Cytoskeleton

A cytoskeleton is present in all cells of all domains of life (archaea,

bacteria, eukaryotes). It is a complex network of interlinking filaments
Cell biology
and tubules that extend throughout the cytoplasm, from the nucleus to The animal cell
the plasma membrane.[1] The cytoskeletal systems of different
organisms are composed of similar proteins. In eukaryotes, the
cytoskeletal matrix is a dynamic structure composed of three main
proteins, which are capable of rapid growth or disassembly dependent on
the cell's requirements at a certain period of time.[2]

The structure, function and dynamic behavior of the cytoskeleton can be

very different, depending on organism and cell type.[3][4] Even within
one cell the cytoskeleton can change through association with other
proteins and the previous history of the network.[5] Components of a typical animal cell:

A multitude of functions can be performed by the cytoskeleton. Its 1. Nucleolus

primary function would arguably be to give the cell its shape and
2. Nucleus
mechanical resistance to deformation,[3] and through association with
3. Ribosome (little dots)
extracellular connective tissue and other cells it stabilizes entire
tissues.[3][6] The cytoskeleton can also contract, thereby deforming the 4. Vesicle
cell and the cell's environment and allowing cells to migrate.[5] 5. Rough endoplasmic reticulum
Moreover, it is involved in many cell signaling pathways: in the uptake 6. Golgi apparatus (or "Golgi body")
of extracellular material (endocytosis),[7] segregates chromosomes 7. Cytoskeleton
during cellular division,[3] is involved in cytokinesis (the division of a
8. Smooth endoplasmic reticulum
mother cell into two daughter cells),[4] provides a scaffold to organize
the contents of the cell in space [5] and for intracellular transport (for
9. Mitochondrion
example, the movement of vesicles and organelles within the cell);[3] 10. Vacuole
and can be a template for the construction of a cell wall.[3] Furthermore, 11. Cytosol (fluid that contains organelles,
it forms specialized structures, such as flagella, cilia, lamellipodia and comprising the cytoplasm)
podosomes. 12. Lysosome

A large-scale example of an action performed by the cytoskeleton is 13. Centrosome

muscle contraction. In the muscle, there are groups of highly specialized 14. Cell membrane
cells that work together to perform a function known as muscle
contraction. A main component in the cytoskeleton that helps show the true function of this muscle contraction is known as a
microfilament. Microfilaments are composed of the most abundant cellular protein known as actin.[8] During contraction of amuscle,
within each muscle cell,myosin molecular motors collectively exert forces on parallel actin filaments. Muscle contraction starts from
nerve impulses which then causes increased amounts of calcium to be released from the sarcoplasmic reticulum. Increases in calcium
in the cytosol allows muscle contraction to begin with the help of two proteins, tropomyosin and troponin.[8] Tropomyosin inhibits
the interaction between actin and myosin, while troponin senses the increase in calcium and releases the inhibition.[9] This action
contracts the muscle cell, and through the synchronous process in many muscle cells, the entire muscle.

Contents
History
Eukaryotic cytoskeleton
 Microfilaments (actin filaments)
Intermediate filaments
Microtubules
Comparison
Septins
Spectrin
Yeast cytoskeleton
Prokaryotic cytoskeleton
FtsZ
MreB and ParM
Crescentin
Common features and differences between prokaryotes and eukaryotes
Cytoplasmic streaming
See also
References
External links The eukaryotic cytoskeleton. Actin filaments are
shown in red, and microtubules composed of beta
tubulin are in green.
History
In 1903, Nikolai K. Koltsov proposed that the shape of cells was determined by a network of tubules that he termed the cytoskeleton.
The concept of a protein mosaic that dynamically coordinated cytoplasmic biochemistry was proposed by Rudolph Peters in 1929[10]
while the term (cytosquelette, in French) was first introduced by French embryologistPaul Wintrebert in 1931.[11]

When the cytoskeleton was first introduced, it was thought to be an uninteresting gel-like substance that helps organelles stay in
place.[12] Much research took place to try to understand the purpose of the cytoskeleton and its components. With the help of Stuart
Hameroff and Roger Penrose, they discovered that microtubules vibrate within neurons in the brain which suggest that brain waves
come from deeper microtubule vibrations.[13] This discovery showed that the cytoskeleton is not just a gel like substance but it
actually has a purpose.

Initially, it was thought that the cytoskeleton was exclusive to eukaryotes but in 1992, it was discovered to be present in prokaryotes
as well. This discovery came after the realization that bacteria possess proteins that are homologous to tubulin and actin; the main
components of the eukaryotic cytoskeleton.[14]

Eukaryotic cytoskeleton
Eukaryotic cells contain three main kinds of cytoskeletal filaments:
microfilaments, microtubules, and intermediate filaments. Each
cytoskeletal filament type is formed by polymerization of a distinct
type of protein subunit and has its own characteristic shape and
intracellular distribution. Microfilaments are polymers of the protein
actin and are 7 nm in diameter. Microtubules are composed of tubulin
and are 25 nm in diameter. Intermediate filaments are composed of
various proteins, depending on the type of cell in which they are
found; they are normally 8-12 nm in diameter.[1] The cytoskeleton
provides the cell with structure and shape, and by excluding
macromolecules from some of the cytosol, it adds to the level of
macromolecular crowding in this compartment.[15] Cytoskeletal
Actin cytoskeleton of mouse embryo fibroblasts,
elements interact extensively and intimately with cellular stained with phalloidin
membranes.[16]
Neurodegenerative disorders have recently become more understood in context to what parts of the cell they affect. Diseases, such as
Parkinson's disease, Alzheimer's disease, Huntington's disease, and amyotrophic lateral sclerosis (ALS) have had breakthrough
research that supports the conclusion that neurodegenerative diseases affect the cytoskeleton. Parkinson's disease is a condition that
causes the degradation of neurons, resulting in tremors, rigidity, and other non-motor symptoms. Research has found evidence that
microtubule assembly and stability in the cytoskeleton is compromised causing the neurons to degrade over time.[17] Alzheimer's
disease is much like Parkinson's in that it is also a neurodegenerative disease that affects the cytoskeleton. Tau proteins, which
stabilize microtubules, malfunction in patient's affected by Alzheimers, causing pathology with the cytoskeleton.[18] Huntington's
disease has also been found to affect the cytoskeleton of cells by excess glutamine in the Huntington protein, which is involved with
linking vesicles to the cytoskeleton. An error with this protein is proposed to be a factor in the development of the disease.[19] A
fourth neurodegenerative disorder is amyotrophic lateral sclerosis, or ALS, which causes a loss of movement by the degradation of
motor neurons from defects of the cytoskeleton.[20]

A number of small-molecule cytoskeletal drugs have been discovered that interact with actin and microtubules. These compounds
have proven useful in studying the cytoskeleton and several have clinical applications.

All filaments interact with accessory proteins that regulate and link the filaments to other cell compounds and each other. The
accessory proteins are essential for controlled assembly of cytoskeletal filaments in particular locations, and they include motor
proteins.[21]

Microfilaments (actin filaments)

Microfilaments are composed of linear polymers of G-actin proteins, and generate force when the growing (plus) end of the filament
pushes against a barrier, such as the cell membrane. They also act as tracks for the movement of myosin molecules that affix to the
microfilament and "walk" along them. In general, the major component or protein of microfilaments are actin. The G-actin monomer
combines to form a polymer which continues to form the microfilament (actin filament). These subunits then assemble into two
chains that intertwine into what is called, F-actin chains.[22] Myosin motoring along F-actin filaments generates contractile forces in
so-called actomyosin fibers, both in muscle as well as most non-muscle cell types.[23] Actin structures are controlled by the Rho
family of small GTP-binding proteins such as Rho itself for contractile acto-myosin filaments ("stress fibers"), Rac for lamellipodia
and Cdc42 for filopodia.

Functions include:

Muscle contraction
Cell movement
Intracellular transport/trafficking
Maintenance of eukaryotic cell shape
Cytokinesis
Cytoplasmic streaming[22]

Intermediate filaments
Intermediate filaments are a part of the cytoskeleton of many eukaryotic cells. These filaments, averaging 10 nanometers in diameter,
are more stable (strongly bound) than actin filaments, and heterogeneous constituents of the cytoskeleton. Like actin filaments, they
function in the maintenance of cell-shape by bearing tension (microtubules, by contrast, resist compression but can also bear tension
during mitosis and during the positioning of the centrosome). Intermediate filaments organize the internal tridimensional structure of
the cell, anchoring organelles and serving as structural components of the nuclear lamina. They also participate in some cell-cell and
cell-matrix junctions. Nuclear lamina exist in all animals and all tissues. Some animals like the fruit fly do not have any cytoplasmic
intermediate filaments. In those animals that express cytoplasmic intermediate filaments, these are tissue specific.[6] Keratin
intermediate filaments in epithelial cells provide protection for different mechanical stresses the skin may endure. They also provide
protection for organs against metabolic, oxidative, and chemical stresses. Strengthening of epithelial cells with these intermediate
[24]
filaments may prevent onset ofapoptosis, or cell death, by reducing the probability of stress.
Intermediate filaments are most commonly known as the support system or
“scaffolding” for the cell and nucleus while also playing a role in some cell functions. In
combination with proteins and desmosomes, the intermediate filaments form cell-cell
connections and anchor the cell-matrix junctions that are used in messaging between
cells as well as vital functions of the cell. These connections allow the cell to
communicate through the desmosome of multiple cells to adjust structures of the tissue
based on signals from the cells environment. Mutations in the IF proteins have been
shown to cause serious medical issues such as premature aging, desmin mutations
compromising organs, Alexander Disease, and muscular dystrophy.[25]

Different intermediate filaments are:

Microscopy of keratin filaments
made of vimentins. Vimentin intermediate filaments are in general present inside cells
in mesenchymal cells.
made of keratin. Keratin is present in general in epithelial cells.
neurofilaments of neural cells.
made of lamin, giving structural support to the nuclear envelope.
[26]
made of desmin, play an important role in structural and mechanical support of muscle cells.

Microtubules
Microtubules are hollow cylinders about 23 nm in diameter (lumen = approximately
15 nm in diameter), most commonly comprising 13 protofilaments that, in turn, are
polymers of alpha and beta tubulin. They have a very dynamic behavior, binding GTP
for polymerization. They are commonly organized by the centrosome.

In nine triplet sets (star-shaped), they form the centrioles, and in nine doublets oriented
about two additional microtubules (wheel-shaped), they form cilia and flagella. The
latter formation is commonly referred to as a "9+2" arrangement, wherein each doublet
is connected to another by the protein dynein. As both flagella and cilia are structural
components of the cell, and are maintained by microtubules, they can be considered part Microtubules in a gel-fixated cell
of the cytoskeleton. There are two types of cilia: motile and non-motile cilia. Cilia are
short and more numerous than flagella. The motile cilia have a rhythmic waving or
beating motion compared to the non-motile cilia which receive sensory information for the cell; processing signals from the other
cells or the fluids surrounding it. Additionally, the microtubules control the beating (movement) of the cilia and flagella.[27] Also, the
dynein arms attached to the microtubules function as the molecular motors. The motion of the cilia and flagella is created by the
microtubules sliding past one another, which requires ATP.[27] They play key roles in:

intracellular transport (associated with dyneins andkinesins, they transport organelles like mitochondria or vesicles).
the axoneme of cilia and flagella.
the mitotic spindle.
synthesis of the cell wall in plants.
In addition to the roles described above, Stuart Hameroff and Roger Penrose have
[28]
proposed that microtubules function in consciousness.

Comparison

Cross section diagram through

the cilium shows the “9 + 2”
arrangement of microtubules.
 Cytoskeleton Diameter
Structure Subunit examples[29]
type[29] (nm)[30]
Microfilaments 6 double helix actin

vimentin (mesenchyme)
glial fibrillary acidic protein
Intermediate (glial cells)
10 two anti-parallel helices/dimers, forming tetramers neurofilament proteins
filaments
(neuronal processes)
keratins (epithelial cells)
nuclear lamins

protofilaments, in turn consisting of tubulin

Microtubules 23 α- and β-tubulin
subunits in complex withstathmin[31]

Septins
Septins are a group of the highly conservedGTP binding proteins found ineukaryotes. Different septins form protein complexes with
each other. These can assemble to filaments and rings. Therefore, septins can be considered part of the cytoskeleton.[32] The function
of septins in cells include serving as a localized attachment site for other proteins, and preventing the diffusion of certain molecules
from one cell compartment to another.[32] In yeast cells, they build scaffolding to provide structural support during cell division and
compartmentalize parts of the cell. Recent research in human cells suggests that septins build cages around bacterial pathogens,
[33]
immobilizing the harmful microbes and preventing them from invading other cells.

Spectrin
Spectrin is a cytoskeletal protein that lines the intracellular side of the plasma membrane in eukaryotic cells. Spectrin forms
pentagonal or hexagonal arrangements, forming a scaffolding and playing an important role in maintenance of plasma membrane
integrity and cytoskeletal structure.[34]

Yeast cytoskeleton
In budding yeast (an important model organism), actin forms cortical patches, actin cables, and a cytokinetic ring and the cap.
Cortical patches are discrete actin bodies on the membrane and are vital for endocytosis, especially the recycling of glucan synthase
which is important for cell wall synthesis. Actin cables are bundles of actin filaments and are involved in the transport of vesicles
towards the cap (which contains a number of different proteins to polarize cell growth) and in the positioning of mitochondria. The
cytokinetic ring forms and constricts around the site ofcell division.[35]

Prokaryotic cytoskeleton
Prior to the work of Jones et al., 2001, the cell wall was believed to be the deciding factor for many bacterial cell shapes, including
rods and spirals. When studied, many misshapen bacteria were found to have mutations linked to development of a cell envelope.[36]
The cytoskeleton was once thought to be a feature only of eukaryotic cells, but homologues to all the major proteins of the eukaryotic
cytoskeleton have been found in prokaryotes.[37] Harold Erickson notes that before 1992, only eukaryotes were believed to have
cytoskeleton components. However, research in the early '90s suggested that bacteria and archaea had homologues of actin and
tubulin, and that these were the basis of eukaryotic microtubules and microfilaments.[38] Although the evolutionary relationships are
so distant that they are not obvious from protein sequence comparisons alone, the similarity of their three-dimensional structures and
similar functions in maintaining cell shape and polarity provides strong evidence that the eukaryotic and prokaryotic cytoskeletons
are truly homologous.[39] Three laboratories independently discovered that FtsZ, a protein already known as a key player in bacterial
cytokinesis, had the "tubulin signature sequence" present in all α-, β-, and γ-tubulins.[38] However, some structures in the bacterial
[23][40]
cytoskeleton may not have been identified as of yet.
FtsZ
FtsZ was the first protein of the prokaryotic cytoskeleton to be identified. Like tubulin, FtsZ forms filaments in the presence of
guanosine triphosphate (GTP), but these filaments do not group into tubules. During cell division, FtsZ is the first protein to move to
the division site, and is essential for recruiting other proteins that synthesize the new
cell wall between the dividing cells.

MreB and ParM

Prokaryotic actin-like proteins, such as MreB, are involved in the maintenance of cell shape. All non-spherical bacteria have genes
encoding actin-like proteins, and these proteins form a helical network beneath the cell membrane that guides the proteins involved in
cell wall biosynthesis.[41]

Some plasmids encode a separate system that involves an actin-like protein ParM. Filaments of ParM exhibitdynamic instability, and
may partition plasmid DNA into the dividing daughter cells by a mechanism analogous to that used by microtubules during
eukaryotic mitosis.[23][42]

Crescentin
The bacterium Caulobacter crescentus contains a third protein, crescentin, that is related to the intermediate filaments of eukaryotic
cells. Crescentin is also involved in maintaining cell shape, such as helical and vibrioid forms of bacteria, but the mechanism by
which it does this is currently unclear.[43] Additionally, curvature could be described by the displacement of crescentic filaments,
after the disruption of peptidoglycan synthesis.[44]

Common features and differences between prokaryotes and

eukaryotes
By definition, the cytoskeleton is composed of proteins that can form longitudinal arrays (fibres) in all organisms. These filament
forming proteins have been classified into 4 classes. Tubulin-like, actin-like, Walker A cytoskeletal ATPases (WACA-proteins), and
intermediate filaments.[4][23]

Tubulin-like proteins are tubulin in eukaryotes and FtsZ, TubZ, RepX in prokaryotes. Actin-like proteins are actin in eukaryotes and
MreB, FtsA in prokaryotes. An example of a WACA-proteins, which are mostly found in prokaryotes, is MinD. Examples for
intermediate filaments, which have almost exclusively been found in animals (i.e. eukaryotes) are the lamins, keratins, vimentin,
neurofilaments, and desmin.[4]

Although tubulin-like proteins share some amino acid sequence similarity, their equivalence in protein-fold and the similarity in the
ATP binding domain.[4][23]
GTP binding site is more striking. The same holds true for the actin-like proteins and their structure and

Cytoskeletal proteins are usually correlated with cell shape, DNA segregation and cell division in prokaryotes and eukaryotes. Which
proteins fulfill which task is very different. For example, DNA segregation in all eukaryotes happens through use of tubulin, but in
prokaryotes either WACA proteins, actin-like or tubulin-like proteins can be used. Cell division is mediated in eukaryotes by actin,
but in prokaryotes usually by tubulin-like (often FtsZ-ring) proteins and sometimes (Crenarchaeota) ESCRT-III, which in eukaryotes
still has a role in the last step of division.[4]

Cytoplasmic streaming
Cytoplasmic streaming, also known as cylcosis, is the active movement of a cell’s contents along the components of the cytoskeleton.
While mainly seen in plants, all cell types use this process for transportation of waste, nutrients, and organelles to other parts of the
cell. [45] Plant and algae cells are generally larger than many other cells; so cytoplasmic streaming is important in these types of cells.
This is because the cell’s extra volume requires cytoplasmic streaming in order to move organelles throughout the entire cell.[46]
Organelles move along microfilaments in the cytoskeleton driven by myosin motors binding and pushing along actin filament
bundles.[45]

See also
Cell (biology)
Organelle
Nuclear matrix
Microfilament
Cell cortex

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External links
Cytoskeleton Monthly News and Blog
MBInfo - Cytoskeleton Dynamics
Cytoskeleton, Cell Motility and Motors - The V irtual Library of Biochemistry, Molecular Biology and Cell Biology
Cytoskeleton database, clinical trials, recent literature, lab registry ...
Animation of leukocyte adhesion(Animation with some images of actin and microtubule assembly and dynamics.)
http://cellix.imba.oeaw.ac.at/ Cytoskeleton and cell motility including videos
Open access review articleon the emergent complexity of the cytoskeleton (appeared inAdvances in Physics, 2013)

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