recognized by various integrins on the cell surface.

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● Fibronectin fibrils can
form a loose network to
which cells attach.

● Myoblast cells on an ECM

containing fibronectin in
vitro, immunostained for
fibronectin (green) and
for DNA in the nucleus
(blue).

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➢ Laminins bind cells to the basal lamina

Laminins are conserved from simple invertebrates to humans.

Laminins are found mainly in the basal lamina基底層, a thin sheet

of specialized extracellular material, typically about 50 nm
thick, underlies epithelial cells, thereby separating them from
connective tissues.

Basal laminae also surround muscle cells, fat cells, and the
Schwann cells that form myelin sheaths around nerve cells.

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 Properties of the basal lamina

Despite differences in function and specific molecular composition

from tissue to tissue, all forms of basal lamina contain type IV
collagen (very fine, unstriated fibrils), proteoglycans, laminins, and
another glycoprotein called nidogen or entactin.

● Laminins are thought to be localized mainly on the surface of the

lamina that faces the overlying epithelia cells, where they help
bind the cells to the lamina.

● Fibronectins are located on the other side of the lamina, where

they help anchor cells of the connective tissue.

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 Cells can alter the properties of the basal lamina by secreting
enzymes that catalyze changes in the basal lamina.

● Matrix metalloproteinases間質金屬蛋白酶(MMPs) require metal ions

as cofactors, degrade the ECM locally, allowing cells to pass
through the ECM.

● Such activity is important for cells such as leukocytes to invade

injured tissues during inflammation.

● MMPs are also involved in abnormal invasive behavior; the MMP

activity of invasive cancer cells, such as metastatic melanoma cells,
is very high.

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 Properties of laminin

Laminin, a very large protein with a molecular weight of about

850,000, consists of three long polypeptides, denoted a, b, and g.

● There are several types of each of the three subunits, which can
combine to form many types of laminin.

● Disulfide bonds hold the polypeptide chains together in the shape

of a cross, with part of the long arm wound into a three stranded
coil.

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● Laminin consists of several
domains that include
binding sites for type IV
collagen, heparin, heparan
sulfate, and nidogen as well
as for laminin receptor on
the surface of overlying
cells.

● Its binding sites allow

laminin to serve as a
bridging molecule that
attaches cells to the basal
lamina.
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➢ Integrins are cell surface receptors that bind ECM components

Fibronectins and laminins can bind to animal cells because the

plasma membranes of most cells have specific receptors on their
surfaces that recognize and bind to specific regions of the
fibronectin or laminin molecule.

These receptors (and those for a variety of other ECM

constituents) belong to a large family of transmembrane proteins
that are called integrins.

● Integrins: their role in integrating the cytoskeleton with the

extracellular matrix.

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 Structure of integrins

An integrin consists of two large transmembrane polypeptides,

the a and b subunits, that associate with each other noncovalently.

● For a specific integrin, the extracellular portions of the a and b

subunits interact to form the binding site for a particular ECM
protein, with most of the binding specificity apparently depending
on the a subunit.

● On the cytoplasmic side of the membrane, integrins have binding

sites for specific linker proteins that mechanically link the
cytoskeleton and the ECM across the plasma membrane.

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● The presence of multiple types
of both a and b subunits results
in a large number of different
integrin heterodimers, which
vary in their binding
specificities.

● The most common integrin that

binds fibronectin is a5b1,
whereas a6b1 binds laminin.

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 Integrins and the cytoskeleton

The tails of integrins interact with proteins in the cytosol that link
integrins to cytoskeletal proteins.

Integrins make two main types of connections to the cytoskeleton:

● Focal adhesions; migratory and non-epithelial cells attach to

extracellular matrix molecules.

● Hemidesmosomes; epithelial cells attach to laminin in the basal

lamina.

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 Focal adhesions contain clustered integrins that interact with
bundles of actin microfilaments via several linker proteins.

● Linker proteins include:

✓ talin, which can bind to the actin-binding protein vinculin;

✓ a-actinin, which can bind directly to actin microfilaments.

● Integrins play important roles in regulating cell movement and

cell attachment.

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● An invasive human breast
cancer cell stained for F-
actin (red) and vinculin to
mark integrin attachment
sites (blue).

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 The integrin found in hemidesmosomes is a6b4 integrin.
● The integrins attached to intermediate filaments via linker proteins
such as plectin網蛋白.

79
 Integrin function

Because they bind to components of the ECM on the outside of

the cell and to actin microfilaments on the inside, integrins play
important roles in regulating cell movement and cell attachment.

● For example, mice lacking a particular integrin subunit (a7)

required for attachment to laminin develop a distinctive form of
progressive muscular dystrophy肌肉萎縮症.

● Humans that carry the same mutation develop progressive muscle

degeneration.

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 Integrins and signaling

Integrins also interact with intracellular signaling pathways, for

example:

● Signals such as binding of growth factors that lead to MAP kinase

activation can result in integrin clustering.

✓ “inside out” signaling: internal changes in the cell result in effects

on integrins at the surface; result from conformational changes
in the cytoplasmic regions of the a and b subunits.

● Integrins can also act as receptors that activate intracellular

signaling themselves (“outside in” signaling).

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 The original observations that suggested involvement of integrins
in signaling came from studies of cancer cells.

● For most normal cells to grow in culture, they must be attached

to a substratum; if such cells are prevented from attaching to an
extracellular matrix layer, they will cease dividing and undergo
apoptosis (anchorage-dependent growth貼附性生長).

● Cancer cells will continue to grow even when they are not firmly
attached to an extracellular matrix layer, apparently because
they no longer need to transduce signals that result from
attachment to the extracellular matrix.

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● Anchorage-dependent growth involves the activation of intracellular
pathways following integrin clustering.

● Several kinases are activated at focal adhesions following integrin

clustering, they are recruited to focal adhesions by adapter proteins
such as paxillin.

✓ These include focal adhesion kinase (FAK), kindlins, and integrin-

linked kinase (ILK).

✓ Cancer cells contain activated FAK even when they are not attached,
and cells can be transformed into cancerlike cells by the expression
of a mutant, activated form of FAK.

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➢ The dystrophin/dystroglycan complex stabilizes attachments of
muscle cells to the extracellular matrix

The costamere肋節 is an attachment structure at the surface of

striated muscle.

Costameres are aligned in register with Z-discs around the

surface of muscle cells; they physically attach muscle fibers at
the surface of the muscle cells to the plasma membranes, which
in turn are anchored to the ECM surrounding the muscle cells.

Costameres contain many of the same proteins found at focal

contacts, including b1-integrin, vinculin, talin, and a-actinin.

84
 In addition, costameres contain a specialized protein complex that
includes the large protein dystrophin.

● Mutations in the dystrophin gene cause the two most common types
of muscular dystrophy, Duchenne muscular dystrophy (DMD) and
Becker muscular dystrophy (BMD).

● DMD and BMD affect 1 in 3500 patients worldwide each year.

● Because the dystrophin gene is on the X chromosome, DMD and
BMD virtually always affect only boys.

85
 Dystrophin interacts with a multiprotein complex that includes
the integral membrane protein dystroglycan.

● Dystroglycan binds to laminin, linking the costameres to the

extracellular matrix.

● Dystrophin probably acts like a stiff spring, preventing damage

to muscle cells where they attach to the ECM and exert force
on the ECM during contraction.

● When dystrophin is absent, muscle cells are much more

susceptible to damage and eventual degeneration.

86
● Muscle cells immunostained
for dystrophin (green).
Blue-stained DNA marks the
locations of cell nuclei.
● Costameres are visible as
stripes of dystrophin.

87
 The plant cell surface

➢ Cell walls provide a structural framework and serve as a

permeability barrier

The presence of the cell wall is one of the major factors

causing plants to differ so much from animals.

Specifically, the rigidity of the wall makes cell movements

virtually impossible.

The sturdy cell walls enable plant cells to withstand the

considerable turgor pressure that is exerted by the uptake
of water.

The wall is also a permeability barrier for large molecules.

88
➢ The plant cell wall is a network of cellulose microfibrils,
polysaccharides, and glycoproteins
Plant cell walls contain cellulose纖維素 microfibrils enmeshed in a
complex network of branched polysaccharides and glycoproteins
called extensins伸展蛋白.

The two main types of polysaccharides are hemicelluloses and

pectins果膠.

● Cellulose, hemicelluloses, and glycoproteins are linked together

to form a rigid interconnected network that is embedded in a
pectin matrix.
● Lignins木質素 are localized between the cellulose fibrils and make
the wall especially strong and rigid.

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90
 Cellulose and hemicellulose

The predominant polysaccharide of the plant cell wall is cellulose,

which is the single most abundant organic macromolecule on earth.

● Cellulose is an unbranched polymer consisting of thousands of b-D-

glucose units linked together by b(1-›4) bonds.

● Cellulose molecules are long, ribbonlike structures that are

stabilized by intramolecular hydrogen bonds.

● Many such molecules (50-60, typically) associate laterally to form

the microfibrils found in cell walls.

● Cellulose microfibrils are often twisted together in a ropelike

fashion to generate even larger structures, called macrofibrils.

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 Hemicelluloses are chemically and structurally distinct from
cellulose.

● The hemicelluloses are a heterogeneous group of polysaccharides,

each consisting of a long, linear chain of a single kind of sugar
(glucose or xylose木糖) with short side chains bonded into a rigid
network.

● The side chains usually contain several kinds of sugars, including

the hexoses glucose, galactose, and mannose and the pentoses
xylose and arabinose.

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 Other cell wall components

Pectins are also branched polysaccharides, but with backbones

called rhamnogalacturonans鼠李聚糖半乳糖醛酸聚糖 that consist
mainly of negatively charged galacturonic acid and rhamnose.

● The side chains attached to the backbone contain some of the

same monosaccharides found in hemicelluloses.

● Pectin molecules form the matrix in which cellulose microfibrils

are embedded.

● Because of their highly branched structure and their negative

charge, pectins trap and bind water molecules; as a result,
pectins have a gel-like consistency.

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 Extensins are glycoproteins; they are rigid, rodlike molecules
that are tightly woven into the complex polysaccharide network
of the cell wall.

● Extensins are initially deposited in the cell wall in a soluble

form.

● Once deposited, extensins become covalently crosslinked to

one another and to cellulose, generating a reinforced protein-
polysaccharide complex.

● Extensins are least abundant in the cell walls of actively

growing tissues and most abundant in the cell walls of tissues
that provide mechanical support to the plant.

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 Lignins are very insoluble polymers of aromatic alcohols that
occur mainly in woody tissues.

● The Latin word for “wood” is lignum.

● Lignin molecules are localized mainly between the cellulose
fibrils, where they function to resist compression forces.

● Lignin accounts for as much as 25% of the dry weight of

woody plants, making it second only to cellulose as the most
abundant organic compound on Earth.

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➢ Cell walls are synthesized in several discrete stages

The plant cell wall components are secreted from the cell stepwise,
creating a series of layers in which the first layer to be synthesized
ends up farthest away from the plasma membrane.

The first structure to be laid down is called the middle lamella中膠層;

it is shared by neighboring cell walls and holds adjacent cells
together.

The next structure to be formed is called the primary cell wall,

which forms when the cells are still growing.

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● The primary cell wall consists of a loosely organized network of
cellulose microfibrils associated with hemicelluloses, pectins, and
glycoproteins.

● The cellulose microfibrils are generated by cellulose-synthesizing

enzyme complexes called rosettes花環體 that are localized within
the plasma membrane.

● Because the microfibrils are anchored to other wall components,

the rosettes must move in the plane of the membrane as they
lengthen the growing cellulose microfibrils.

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98
 When the shoots or roots of a plant are growing, cell walls must be
remodeled.

● A family of proteins called expansins擴張素 helps cell walls retain

their pliability.

● One way in which expansins may act is by disrupting the normal

hydrogen bonding of glycans within the microfibrils of the cell wall
to allow for rearrangement of the microfibrils.

● The plant hormone auxin (indole-3-acetic acid) likely stimulates

expansin activity.

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 Many cells that have stopped growing add a thicker, more
rigid set of layers that are referred to collectively as the
secondary cell wall.

● The components of the multilayered secondary wall are

added to the inner surface of the primary wall after cell
growth has ceased.

● Cellulose and lignins are the primary constituents of the

secondary wall, making this structure significantly stronger,
harder, and more rigid than the primary wall.

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● Each layer of the secondary wall consists of densely packed bundles
of cellulose microfibrils, arranged in paralled and oriented to lie at
an angle to the microfibrils of adjacent layers.

● As the secondary walls form, microtubules located beneath the

plasma membrane are oriented in the same direction as the newly
formed cellulose microfibrils, and the cellulose-synthesizing
rosettes are aggregated into large arrays containing dozens of
rosettes.

● The underlying microtubules are thought to guide the movement of

these rosette aggregates, which synthesize large parallel bundles
of cellulose microfibrils as they move.

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102
➢ Plasmodesmata permit direct cell-cell communication through the
cell wall

Plasmodesmata原生質絲,胞間連絲(singular: plasmodesma) are cytosolic

channels through relatively large openings in the cell wall, allowing
continuity of the plasma membranes from two adjacent cells.

A plasmodesma is cylindrical in shape, the channel diameter varies

from about 20 to about 200 nm.

A single tubular structure, the desmotubule連絲微管, usually lies in

the central channel of the plasmodesma.

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104
 ER cisternae are often seen near the plasmodesmata on either
side of the cell wall.

● ER membranes from adjoining cells are continuous with the

desmotubule and with the ER of the other cells; the ring of
cytosol between the desmotubule and the membrane that lines
the plasmodesma is called the annulus環,輪.

● The annulus is thought to provide cytosolic continuity between

adjacent cells, thereby allowing molecules to pass freely from
one cell to the next.

● The plasmodesmata therefore provide for continuity of the

plasma membrane, the ER, and the cytoplasm between adjacent
cells.
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In many respects, plasmodesmata appear to function somewhat like
gap junctions.

They reduce electrical resistance between adjacent cells by about

50-fold compared with cells that are completely separated by
plasma membranes.

In fact, the movement of ions between adjacent cells is proportional

to the number of plasmodesmata that connect the cells.

However, plasmodesmata allow the passage of much larger molecules,

including signaling molecules, RNAs, transcription factors, and even
viruses.

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