COMPARTMENTALIZATION OF EUKARYOTIC CELL

In eukaryotes (which are approximately a thousand times the volume of bacteria) the rates of
chemical reactions would be limited by the diffusion of small molecules if a cell were not
partitioned into smaller compartments termed organelles. Each organelle is surrounded by one or
more biomembranes, and each type of organelle contains a unique complement of proteins – some
embedded in its membrane(s), others in its aqueous interior space, or lumen. These proteins enable
each organelle to carry out its characteristic cellular functions.
The table below provides a short description of the main organelles of an animal cell:
STRUCTURE DESCRIPTION BIOLOGICAL ROLE
STRUCTURAL ELEMENTS
Cytosketeton Network of protein filaments
Structural support; cell movement
Flagella(cilia, Cellular extensions Motility or moving fluids over
microvilli) surfaces
Centrioles Hollow microtubules Moving chromosomes during cell
division
ENDOMEMBRANE SYSTEM
Plasma membrane Lipid bilayer in which proteins are Regulates what passes into and out of
embedded cell; cell-to-cell communication
Endoplasmic Network of internal membranes; Rough type processes proteins for
reticulum forms compartments and vesicles secretion and synthesizes
phospholipids; smooth type synthesize
fats and steroids
Nucleus Structure bounded by double Control center of cell; directs protein
membrane; contains chromosomes synthesis and cell reproduction
Golgi apparatus Stacks of flattened vesicles Modifies and packages proteins for
export from cell; forms secretory
vesicles
Lysosomes Vesicles derived from Golgi Digest worn-out mitochondria and cell
complex that contain hydrolytic debris; play role in cell death
digestive enzymes
ENERGY-PRODUCTING ORGANELLES
Mitochondria Power plant of the cell; site of
Bacteria-like elements with double
membrane oxidative metabolism; synthesis of
ATP
ORGANELLES OF GENE EXPRESSION
Chromosomes Long threads of DNA that form a Contain hereditary information
complex with protein
Nucleolus Site of rRNA synthesis Assembles ribosomes
Ribosomes Small, complex assemblies of Site of protein synthesis
protein, often bound to ER

The cytoplasm is the part of the cell outside the largest organelle, the nucleus. It is composed
of hyaloplasm and cell organelles dispersed in it. The cytosol, the aqueous part of the hyaloplasm
also contains its own distinctive proteins.
Cytoplasm
 Cell Compartmentalization. PL4.

Hyaloplasm
Cell organelles
Cytosol Cytoskeleton
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The cytoplasm is a colloidal solution. It is viscous, semifluid and precipitates if placed into
water. It is constantly active (rotation and streaming), allowing the cell to be in a continuous
dynamic flux.

ER - ENDOPLASMIC RETICULUM
Generally, the largest membrane in a eukaryotic cell encloses the endoplasmic reticulum (ER)
– an extensive network of closed, flattened membrane-bounded sacs called cisternae. The
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endoplasmic reticulum has a number of functions in the cell but is particularly important in the
synthesis of lipids, membrane proteins, and secreted proteins.
The Smooth Endoplasmic Reticulum - it lacks ribosomes and is the place for synthesis of
fatty acids and phospholipids. Although many cells have very little smooth ER, this organelle is
abundant in hepatocytes. Enzymes in the smooth ER of the liver also modify or detoxify
hydrophobic chemicals such as pesticides and carcinogens by chemically converting them into more
water-soluble, conjugated products that can be excreted from the body. High doses of such
compounds result in a large proliferation of the smooth ER in liver cells.
The Rough Endoplasmic Reticulum – its cytosolic face is studded with ribosomes.
Ribosomes bound to the rough ER synthesize certain membrane and organelle proteins and
virtually all proteins to be secreted from the cell. A ribosome that fabricates such a protein is bound
to the rough ER by the nascent polypeptide chain of the protein. As the growing polypeptide
emerges from the ribosome, it passes through the rough ER membrane, with the help of specific
proteins in the membrane. Newly made membrane proteins remain associated with the rough ER
membrane, and proteins to be secreted accumulate in the lumen of the organelle. All eukaryotic
cells contain a noticeable amount of rough ER because it is needed for the synthesis of plasma
membrane proteins and proteins of the extracellular matrix. Rough ER is particularly abundant in
specialized cells that produce an abundance of specific proteins to be secreted. For example, plasma
cells produce antibodies, pancreatic acinar cells synthesize digestive enzymes, and cells in the
pancreatic islets of Langerhans produce the polypeptide hormones insulin and glucagon. In
secretory cells a large part of the cytosol is filled with rough ER and secretory vesicles.
Several minutes after proteins are synthesized in the rough ER, most of them leave the
organelle within small membrane-bounded transport vesicles. These vesicles, which bud from
regions of the rough ER not coated with ribosomes, carry the proteins to another membrane-limited
organelle, the Golgi complex.

GOLGI COMPLEX (GOLGI APPARATUS)

This organelle is a series of flattened
membrane vesicles or sacs (cisternae), surrounded
by a number of more or less spherical
membranelimited vesicles. The stack of Golgi
cisternae has three defined regions—the cis, the
medial, and the trans. Transport vesicles from the
rough ER fuse with the cis region of the Golgi
complex, where they deposit their protein contents.
These proteins then progress from the cis to the
medial and to the trans region. Within each region
are different enzymes that modify proteins to be
secreted and membrane proteins differently,
depending on their structures and their final
destinations.
After proteins to be secreted and membrane
proteins are modified in the Golgi complex, they
are transported out of the complex by a second set
of vesicles, which seem to bud from the trans side
of the Golgi complex. Some vesicles carry
membrane proteins destined for the plasma membrane or soluble proteins to be released from the
cell surface; others carry soluble or membrane proteins to lysosomes or other organelles.
So, Golgi complex functions as a factory in which proteins received from the ER are further
processed and sorted for transport to their eventual destinations: lysosomes, the plasma membrane,

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or secretion. In addition, glycolipids and sphingomyelin are synthesized within the Golgi. Proteins,
as well as lipids and polysaccharides, are transported from the Golgi apparatus to their final
destinations through the secretory pathway. This involves the sorting of proteins into different kinds
of transport vesicles, which bud from the trans Golgi network and deliver their contents to the
appropriate cellular locations. Proteins that function within the Golgi apparatus must be retained
within that organelle, rather than being transported along the secretory pathway. In contrast to the
ER, all of the proteins retained within the Golgi complex are associated with the Golgi membrane
rather than being soluble proteins within the 1) the formation of the plasma membrane; 2)
lumen. The signals responsible for retention of the synthesis of polysaccharides,
some proteins within the Golgi have been glycoproteins, glycolipids and sphingomyelin
localized to their transmembrane domains, which (the only nonglycerol phospholipid in cell
retain proteins within the Golgi apparatus by membranes);
preventing them from being packaged in the 3) the modification of products through the
transport vesicles that leave the trans Golgi addition of fatty acids, sulfation and
network. glycosylation;
Functions of Golgi apparatus: 4) the concentration and packaging
of
synthesized material into secretory
versicles; 5) the biogenesis of lysosomes.

Biogenesis: Large membrane-bounded

organelles, such as the Golgi apparatus and
the endoplasmic reticulum, break up into
many smaller fragments during M phase,
which ensures their even distribution into
daughter cells during cytokinesis. In such a
way these organelles are developed from the
preexisting organelles (ER or GA).

LYSOSOMES
Transport from the Golgi apparatus Proteins are sorted in
the trans Golgi network and transported in vesicles to their
final destinations. In the absence of specific targeting signals,
proteins are carried to the plasma membrane by constitutive
secretion. Alternatively, proteins can be diverted from the
constitutive secretion pathway and targeted to other
destinations, such as lysosomes or regulated secretion from
the cells.

Lysosomes provide an excellent example of the ability of intracellular membranes to form

closed compartments in which the composition of the lumen differs substantially from that of the
surrounding cytosol. Found exclusively in animal cells, lysosomes are responsible for degrading
certain components that have become obsolete for the cell or
organism. The process by which an aged organelle is degraded in a
lysosome is called autophagy (―eating oneself‖). A process in
which excessive amounts of secreted material (ex.: proteins,
hormones, etc.) are fused with lysosomes for hydrolysis is called
crinophagy. Materials taken into a cell by endocytosis or
phagocytosis also may be degraded in lysosomes. In phagocytosis,
large, insoluble particles (e.g., bacteria) are enveloped by the
plasma membrane and internalized.
Lysosomes contain a group of enzymes that degrade polymers
into their monomeric subunits. For example, nucleases degrade
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RNA and DNA into nucleotides; proteases degrade a variety of proteins and peptides;
phosphatases remove phosphate groups from nucleotides, phospholipids, and other compounds,
etc. All the lysosomal enzymes work most efficiently at acid pH values and collectively are termed
acid hydrolases. The enzymes are
Content of a Lysosome
synthesized by ribosomes on the ER and are processed and packaged by the Golgi apparatus.
Like all other intracellular organelles, the
lysosome not only contains a unique collection of
enzymes, but also has a unique surrounding
membrane. Two types of transport proteins in the
lysosomal membrane work together to pump H +
(H+-ATPase) and Cl- ions from the cytosol across
the membrane, thereby acidifying the lumen. The
acid pH helps to denature proteins, making them
accessible to the action of the lysosomal
hydrolases. Most of the lysosomal membrane
proteins are unusually highly glycosylated, which
helps to protect them from the lysosomal proteases in the lumen (making the lysosomal membrane
resistant to acid denaturation). Lysosomal enzymes are poorly active at the neutral pH of cells and
most extracellular fluids. Thus, if a lysosome releases its enzymes into the cytosol, where the pH is
between 7.0 and 7.3, they cause little degradation of cytosolic components.
Lysosomes vary in size and shape, and several hundred may be present in a typical animal
cell. Several types of lysosomes can be distinguished: Primary lysosomes are roughly spherical and
do not contain obvious particulate or membrane debris. Secondary lysosomes, which are larger and
irregularly shaped, appear to result from the fusion of primary lysosomes with other
membranebounded organelles and vesicles. They contain particles or membranes in the process of
being digested.
The functions of lysosomes include:
 The digestion of intracellular and extracellular
materials;
 The autolysis (the self destruction if a cell is deformed
or aged);
 The function of defense of a cell against invasion by
bacteria, viruses and toxic substances;
 They play an important role in the fertilization of an
ovum by a sperm cell. The acrosome at the tip of the
head of the sperm contains lysosomes which
hydrolyze the membrane of the ovum.

Lysosomal storage diseases result in the accumulation of the undigested substrates in lysosomes,
with severe pathological consequences, most often in the nervous system. This occurs in Hurler's
disease, for example, in which the enzyme required for the breakdown of glycosaminoglycans is
defective or missing. Tay-Sachs disease is caused by a defect in one enzyme catalyzing a step in the
lysosomal breakdown of gangliosides. The resulting accumulation of these glycolipids, especially in
nerve cells, has devastating consequences. The symptoms of this inherited disease are usually
evident before the age of 1. Affected children commonly become demented and blind by age 2 and
die before their third birthday. Nerve cells from such children are greatly enlarged with swollen
lipid-filled lysosomes. The most severe form of lysosomal storage disease, however, is a very rare
disorder called inclusion-cell disease (I-cell disease). In this disease almost all of the hydrolytic
enzymes are missing from the lysosomes of fibroblasts, and their undigested substrates accumulate
in lysosomes, which consequently form large ―inclusions‖ in the patients' cells.
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PROTEASOMES
Cytosolic and nuclear proteins generally are not degraded in lysosomes but rather in
proteasomes, large multiprotein complexes located mainly in the cytosol. The numerous
proteasomes dispersed throughout the cell proteolytically cleave ubiquitin-tagged proteins in an
ATP-dependent process that yields short (7- to 8-residue) peptides and intact
ubiquitin (Ub - a special polypeptide) molecules.
Proteasomes functions:
1. They remove abnormal and misfolded proteins from the cell.
2. They are involved in the cell's stress response.
3. As part of the Ub system, they are involved in regulating the cell cycle.
4. They are involved in cellular differentiation (where they degrade transcription
factors and metabolic enzymes).
5. They play an important role in the immune system.
Proteasomes are cylindrical structures very similar to chaperons (a large proteasome group of
protein families whose role is to stabilize unfolded proteins, unfold them for translocation across
membranes or for degradation, and/or to assist in their correct folding and assembly).

PEROXISOMES
All animal cells (except erythrocytes) contain peroxisomes, a class of single-membrane bound,
roughly spherical organelles that contain several oxidases – enzymes that use molecular oxygen to
oxidize organic substances, in the process forming hydrogen peroxide (H 2O2), a corrosive
substance.

Peroxisomes also contain abundant amounts of the enzyme catalase, which utilizes the H2O2
generated by other enzymes in the organelle to oxidize a variety of other substrates, such as
phenols, formic acid, formaldehyde, and alcohol, by the ―peroxidative‖ reaction:
H2O2 + R′ H2 → R′ + 2H2O
This type of oxidative reaction is particularly important in liver and kidney cells, where the
peroxisomes detoxify various toxic molecules that enter the bloodstream. About 25% of the ethanol
we drink is oxidized to acetaldehyde in this way. Catalase also degrades hydrogen peroxide to yield
water and oxygen:
2 H2O2 Catalase→ 2 H2O + O2
In contrast with the oxidation of fatty acids in mitochondria, which produces CO 2 and is
coupled to the generation of ATP, peroxisomal oxidation of fatty acids yields acetyl groups and is
not linked to ATP formation. The energy released during peroxisomal oxidation is converted into
heat, and the acetyl groups are transported into the cytosol, where they are used in the synthesis of
cholesterol and other metabolites. In most eukaryotic cells, the peroxisome is the principal organelle
in which fatty acids are oxidized, thereby generating precursors for important biosynthetic
pathways. Particularly in liver and kidney cells, various toxic molecules that enter the bloodstream
also are degraded in peroxisomes, producing harmless products.
In the human genetic disease X-linked adrenoleukodystrophy (ADL), peroxisomal oxidation
of very long chain fatty acids is defective. The ADL gene encodes the peroxisomal membrane
protein that transports into peroxisomes an enzyme required for the oxidation of these fatty acids.
Persons with the severe form of ADL are unaffected until midchildhood, when severe neurological
disorders appear, followed by death within a few years. Another example of peroxisomal
misfunction is the inherited human disease Zellweger syndrome, in which a defect in importing
proteins into peroxisomes leads to a severe peroxisomal deficiency. These individuals, whose cells
contain ―empty‖ peroxisomes, have severe abnormalities in their brain, liver, and kidneys, and they

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die soon after birth. One form of this disease has been shown to be due to a mutation in the gene
encoding a peroxisomal integral membrane protein, the peroxin Pex2, involved in protein import.
Biogenesis: Since 1985 it has been thought that peroxisomes are autonomous organelles
multiplying by growth and division (like mitochondrion). Lately though support for an
ERperoxisome connection came. Recent studies show that peroxisomes are at most semi-
autonomous organelles because the ER supplies the membrane of peroxisomes. This process is
guided by a few pioneering peroxisomal membrane proteins that start their life in the ER and
contribute to the
formation of a
specialized extension
from the rough ER.
After reaching a
considerable size, this
specialized ER is
detached from the
rough ER. Additional
integral membrane and
peripheral proteins are
recruited until the
protein import
machinery has been
assembled and the
import of matrix
proteins can start as the
ERPM --Peroxisome Connection plasma membrane; L - lysosome; E - endosome, P - peroxisome; G - Golgi;
last step in the ER - endoplasmic reticulum; N - nucleus. peroxisome maturation
pathway.
Peroxisomal proteins are synthesized on free polyribosomes. The folding starts in the cytosol
before they are taken en route to their final destination within the cell. Peroxisomal targeting signals
(PTSs) are recognized by cytosolic proteins (receptors) that guide their cargo to the peroxisomal
membrane.

NUCLEUS
The nucleus, the largest organelle in animal cells, is surrounded by two membranes, each one
a phospholipid bilayer containing many different types of proteins. The inner nuclear membrane
defines the nucleus itself. In most cells, the outer nuclear membrane is continuous with the rough
endoplasmic reticulum, and the space between the inner and outer nuclear membranes is continuous
with the lumen of the rough endoplasmic reticulum. The two nuclear membranes appear to fuse at
nuclear pores, the ringlike complexes composed of specific membrane proteins through which
material moves between the nucleus and the cytosol. In a growing or differentiating cell, the nucleus
is metabolically active, replicating DNA and synthesizing rRNA, tRNA, and mRNA. Within the
nucleus mRNA binds to specific proteins, forming ribonucleoproteid particles. Most of the cell’s
ribosomal RNA is synthesized in the nucleolus, a subcompartment of the nucleus that is not
bounded by a phospholipid membrane. Some ribosomal proteins are added to ribosomal RNAs
within the nucleolus as well. The finished or partly finished ribosomal subunits, as well as tRNAs
and mRNA-containing particles, pass through a nuclear pore into the cytosol for use in protein
synthesis. In mature erythrocytes from nonmammalian vertebrates and other types of ―resting‖
cells, the nucleus is inactive or dormant and minimal synthesis of DNA and RNA takes place.
In a nucleus that is not dividing, the chromosomes are dispersed and not dense enough to be
observed in the light microscope. Only during cell division individual chromosomes are visible by
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light microscopy. In the electron microscope, the nonnucleolar regions of the nucleus, called the
nucleoplasm, can be seen to have dark- and lightstaining areas. The dark areas, which are often
closely associated with the nuclear membrane, contain condensed concentrated DNA, called
heterochromatin. Fibrous proteins called lamins form a two-dimensional network along the inner
surface of the inner membrane, giving it shape and apparently binding DNA to it. The breakdown of
this network occurs early in cell division. The lightstaining areas form the euchromatin –
transcriptionally active part.

MITOCHONDRION
Most eukaryotic cells contain many mitochondria, which occupy up to 25 percent of the
volume of the cytoplasm. The two membranes that bound a mitochondrion differ in composition
and function. The outer membrane, composed of about half lipid and half protein, contains porins
that make the membrane permeable to certain molecules. The inner membrane, which is much less
permeable, is about 20 – 25% lipid and 75 - 80% protein - a higher proportion of protein than exists
in other cellular membranes. The surface area of the inner membrane is greatly increased by a large
number of infoldings, or cristae, that protrude into the matrix, or central space.
In nonphotosynthetic cells, the principal fuels
for ATP synthesis are fatty acids and glucose.
The complete aerobic degradation of glucose to
CO2 and H2O is coupled to the synthesis of as
many as 30 molecules of ATP. In eukaryotic
cells, the initial stages of glucose degradation
take place in the cytosol, where 2 ATP
molecules per glucose molecule are generated.
The terminal stages of oxidation and the
coupled synthesis of ATP are carried out by
enzymes in the mitochondrial matrix and inner
membrane. As many as 28 ATP molecules per
glucose molecule are generated
in mitochondria. Similarly,
virtually all the ATP formed in the oxidation of fatty acids to CO2 is generated in mitochondria.
Thus mitochondria can be regarded as the ―power plants‖ of the cell.
Mitochondrial genome: Mitochondria contain also their own genetic apparatus composed of
DNA (circular), mRNA, tRNA, rRNA, which is situated in matrix. The mt genome contains 37
genes, all of which are involved in the production of energy and its storage in ATP. Thirteen of these
genes encode proteins; 22 genes encode tRNAs and 2 genes - ribosomal RNAs that translate the
proteins' genes within the mitochrondrion. Mammalian mt genes use a slightly different genetic
code than nuclear genes.
Biogenesis: Mitochondria are self-replicative, which means that one mitochondrion can form
a second one, a third one, whenever the cell needs increased amounts of ATP.

RIBOSOMES
Ribosomes are essential for almost all prokaryotic and eukaryotic cells. Prokaryotic
ribosomes have a sedimentation value of 70S when centrifuged and are found in bacteria,
mitocondria and chloroplasts. Eukaryotic ribosomes have a value of 80S and are found in the
cytoplasm of eukaryotic cells.
The ribosome complex may be attached to both the endoplasmic reticulum and the nuclear
membrane. They are also as free floating structures in the cytoplasm. They often cluster together in
groups along a strand of mRNA to form polyribosomes (polysomes).
Free ribosomes Attached ribosomes

Location: Cytosol Attached to ER

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Proteins are synthesized for: Mitochondria Golgi complex

Nucleus Lysosomes
Peroxisomes Secretor vesicles
Cell
membrane Biogenesis: Ribosomes are approximately 150-200 Ao in size
and consist of 1 large and 1 small subunit. Normally these subunits exist
independently in different regions of the cell, but associate to perform
protein synthesis. The subunits consist of rRNA and ribosomal proteins,
which associate together in the nucleolus (place of ribosomal biogenesis).

CYTOSKELETON
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. 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 arrangement.
Microfilaments, also called actin
filaments (because they are made mainly of a
globular protein - actin), are 8–9 nm in
diameter and have a twisted two-stranded
structure. They play an important role in the
movement of substances within the cell, form
an elastic support for the cell membrane, in
muscle cells they are organized into a special
contractile machine that is the basis of muscle
Structural Organization of Microtubule, contraction.
Microfilament and Intermediate Filament Microtubules are hollow
tube-like structures, 25 nm in diameter,
that radiate from
the centrioles towards the periphery of a cell. Their walls are formed by 13 parallel filaments called
protofilaments. Microtubules are made of tubulin subunits. They are presented in cytoplasm, in
flagellum of a sperm, in cilium, in centrioles and the mitotic spindle.
Intermediate filaments (IFs) have the structure of a 10-nm-diameter rope. 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.

Most eukaryotic cells contain all three types of cytoskeletal filaments, often concentrated in
distinct locations. For example, in the absorptive epithelial cells that line the lumen of the intestine,
actin microfilaments are abundant in the apical region, where they are associated with cell–cell
junctions and support a dense carpet of microvilli. Actin filaments are also present in a narrow zone
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adjacent to the plasma membrane in the lateral regions of these cells. Keratin intermediate
filaments, forming a meshwork, connect microvilli and are tethered to junctions between cells.
Lamin intermediate filaments support the inner nuclear membrane. 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.
The cytoskeleton has been highly conserved in evolution. A comparison of gene sequences
shows only a small percentage of differences in sequence between yeast actin and tubulin and
human actin and tubulin. This structural conservation is explained by the variety of critical
functions that depend on the cytoskeleton. A mutation in a cytoskeleton protein subunit could
disrupt the assembly of filaments and their binding to other proteins. Analyses of gene sequences
and protein structures have identified bacterial homologs of actin and tubulin. The absence of IFlike
proteins in bacteria and unicellular eukaryotes is evidence that intermediate filaments appeared later
in the evolution of the cytoskeletal system. The first IF protein to arise was most likely a nuclear
lamin from which cytosolic IF proteins later evolved.

CENTRIOLES
Centrioles both assemble and organize long, hollow cylinders of microtubules. Under the
electron microscope the centrioles appear as two short, hollow, cylinders usually lying at right
angles to each other. Each centriole is made up of nine microtubule triplets, which lie evenly spaced
in a ring. There are no microtubules in the center (9+0 arrangement).
The centrioles appear as two, darkly
staining granules, usually above the nucleus in
animal cells. They are generally absent in plant
cells, except in motile cells. The centrioles lie
in a small mass of specialized cytoplasm
called centrospheres (or pericentriolar
material). The centrioles and the centrosphere
are together described as centrosome that
serves as microtubule organizing centers
(MTOCs). Microtubules help determine the
cell shape, move chromosomes during cell
Centriole Structure division, and provide the internal structure of
cilia and flagella.

Biogenesis: During interphase of each cell cycle, the centrioles and other components of the
centrosome are duplicated but remain together as a single complex on one side of the nucleus. As
mitosis begins, this complex splits in two and each centriole pair becomes part of a separate MTOC
that nucleates a radial array of microtubules called an aster. The two asters move to opposite sides
of the nucleus to form the two poles of the mitotic spindle. As mitosis ends and the nuclear
envelope re-forms around the separated chromosomes, each daughter cell receives a centrosome
(the former spindle pole) in association with its chromosomes.

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Centriole Replication. At a certain point in G 1 phase the two centrioles separate by a few
micrometers. During S phase a daughter centriole begins to grow near the base of each old
centriole and at a right angle to it, the elongation being completed by G 2 phase. The two
centriole pairs remain close together in a single centrosomal complex until the beginning
of M phase, when the centrosome splits in two and the two halves begin to separate.

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