CYTOSKELETON

In addition to the membrane-enclosed organelles, the cytoplasm of most cells contains a variety of protein filamentous networks. DEFINITION : Cells have a cytoskeleton, a network made of interconnected filaments and microtubules in the cytoplasm along with proteins that anchor them and tie them together. The name cytoskeleton is convenient in that it allows us to compare the cytoskeleton to our bones and muscles. Bones and muscles give us structure and produce movement. Similarly, the elements of the cytoskeleton maintain cell shape and allow the cell and its contents to move. Some cells move by using cilia and flagella, which are made up of microtubules. In addition, proteins and organelles move along microtubules and microfilaments from one part of the cell to another propelled by molecular motors. FUNCTION: • • • • • • • Shape, integrity and rigidity of the cell Mechanical strength Large scale movements of cell along a surface Contraction of muscle cells Intracellular transport of organelles and vesicles, cytoplasmic streaming Segregation of chromosomes during mitosis Pinching apart of animal cells (cytokinesis)

There are three classes of cytoskeletal filaments, based on their diameter and the types of protein they contain. In order of size, starting with the thinnest, they are (1) microfilaments (Actin filaments), (2) intermediate filaments, and (3) microtubules. Microfilaments and microtubules can be assembled and disassembled rapidly, allowing a cell to alter these components of its cytoskeletal framework according to changing requirements. In contrast, intermediate filaments, once assembled, are less readily disassembled. The molecules that make up the three filament systems have been highly conserved throughout evolution; the cytoskeletal proteins present in the cells of complex organisms such as humans are much the same as those in a simple organism such as a yeast. Although the individual molecules making up the cytoskeleton are below the limit of resolution of the light microscope, the

This gives the microtubule an built-in molecular polarity. γ-tubulin. and lost from. By convention. They are made up of two globular protein subunits. Tubulin subunits are added to. The tubules also contain other proteins that facilitate their formation. ( Microtubules radiate from the centrosome).cytoskeleton itself can be readily observed within the cell by using fluorescence microscopy MICROTUBULES : STRUCTURE: Microtubules are long. The α and β subunits form heterodimers (known as protofilaments) . which aggregate to form long tubes made up of stacked rings. A third subunit. hollow cylinders with 5-nm walls made up of 13 longitudinal rows(protofilaments) of the globular protein tubulin surrounding a cavity 15 nm in diameter. one end much more rapidly than the other. does not itself contribute to microtubule structure but which is found at the centrosome and plays a role in initiating microtubule assembly. α β α β and so on. Within each protofilament the tubulin dimers are arranged in a “head-to tail” manner. α. with each ring usually containing 13 subunits. the fast growing end is referred to as the (+) end and the slow .and β-tubulin.

The microtubule network (the minus end – ALPHA monomer) begins in the nucleus at the centriole and extends outward to the plasma membrane (usually the plus end. sometimes disappearing completely. Therefore in a protofilament. As GTP is . This phenomenon is referred to as dynamic instability.growing end as the (−) end. Tubulin polymerises end to end with the alpha subunit of one dimer coming in contact with the beta subunit of the next. which creates a conformational change in the dimer that favors addition of dimers to the tubulin polymer and arrange themselves to an imperfect helix. The – end is capped thus leaving out only the + end from where elongation can occur. Individual microtubules undergo periods of slow growth followed by rapid shrinkage.and + ends). but the end to which they add more rapidly (the plus end) has a net rate of growth. Microtubule assembly is regulated by the centrosome which lies near the nucleus. The dimer bind GTP.and β-tubulin [GTP not marked – For exams mark GTP GDP dissociation] FORMATION: Remarkably. (.end. Tubulin dimers composed of one alpha and one beta subunit polymerise end to end. and the end where disassembly predominates is the .BETA monomer). The end where assembly predominates is called the + end. while there will be an exposed beta subunit at the other end. one end ll have an exposed alpha subunit. Both processes occur simultaneously in vitro. The assembly of microtubules is facilitated by warmth and various other factors. A striking feature that aids in microtubule function is its peculiar polarity. microtubules can assemble and disassemble. and the end to which they add more slowly (the minus end) has a net rate of loss. The protofilaments bundle in a parallel manner to one another so in a microtubule there is one + end where only beta subunits are exposed while at the – end only alpha subunits. Figure : Assembly and disassembly of a microtubule by aggregation and disaggregation of dimers made up of α. The dimers can add to and dissociate from both ends of the tubulin. and disassembly is facilitated by cold and other factors.

2. Form the spindle. Present in all nucleated cells and the platelets in blood. 3. GTP hydrolyses on beta tubulin. In plants direct the deposition of cellulose fibers on the outside of the cell membrane. Centrosome is known as the microtubule organising centre. which moves the chromosomes in mitosis. organelles such as secretory granules. Microtubule-associated proteins (MAPs) attach microtubules to other cellular components. They contain a pair of centrioles. Centrioles have a characteristic nine-way pattern that we will meet again in cilia and flagella. microtubules are a dynamic portion of the cell skeleton. A microtubule is stable when capped with GTP bound tubulins and unstable with GDP tubulin caps. creates a core of less stable GDP tubulin. After incorporation. responsible for positioning of organelles. In animals. lying immediately beneath the cell membrane. oriented at right angles to the direction of cell expansion FUNCTIONS: Because of their constant assembly and disassembly. Microtubules in plant cells have a quite different organization. the binding of tubulin subunits is weakened. GTP bound alpha tubulin is more stable than GTP bound beta tubulin. The GTP cap model of instability : 1. • • • • • • They can form bundles of rigid fibers that helps to maintain shape and gives mechanical strength to the cells. basal bodies and centrioles – responsible for motility.hydrolyzed to GDP. Microtubules can transport in both directions. 4. Vesicles get attached to MAPs and move along microtubule conveyor belt. Essential component of cilia. resulting in their dissociation (dynamic instability). provide the tracks for transport of vesicles. DYNAMIC INSTABILTY : See definition above. Loss of the cap causes the dissociation. . the net rate and direction of growth is dictated by the fastest growing end of the microtubule. flagella. and mitochondria from one part of the cell to another. Thus. and can determine cell shape and polarity.

They are also involved in the positioning of the Golgi complex and the movement of chromosomes during mitosis. Cytoplasmic dyneins are huge proteins that move vesicles and organelles to the minus end. The anticancer drug paclitaxel (Taxol) binds to microtubules and makes them so stable that organelles cannot move. Microvilli. Both proteins consist of a tail that binds to the cargo to be transported and two (kinesin) or three (dynein) globular heads that interact with the surface of the microtubule. . vesicles. Organelles. extremely thin fibres of about 5nm diameter composed of actin monomers that usually occur in bundles or other groupings. Actin filaments have been isolated from various types of cells. which project from certain cells and can shorten and extend. Kinesins moves molecules. and the cells die. generating movement. The microfilament of ectoplasm contains only actin where as of endoplasm contains both actin and myosin. MICROFILAMENTS: They are long. contain actin filaments. This is subdivided into outward or anterograde transport [by kinesin] and inward or retrograde [by dynein] transport. small vesicles. In nerve cells. generally toward the nucleus. and even mRNA are transported in both directions in a phenomenon referred to as axonal transport. Both are dependent upon microtubule molecular motors that are abundant in nerve cells. especially those in which movement occurs. It is seen particularly clearly in some specialized cell types such as the pigment cells called chromatophores in the skin of fish and amphibia.Eg :) HMW (High Molecular weight proteins) include MAP –I and MAP-II Tau proteins FUNCTIONS OF MAPs: Stability to the tubulins Inhibits dissociation of tubulin Role of Microtubules in Intracellular transport: Motility is a general property of microtubules within cells. Microtubule assembly is prevented by colchicine and vinblastine. Specificity is imparted to this process by having multiple dyneins and kinesins in a single cell. The inward and outward movement of pigment granules along radial arrays of microtubules underlies the remarkable color changes such animals are able to display. usually toward the plasma membrane. and organelles toward the plus end of microtubules. KINESINS AND DYNEINS: Motor proteins called kinesins and cytoplasmic dyneins use ATP energy to move cargo along the microtubules. Mitotic spindles cannot form. each responsible for transporting a specific type of cargo.

Because it is a globular protein. NOTE : Cells are anchored to the extracellular matrix through transmembrane proteins such as integrins.abundant in the lamellipodia that cells put out when they crawl along surfaces Help in movement of microvilli as they reach to the tips of the microvilli on the epithelial cells of the intestinal mucosa. providing structural strength at the edges by its interaction with myosin brings about contraction of muscle.end). the long filamentous chains that are the microfilaments. They also depolymerize in vivo. as in microtubules) and depolymerization at the other (the .Actin filaments. like microtubules. like microtubules. present in all types of cells. actin is particularly associated with the cell periphery. Each actin filament is composed of two chains of actin monomers twisted around one another like two strands of beads. Links transmembrane proteins to cytoplasmic proteins Anchors the centrosomes at opposite poles of cell during mitosis Pinches dividing animal cells apart during cytokinesis Generate cytoplasmic streaming in some cells Generate locomotion in cells such as WBC. forming long filaments of diameter only 5 nm. the actin monomer is designated G – actin while the filament that forms from it is referred to as F-actin. can assemble and disassemble. with polymerization often occurring at one end of a microfilament (the + end. can assemble and disassemble. Actin filaments. The actin filaments interact with integrin receptors and form focal adhesion complexes which serve as points of traction with the surface over which the cell pulls itself. These are dimeric proteins that have an extracellular . amoeba . Actin and tubulin polymerize by similar mechanism :  Grow by addition of monomers  Rate of growth faster at the plus end  Naked actin or tubulin filaments (without ABP’s or MAP’s) are highly unstable and can disassemble from both ends  Actin is formed by ATP hydrolysis while Tubulin by GTP hydrolysis FUNCTIONS: • • • • • • • • • In animal cells. The actin molecules (G-actin) polymerize in vivo to form F-actin. It is the most abundant protein in mammalian cells. STRUCTURE: Structure is highly conserved.

• • • TYPES OF INTERMEDIATE FILAMENTS : Although assembled from a variety of IF proteins. and makes the horns and hooves of our domestic animals and pets. Alpha-actinin. fimbrin. antistress (as they form stable bundles) They form flexible scaffolding for the cell and help it resist external pressure. and when they are abnormal in humans. Mostly found in all animal cells but not in fungi & plant cells. cells rupture more easily. Generally 8-14 nm in diameter and are made up of various subunits. filaments appear similar in the electron microscope. forms our hair and finger nails.actin .domain that binds to collagen and other extracellular matrix proteins and an intracellular domain that attaches to actin microfilaments on the inside • Anchoring cell junctions (In adherens junctions the cell adhesion molecules are linked to actin microfilaments by linking proteins such as catenin) ACTIN BINDING PROTEINS (ABP’S) : Proteins that bind to actin through the actin binding domain on their structure. FUNCTIONS OF ABP’s : 1. distriphin. Acidic Keratins Together known as Tonofilaments. filaments composed of keratin. Controls the equilibrium between F-actin and G. Some of these filaments connect the nuclear membrane to the cell membrane. They are extremely stable (Unlike the other two) FUNCTIONS: • • Mechanincal support to cells. blistering of the skin is common. Produced by epithelial cells. . five types exist: 1. eutrophin.e. INTERMEDIATE FILAMENTS: Intermediate filaments differ in structure and function. all inter. Anchoring cell junctions (In desmosomes the cell adhesion molecules are linked to intermediate filaments) Bind cytoskeletal elements such as microfilaments and microtubules to the plasma membrane. (Less well understood compared to other two ). Stability to Microfilaments 2.i. Basic keratins protein that gives our skin its protective coating. In their absence. Eg :) Thymosin. the 2. affects the formation of microfilaments.

2 micrometer in diameter. Neurofilaments – Nerve cells contain neurofilaments [Type H. 5. This 9+2 arrangement and its associated structure constitutes the axoneme. and glial cells contain glial filaments. Provides structural stability CILIA & FLAGELLA – CELLULAR MOTILITY ORGANELLES Cilium means ‘eyelash’ Cilia are movable organelles that are 5-10 micrometre long and 0. . 4. Each cilium is surrounded by the plasma membrane and contains a central doublet of microtubules surrounded by nine pairs of fused microtubules. endothelial cells and leukocytes contain vimentin filaments. Nuclear lamins – Underlies and strengthens the nuclear envelope in all eukaryotic cells. Lamins are present in nucleus while others in the plasma membrane of the cell. plakoglobin 1. phakinins etc. female reproductive tract. plectin. They are present on the apical epithelial surfaces of the respiratory tract.3. The axoneme is enclosed by an extension of the cell membrane. filensins. also includes internexins. INTERMEDIATE FILAMENT ASSOCIATED PROTEINS [IFAP’S]: Eg :) Filaggrin. M or L : Heavy. Mediates the organization of various types of IF into networks 2. nuclear lamins reinforce and helps reformation of the nuclear envelope after cell division. STRUCTURE: Cilia are visible in the light microscope however the complex internal structure is revealed only when viewed through the electron microscope. fibroblasts. sensory organs etc. Lamins are expressed in all cells while others show tissue specific expression. Medium or Low depending upon the molecular weight]. Vimentin-like-proteins muscle cells contain desmin filaments.

auditory and visual epithelia) they help in the reception of senses by forming chemoreceptors. The subunit A outer and inner arms contain ATPase motor protein dynein converts the energy released byATP hydrolysis into the mechanical work of ciliary and flagellar beating • • FUNCTIONS: Cilia bend as microtubules in the axoneme slide past one another. This motion is driven by ATP hydrolysis caused by dynein.• T h e central pair is two complete microtubules connected by a cm bridge and surrounded by a central sheath • Each of the nine outer pairs of doublets consists of a complete microtubule called subunit A and an incomplete microtubule called subunit B. a radial spoke with a spoke head also projects from subunit A towards the central sheath. Projecting from subunit A are an hooked outer arm and an angled inner arm. larynx. . each complete microtubule appears to be formed from a ring of 13 subunits while the incomplete subunit is formed from only 11. mechanoreceptors and photoreceptors.( olfactory. In transverse sections. which abuts on subunit A. • • • In the respiratory tract. they propel ova and mucus through the system (uterine tubes and uterus) In the sensory organs. they propel mucus and debris out of the system (nasal cavities. trachea and bronchi) In the female reproductive tract.

MECHANISM OF MOVEMENT : The real difference between cilia and flagella lies in the nature of their movement. for example. sliding is converted into bending. which is absent in cilia and they provide rigidity. Like the propeller of a boat. perpendicular to the surface of the cell. Flagella wriggle like eels. The bacterial flagellum itself is a specialized piece of extracellular cell wall. They generate waves that pass along their length. Cilia usually present in large numbers (100’s) while flagella are usually single or paired. each outer doublet has a large electron dense outer fibre. The movement is biphasic. usually from base to tip at constant amplitude. Using ATP produced by mitochondria near the base of the cilium as fuel. In the spermatozoan flagella. . consisting of an effective stroke in which the cilium is held rigid and bends only at its base and a recovery stroke in which the bend formed at the base passes out to the tip. the dynein arms push on the adjacent outer doublets. Thus the movement of water by a flagellum is parallel to its axis while a cilium moves water perpendicular to its axis and. FLAGELLA: Flagellum means ‘whip’ Same as cilia in internal structure however they are much longer.• Protist movement Eg:) Swimming of paramaecium MECHANISM OF MOVEMENT: Cilia row like oars. made of one protein (flagellin) that has no similarity to tubulin or dynein. forcing a sliding movement to occur between adjacent outer doublets. spermatozoan flagella are about 50 micrometer long. the motion of the bacterial flagellum is entirely driven by the rotary motor at its base. Length varies from cell to cell. Because the arms are activated in a strict sequence both around and along the axoneme and because the amount of sliding is restricted by the radial spokes and interdoublet links. hence.

which contains a pair of centrioles.BASAL BODIES: Organelles that anchors each cilium to the cell’s apical surface in ciliated epithelia. It also has electron dense pericentriolar satellites that radiate away from the triplets like the vanes of a pinwheel. centrioles replicate and then become concentrated in the apical surface. however basal bodies have nine peripheral triplets of microtubules rather than doublets. Then centrioles form a microtubule containing mitotic spindle that moves chromosomes during mitosis. It is assumed that centrioles probably produce basal bodies which in turn probably produce a ciliary projection. . In ciliated epithelia. CENTRIOLES: Many cells have a perinuclear centrosome. The arrangement of microtubules in basal bodies are similar to that of cilia. Each centriole has nine peripheral microtubule triplets but lacks a central pair. Striated bundles of fibres called rootlets anchor basal bodies to the surrounding cytoplasm. HAVE NOT INCLUDED ERYTHROCTE CYTOSKELETON [FIGURE REQUIRED] AND A FEW OTHER PORTIONS FOR WHICH NOTES ARE THERE IN THE QUESTION BANK IF POSSIBLE WATCH ANY ANIMATION RELATED TO THE CILIARY ROWING MOVEMENT AND FLAGELLAR BEATING TO UNDERSTAND THE DIFFERENCE. They are paired during interphase and during cell division. centrioles separate and migrate to the poles of the cell. and the ciliary central doublet terminates where the cilia joins the basal bodies.

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