The Cytoskeleton

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 Cytoskeleton
• For cells to function properly, they must organize themselves in space and
interact mechanically with their environment
• They must be correctly shaped, physically robust, and properly structured
internally
• All cells have to be able to rearrange their internal components as they
grow, divide, and adapt to changing circumstances
• Eukaryotic cells have developed all these spatial and mechanical functions
to a very high degree, and they depend on a remarkable system of
filaments called the cytoskeleton
• It participates in cell division, intracellular traffic of organelles, ferrying of
materials, supports fragile plasma membrane, provides mechanical support,
enables cells such as sperm to swim, fibroblasts and white blood cells to
crawl across surfaces, provides the machinery in the muscle cells for
contraction and in the nerve cell to extend an axon and dendrites, guides
the growth of the plant cell wall and controls the amazing diversity of
eukaryotic cell shapes
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 The Cytoskeleton: Components and Structural Functions

• The cytosol is a major site of cellular metabolism and contains a

large number of different enzymes
• Proteins constitute about 20–30 % of the cytosol by weight, and
from a quarter to half of the total protein within cells is in the
cytosol. Protein concentration in the cytosol range from 200 to
400 mg/ml
• Because of the high concentration of cytosolic proteins,
complexes of proteins can form
• Many investigators believe that the cytosol is
highly organized, with most soluble proteins
either bound to filaments or otherwise
localized in specific regions

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Figure 16-2 Molecular Biology of the Cell (© Garland Science 2008)
 The Cytoskeleton: Components
and Structural Functions
• In an electron micrograph of a
typical animal cell, soluble proteins
packing the cell interior conceal
much of the internal structure. If a
cell is pretreated with a nonionic
detergent (e.g., Triton X-100),
which permeabilizes the
membrane, soluble cytosolic
proteins diffuse away
• In micrographs of detergent-
extracted animal cells, two types of
structures stand out—membrane-
limited organelles and the
filaments of the cytoskeleton,
which fill the cytosol 7
Electron micrograph of the apical part of a detergent-
extracted intestinal epithelial cell.
Microvilli, fingerlike projections of the plasma membrane,
cover the apical surface of an intestinal epithelial cell.
A bundle of microfilaments in the core of each
microvillus stabilizes the structure. The plasma
membrane surrounding a microvillus is attached to
the sides of the bundle by evenly spaced membrane–
microfilament linkages (yellow). The bundle continues
into the cell as a short rootlet. The rootlets of multiple
microvilli are cross-braced by connecting fibers (red)
composed of an intestinal isoform of spectrin. This
fibrous actin-binding protein is found in a narrow
band just below the plasma membrane in many
animal cells. The bases of the rootlets are attached to
keratin intermediate filaments. These numerous
connections anchor the rootlets in a meshwork of
filaments and thereby support the upright orientation
of the microvilli

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 Three Types of Filaments Compose the
Cytoskeleton
• The cytosol of a eukaryotic cell contains three types
of filaments that can be distinguished on the bases
of their diameter, type of subunit, and subunit
arrangment
• Actin filaments, also called microfilaments, are 8–9
nm in diameter and have a twisted two-stranded
structure
• Microtubules are hollow tubelike structures, 24 nm
in diameter, whose walls are formed by adjacent
protofilaments
• Intermediate filaments (IFs) have the structure of a
10-nm-diameter rope

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• Each type of cytoskeletal filament is a polymer of protein
subunits
• Monomeric actin subunits assemble into microfilaments.
• Dimeric subunits composed of α - and β -tubulin polymerize into
microtubules
• Unlike microfilaments and microtubules, which are assembled
from one or two proteins, intermediate filaments are assembled
from a large diverse family of proteins. The most common
intermediate filaments, found in the nucleus, are composed of
lamins.
• Intermediate filaments constructed from other proteins are
expressed preferentially in certain tissues: for example, keratin-
containing filaments in epithelial cells, desmin-containing
filaments in muscle cells, and vimentin-containing filaments in
mesenchymal cells 10
• Most eukaryotic cells contain all three types of cytoskeletal
filaments, often concentrated in distinct locations
• Finally, microtubules, aligned with the long axis of the cell, are in
close proximity to major cell organelles such as the endoplasmic
reticulum, Golgi complex, and vesicles

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 Protein Subunits in Cytoskeletal Filaments

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 Cytoskeletal Filaments Are Organized
into Bundles and Networks
• On first looking at micrographs of a cell, one is struck by the
dense, seemingly disorganized mat of filaments present in the
cytosol. However, a keen eye will start to pick out areas—generally
where the membrane protrudes from the cell surface or where a
cell adheres to the surface or another cell—in which the filaments
are concentrated into bundles.
• From these bundles, the filaments continue into the cell interior,
where they fan out and become part of a network of filaments.
These two structures, bundles and networks, are the most
common arrangements of cytoskeletal filaments in a cell

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• Structurally, bundles differ from networks mainly in the
organization of the filaments. In bundles, the filaments
are closely packed in parallel arrays. In a network, the
filaments crisscross, often at right angles, and are loosely
packed
• Networks can be further subdivided. One type, associated
with the nuclear and plasma membranes, is planar (two-
dimenional), like a net or a web; the other type, present
within the cell, is three-dimensional, giving the cytosol gel-
like properties. In all bundles and networks, the filaments
are held together by various cross-linking proteins

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 Microfilaments and Membrane-Binding Proteins Form
a Skeleton Underlying the Plasma Membrane
• The distinctive shape of a cell depends on the organization of
actin filaments and proteins that connect microfilaments to the
membrane. These proteins, called membrane–microfilament
binding proteins, act as spot welds that tack the actin
cytoskeleton framework to the overlying membrane
• When attached to a bundle of filaments, the membrane
acquires the fingerlike shape of a microvillus or similar
projection
• When attached to a planar network of filaments, the membrane
is held flat like the red blood cell membrane. The simplest
membrane–cytoskeleton connections entail the binding of
integral membrane proteins directly to actin filaments
• More common are complex linkages that connect actin
filaments to integral membrane proteins through peripheral
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Mandal proteins that function as adapter proteins 16
• The richest area of actin filaments in many cells lies in the
cortex, a narrow zone just beneath the plasma membrane.
• In this region, most actin filaments are arranged in a network
that excludes most organelles from the cortical cytoplasm
• Perhaps the simplest cytoskeleton is the two-dimensional
network of actin filaments adjacent to the erythrocyte plasma
membrane
• In more complicated cortical cytoskeletons, such as those in
platelets, epithelial cells, and muscle, actin filaments are part
of a three-dimensional network that fills the cytosol and
anchors the cell to the substratum

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Example of erythrocyte cytoskeletal
network
• A red blood cell must squeeze through
narrow blood capillaries without rupturing
its membrane. The strength and flexibility of
the erythrocyte plasma membrane depend
on a dense cytoskeletal network that
underlies the entire membrane and is
attached to it at many points.
• The primary component of the erythrocyte
cytoskeleton is spectrin, a 200-nm-long
fibrous protein. The entire cytoskeleton is
arranged in a spoke-and-hub network

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• Each spoke is composed of a single
spectrin molecule, which extends
from two hubs and cross-links them.
Each hub comprises a short (14-
subunit) actin filament plus adducin,
tropomyosin, and tropomodulin .
Tropomyosin, and tropomodulin
strengthen the network by
preventing the actin filament from
depolymerizing. Six or seven spokes
radiate from each hub, suggesting
that six or seven spectrin molecules
are bound to the same actin filament

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• To ensure that the erythrocyte
retains its characteristic shape, the
spectrin-actin cytoskeleton is firmly
attached to the overlying
erythrocyte plasma membrane by
two peripheral membrane proteins,
each of which binds to a specific
integral membrane protein and to
membrane phospholipids.

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• Ankyrin connects the center of
spectrin to band 3 protein, an anion-
transport protein in the membrane.
Band 4.1 protein, a component of the
hub, binds to the integral membrane
protein glycophorin
• Both ankyrin and band 4.1 protein
also contain lipid-binding motifs,
which help bind them to the
membrane
• The dual binding by ankyrin and band
4.1 ensures that the membrane is
connected to both the spokes and the
hubs of the spectrin-actin
cytoskeleton
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Cortical cytoskeleton supporting the
plasma membrane in human
erythrocytes.
(a)Electron micrograph of the erythrocyte
membrane showing the spoke and-hub
organization of the cytoskeleton. The
long spokes are composed mainly of
spectrin and can be seen to intersect at
the hubs, or membrane-attachment
sites. The darker spots along the spokes
are ankyrin molecules, which cross-link
spectrin to integral membrane proteins.
(b)Diagram of the erythrocyte cytoskeleton
showing the various components

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 Intermediate Filaments Support the Nuclear
Membrane and Help Connect Cells into Tissues
• Intermediate filaments typically crisscross the cytosol, forming
an internal framework that stretches from the nuclear envelope
to the plasma membrane
• A network of intermediate filaments is located adjacent to some
cellular membranes, where it provides mechanical support. For
example, lamin A and lamin C filaments form an orthogonal
lattice that is associated with lamin B. The entire supporting
structure, called the nuclear lamina, is anchored to the inner
nuclear membrane by prenyl anchors on lamin B.
• Literature\Nuclear Lamin.pdf

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• At the plasma membrane,
intermediate filaments are
attached by adapter proteins
to specialized cell junctions
called desmosomes and
hemidesmosomes, which
mediate cell–cell adhesion and
cell–matrix adhesion,
respectively, particularly in
epithelial tissues
• In this way, intermediate
filaments in one cell are
indirectly connected to
intermediate filaments in a
neighboring cell or to the
extracellular matrix
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 Microtubules Radiate from Centrosomes
and Organize Certain Subcellular Structures
• Like microfilaments and intermediate filaments, microtubules are
not randomly distributed in cells. Rather, microtubules radiate
from the centrosome, which is the primary microtubule-
organizing center (MTOC) in animal cells
• The two ends of a microtubule differ in their dynamic properties
and are commonly designated as the (+) and (-) ends. For this
reason, microtubles can have two distinct orientations relative to
one another and to other cell structures. In many non dividing
animal cells, the MTOC is located at the center of the cell near
the nucleus, and the radiating microtubules are all
oriented with their (+) ends directed toward
the cell periphery

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• Fluorescence micrograph of a
Chinese hamster ovary cell
stained to reveal microtubles
and the MTOC
• The microtubules (green),
detected with an antibody to
tubulin, are seen to radiate from a
central point, the
microtubuleorganizing center
(MTOC), near the nucleus. The
MTOC (yellow) is detected with
an antibody to a protein localized
to the centrosome.
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 Microtubules Radiate from Centrosomes
and Organize Certain Subcellular Structures
• Although most interphase animal cells contain a single
perinuclear MTOC, epithelial cells and plant cells contain
hundreds of MTOCs. Both of these cell types exhibit distinct
functional or structural properties or both in different regions of
the cell. The functional and structural polarity of these cells is
linked to the orientation of microtubules within them.
• The association of microtubules with the endoplasmic reticulum
and other membrane-bounded organelles may be critical to the
location and organization of these organelles within the cell. For
instance, if microtubules are destroyed by drugs such as
nocodazole or colcemid, the ER loses its network like
organization. Microtubules are also critical to the formation of the
mitotic apparatus—the elaborate, transient structure that
captures and subsequently separates replicated chromosomes in
A cell division.
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 Plant Microtubule
• Plant cells lack centrioles or spindle pole bodies except
in their flagellate male gametes, and they are entirely
absent in the conifers and flowering plants. Instead,
the nuclear envelope itself appears to function as the
main MTOC for microtubule nucleation and spindle
organization during plant cell mitosis.
• Plant cells lack centrosomes, and microtubules are
thought to self-organize into structured arrays
• New microtubules branch off preexisting microtubules
in the cortex of plant cells

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 The Interphase Plant Cytoskeleton

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The Plant Cytoskeleton
during Cell Division
Literature\Control of the
Actin Cytoskeleton in
Plant Cell Growth.pdf
Literature\The Plant Cytoskeleton_
Vacuoles and Cell walls make the
Difference.pdf

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 Assembly-Disassembly Reactions

• Both microtubules and microfilaments can be readily converted

between assembled and disassembled forms. In the conversion, the
protein subunits of microtubules and microfilaments are exchanged
rapidly between the fully assembled element and large pools
of disassembled subunits in solution in the cytoplasm. Cells can control
the balance between assembly and disassembly with high precision.
• As a result, the protein subunits can be recycled, and cytoskeletal
structures containing microtubules and microfilaments can be set up or
taken apart as the cell changes its function. As cell division occurs, for
example, microtubules and microfilaments forming cytoskeletal
structures typical of growing cells are rapidly disassembled and then
reassembled into structures that take part in cell division. 

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 Points to remember
• The cytosol is the internal aqueous medium of a cell exclusive
of all organelles and the cytoskeleton. It contains numerous
soluble enzymes responsible for much of the cell’s metabolic
activity
• Three major types of protein filaments—actin filaments,
microtubules, and intermediate filaments—make up the
cytoskeleton
• Microfilaments are assembled from monomeric actin
subunits; microtubules, from α- and β-tubulin subunits; and
intermediate filaments, from lamin subunits and other tissue
specific proteins
• In all animal and plant cells, the cytoskeleton provides
structural stability for the cell and contributes to cell
movement. Some bacteria have a primitive cytoskeleton
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• Actin bundles form the core of microvilli and other fingerlike
projections of the plasma membrane
• Cortical spectrin-actin networks are attached to the cell
membrane by bivalent membrane–microfilament binding
proteins such as ankyrin and band 4.1
• Intermediate filaments are assembled into networks and
bundles by various intermediate filament–binding proteins,
which also cross-link intermediate filaments to the plasma
and nuclear membranes, microtubules, and microfilaments
• In some animal cells, microtubules radiate out from a single
microtubule-organizing center lying at the cell center. Intact
microtubules appear to be necessary for endoplasmic
reticulum and Golgi membranes to form into organized
structures
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Cell–Cell and Cell–Matrix Adhesion

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 Junctions

• Two main ways in which animal cells are bound together: in

connective tissue, the main stress-bearing component is the
extracellular matrix. In epithelial tissue, it is the cytoskeletons
of the cells themselves linked from cell to cell by anchoring
junctions. Cell-matrix attachments bond epithelial tissue to
the connective tissue beneath it.
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• Physical attachment is critical, both in
epithelia and in non-epithelial tissues, but
junctions between cell and cell or between
cells and matrix are diverse in structure and
do more than transmit physical forces. Four
main functions can be distinguished, each
with a different molecular basis

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1. Anchored Junctions:
including both cell-cell
adhesion and cell-matrix
adhesion, transmit
stresses and are
tethered to cytoskeletal
filaments inside the cell

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2. Occluding junctions:
seal the gaps between
cells in epithelia so as
to make the cell sheet
into an impermeable
(or selectively
permeable) barrier

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3. Channel-forming
junctions: create
passageways linking the
cytoplasms of adjacent
cells

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4. Signal-relaying junctions:
alllow signals to be relayed
from cell to cell across
their plasma membranes
at sites of cell-to-cell
contact

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 Cell-Adhesion Molecules (CAM) Bind to One Another and to
Intracellular Proteins
• A large number of CAMs fall into
four major families:
– cadherins
– immunoglobulin (Ig) superfamily
– Integrins
– selectins
• Many CAMs are mosaics of multiple
distinct domains, many of which can
be found in more than one kind of CAM
They are called “repeats” when they exist multiple times in the
same molecule. Some of these domains confer the binding
specificity that characterizes a particular protein. Some other
membrane proteins, whose structures do not belong to any of
the major classes of CAMs, also participate in cell–cell
adhesion in various tissues 44
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• CAMs mediate, through their extracellular domains, adhesive
interactions between cells of the same type (homotypic adhesion)
or between cells of different types (heterotypic adhesion). A CAM
on one cell can directly bind to the same kind of CAM on an
adjacent cell (homophilic binding) or to a different class of CAM
(heterophilic binding)
• CAMs can be broadly distributed along the regions of plasma
membranes that contact other cells or clustered in discrete
patches or spots called cell junctions
• Cell–cell adhesions can be tight and long lasting or relatively weak
and transient
• The associations between nerve cells in the spinal cord or the
metabolic cells in the liver exhibit tight adhesion
• Immune-system cells in the blood can exhibit only weak, short-
lasting interactions, allowing them to roll along and pass through a
blood vessel wall on their way to fight an infection within a tissue
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• The cytosol-facing domains of CAMs recruit sets of
multifunctional adapter proteins. These adapters
act as linkers that directly or indirectly connect
CAMs to elements of the cytoskeleton; they can also recruit
intracellular molecules that function in signaling pathways to
control protein activity and gene expression
• In some cases, a complex aggregate of CAMs, adapter proteins,
and other associated proteins is assembled at the inner surface
of the plasma membrane. Because cell–cell adhesions are
intrinsically associated with the cytoskeleton and signaling
pathways, a cell’s surroundings influence its shape and functional
properties (“outside-in” effects); likewise, cellular shape and
function influence a cell’s surroundings (“inside-out” effects).
Thus connectivity and communication are intimately related
properties of cells in tissues.

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• The formation of many cell–cell adhesions entails two
types of molecular interactions
– First, CAMs on one cell associate laterally through their
extracellular domains or cytosolic domains or both into
homodimers or higher-order oligomers in the plane of the
cell’s plasma membrane; these interactions are called
intracellular, lateral, or cis interactions
– Second, CAM oligomers on one cell bind to the same or
different CAMs on an adjacent cell; these interactions are
called intercellular or trans interactions.
• Trans interactions sometimes induce additional cis
interactions and, as a consequence, yet even more
trans interactions.

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• Adhesive interactions between cells vary considerably, depending
on the particular CAMs participating and the tissue
• Tight adhesion can be generated when many weak interactions
are combined together in a small, well-defined area.
Furthermore, the association of intracellular molecules with the
cytosolic domains of CAMs can dramatically influence the
intermolecular interactions of CAMs by promoting their cis
association (clustering) or by altering their conformation

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Major families of cell-adhesion moleculesv(CAMs)
and adhesion receptors.
Dimeric E-cadherins most commonly form homophilic
(self) cross-bridges with E-cadherins on adjacent
cells. Members of the immunoglobulin (Ig)
superfamily of CAMs can form both homophilic
linkages (shown here) and heterophilic (nonself)
linkages. Selectins, shown as dimers, contain a
carbohydrate-binding lectin domain that recognizes
specialized sugar structures on glycoproteins
(shown here) and glycolipids on adjacent cells.
Heterodimeric integrins (for example, αv and β 3
chains) function as CAMs or as adhesion receptors
(shown here) that bind to very large, multiadhesive
matrix proteins such as fibronectin, only a small
part of which is shown here . Note that CAMs often
form higher-order oligomers within the plane of the
plasma membrane. Many adhesive molecules
contain multiple distinct domains, some of which
are found in more than one kind of CAM. The
cytoplasmic domains of these proteins are often
associated with adapter proteins that link them to
the cytoskeleton or to signaling pathways.

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Schematic model for the
generation of cell–cell
adhesions
Lateral interactions between cell-
adhesion molecules (CAMs)
within the plasma membrane of
a cell form dimers and larger
oligomers. The parts of the
molecules that participate in
these cis interactions vary
among the different CAMs.
Subsequent trans interactions
between distal domains of
CAMs on adjacent cells
generate a zipperlike strong
adhesion between the cells.

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 The Extracellular Matrix Participates
in Adhesion and Other Functions
• Certain cell-surface receptors, including some integrins,
can bind components of the extracellular matrix (ECM),
thereby indirectly adhering cells to each other through
their interactions with the matrix
• Three abundant ECM components:
– proteoglycans, a unique type of glycoprotein
– collagens, proteins that often form fibers
– soluble multi adhesive matrix proteins (e.g., fibronectin)
• The relative volumes of cells versus matrix vary greatly
among different animal tissues and organs. Some
connective tissue, for instance, is mostly matrix,
whereas many organs are composed of very densely
packed cells with relatively little matrix 53
• Although the extracellular matrix generally provides mechanical
support to tissues, it serves several other functions as well
• Different combinations of ECM components tailor the extracellular
matrix for specific purposes: strength in a tendon, tooth, or bone;
cushioning in cartilage; and adhesion in most tissues
• In addition, the composition of the matrix, which can vary,
depending on the anatomical site and physiological status of a
tissue, can let a cell know where it is and what it should do
(environmental cues)
• Changes in ECM components, which are constantly being
remodeled, degraded, and resynthesized locally, can modulate the
interactions of a cell with its environment.

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• The matrix also serves as a reservoir for many extracellular
signaling molecules that control cell growth and differentiation
• In addition, the matrix provides a lattice through or on which cells
can move, particularly in the early stages of tissue assembly
• Morphogenesis—the later stage of embryonic development in
which tissues, organs, and body parts are formed by cell
movements and rearrangements—also is critically dependent on
cell–matrix adhesion as well as cell–cell adhesion

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 Molecular Connections Between the ECM and
Cytoskeleton Are Defective in Muscular Dystrophy

• The importance of the adhesion receptor–mediated linkage between

ECM components and the cytoskeleton is highlighted by a set of
hereditary muscle-wasting diseases, collectively called muscular
dystrophies
• Duchenne muscular dystrophy (DMD), the most common type, is a
sex-linked disorder, affecting 1 in 3300 boys, that results in cardiac or
respiratory failure in the late teens or early twenties
• The first clue to understanding the molecular basis of this disease
came from the discovery that persons with DMD carry mutations in
the gene encoding a protein named dystrophin. This very large protein
was found to be a cytosolic adapter protein, binding to actin filaments
and to an adhesion receptor called dystroglycan

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 Plant Tissues
• The overall structural organization of plants is generally simpler
than that of animals. For instance, plants have only four broad
types of cells, which in mature plants form four basic classes of
tissue: dermal tissue interacts with the environment; vascular
tissue transports water and dissolved substances (e.g., sugars,
ions); space filling ground tissue constitutes the major sites of
metabolism; and sporogenous tissue forms the reproductive
organs
• Plant tissues are organized into just four main organ systems:
stems have support and transport functions; roots provide
anchorage and absorb and store nutrients; leaves are the sites of
photosynthesis; and flowers enclose the reproductive structures.
Thus at the cell, tissue, and organ levels, plants are generally less
complex than most animals
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• Unlike animals, plants do not replace or repair old or
damaged cells or tissues; they simply grow new organs.
• Most importantly in contrast with animals, few cells in plants
directly contact one another through molecules incorporated
into their plasma membranes
• Instead, plant cells are typically surrounded by a rigid cell wall
that contacts the cell walls of adjacent cells
• Also in contrast with animal cells, a plant cell rarely changes
its position in the organism relative to other cells
• These features of plants and their organization have
determined the distinctive molecular mechanisms by which
their cells are incorporated into tissues

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 Only a Few Adhesive Molecules Have Been
Identified in Plants

• Systematic analysis of the Arabidopsis genome

and biochemical analysis of other plant species
provide no evidence for the existence of plant
homologs of most animal CAMs, adhesion
receptors, and ECM components
• This finding is not surprising, given the
dramatically different nature of cell–cell and
cell–matrix/wall interactions in animals and
plants
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• Among the adhesive-type proteins apparently unique to
plants are five wall-associated kinases (WAKs) and WAK-like
proteins expressed in the plasma membrane of Arabidopsis
cells.
• The extracellular regions in all these proteins contain multiple
epidermal growth factor (EGF) repeats, which may directly
participate in binding to other molecules
• Some WAKs have been shown to bind to glycine-rich proteins
in the cell wall, thereby mediating membrane–wall contacts.
• These Arabidopsis proteins have a single transmembrane
domain and an intracellular cytosolic tyrosine kinase domain,
which may participate in signaling pathways

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• The results of in vitro binding assays combined with
in vivo studies and analyses of plant mutants have
identified several macromolecules in the ECM that
are important for adhesion
• For example, normal adhesion of pollen, which
contains sperm cells, to the stigma or style in the
female reproductive organ of the Easter lily requires
a cysteine-rich protein called stigma/stylar cysteine-
rich adhesin (SCA) and a specialized pectin that can
bind to SCA

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• The paucity of plant adhesive molecules
identified to date, in contrast with the many
well-defined animal adhesive molecules, may
be due to the technical difficulties in working
with the ECM/cell wall of plants. Adhesive
interactions are often likely to play different
roles in plant and animal biology, at least in
part because of their differences in
development and physiology
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 References

• Harvey Lodish , Arnold Berk , Chris A. Kaiser ,

Monty Krieger, Anthony Bretscher, Hidde Ploegh,
Angelika Amon ,Matthew P. Scott. 2012. Molecular
Cell Biology, 7th edition, W.H. Freeman. USA.
• Plant Physiology – Salisburry & Ross

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