Microtubulation

Maaloum M, Chretien D, Karsenti E and FIdrber J K FI 1994 Approaching microtubule structure with the scanning tunnelling microscope (STM) J. Ceii Sc/. 107 part II 3127... 

Vale R D, Funatsu T, Pierce D W, Romberg L, Harada Y and Yanagida T 1996 Direct observation of single kinesin molecules moving along microtubules/Vafuro 380 451-3... 

Although the compounds were isolated in quantities of only a few milligrams per kilogram of cmde plant leaves, extensive work on a variety of animal tumor systems led to eventual clinical use of these bases, first alone and later in conjunction with other materials, in the treatment of Hodgkin s disease and acute lymphoblastic leukemia. Their main effect appears to be binding tightly to tubuHn, the basic component of microtubules found in eukaryotic cells, thus interfering with its polymerization and hence the formation of microtubules required for tumor proliferation (82). 

The influences of herbicides on cell division fall into two classes, ie, dismption of the mitotic sequence and inhibition of mitotic entry from interphase (G, S, G2). If ceU-cycle analyses indicate increases in abnormal mitotic figures, combined with decreases in one or more of the normal mitotic stages, the effect is upon mitosis. Mitotic effects usually involve the microtubules of the spindle apparatus in the form of spindle depolymerization, blocked tubulin synthesis, or inhibited microtubule polymerization (163). Alkaloids such as colchicine [64-86-8J,viahla.stiae [865-21-4] and vincristine [57-22-7] dismpt microtubule function (164). Colchicine prevents microtubule formation and promotes disassembly of those already present. Vinblastine and vincristine also bind to free tubulin molecules, precipitating crystalline tubulin in the cytoplasm. The capacities of these dmgs to interfere with mitotic spindles, blocking cell division, makes them useful in cancer treatment. 

Microfilaments and Microtubules. There are two important classes of fibers found in the cytoplasm of many plant and animal ceUs that are characterized by nematic-like organization. These are the microfilaments and microtubules which play a central role in the determination of ceU shape, either as the dynamic element in the contractile mechanism or as the basic cytoskeleton. Microfilaments are proteinaceous bundles having diameters of 6—10 nm that are chemically similar to actin and myosin muscle ceUs. Microtubules also are formed from globular elements, but consist of hoUow tubes that are about 30 nm in diameter, uniform, and highly rigid. Both of these assemblages are found beneath the ceU membrane in a linear organization that is similar to the nematic Hquid crystal stmcture. 

Proteins can be broadly classified into fibrous and globular. Many fibrous proteins serve a stmctural role (11). CC-Keratin has been described. Fibroin, the primary protein in silk, has -sheets packed one on top of another. CoUagen, found in connective tissue, has a triple-hehcal stmcture. Other fibrous proteins have a motile function. Skeletal muscle fibers are made up of thick filaments consisting of the protein myosin, and thin filaments consisting of actin, troponin, and tropomyosin. Muscle contraction is achieved when these filaments sHde past each other. Microtubules and flagellin are proteins responsible for the motion of ciUa and bacterial dageUa. 

It iaterferes with the synthesis of the hyphal walls, the biosynthesis of nucleic acids, and the synthesis of chitin. The iateraction with microtubules has also been described. The sensitivity of a cell seems to depend particularly on the abiUty to form griseofulvin—nucleic acid complexes. Further information concerning griseofulvin is available (21). 

The precise description of geometrical structures of CNTs has been reported by lijima [1], who was the first discoverer of carbon microtubules. Electron diffraction (ED) results are presented in Chap. 3. In this chapter, the authors will focus on the electronic structures of CNTs from the viewpoint of EELS by using TEM equipped with an energy-filter in the column or under the column. 

Certain proteins endow cells with unique capabilities for movement. Cell division, muscle contraction, and cell motility represent some of the ways in which cells execute motion. The contractile and motile proteins underlying these motions share a common property they are filamentous or polymerize to form filaments. Examples include actin and myosin, the filamentous proteins forming the contractile systems of cells, and tubulin, the major component of microtubules (the filaments involved in the mitotic spindle of cell division as well as in flagella and cilia). Another class of proteins involved in movement includes dynein and kinesin, so-called motor proteins that drive the movement of vesicles, granules, and organelles along microtubules serving as established cytoskeletal tracks. ... 

FIGURE 6.47 The structure of a typical microtubule, showing the arrangement of the a- and /3-monomers of the tubulin dimer. 

Because all tubulin dimers in a microtubule are oriented similarly, microtubules are polar structures. The end of the microtubule at which growth occurs is the plus end, and the other is the minus end. Microtubules in vitro carry out a GTP-dependent process called treadmiUing, in which tubulin dimers are added to the plus end at about the same rate at which dimers are removed from the minus end (Figure 17.3). 

Microtubules Are the Fundamental Structural Units of Cilia and Flagella... 

As already noted, microtubules are also the fundamental building blocks of cilia and flagella. Cilia are short, cylindrical, hairlike projections on the surfaces of the cells of many animals and lower plants. The beating motion of cilia functions either to move cells from place to place or to facilitate the movement of extracellular fluid over the cell surface. Flagella are much longer structures found singly or a few at a time on certain cells (such as sperm cells). They pro-... 

FIGURE 17.3 A model of the GTP-depeu-deut treadmiUing process. Both a- aud /J-tubuliu possess two different binding sites for GTP. The polymerization of tubuliu to form microtubules is driven by GTP hydrolysis in a process that is only beginning to be understood in detail. 

FIGURE 17.5 The structure of an axoneme. Note the manner in which two microtubules are joined in the nine outer pairs. The smaller-diameter tubule of each pair, which is a true cylinder, is called the A-tubule and isjoined to the center sheath of the axoneme by a spoke structure. Each outer pair of tubules isjoined to adjacent pairs by a nexin bridge. The A-tubule of each outer pair possesses an outer dynein arm and an inner dynein arm. The larger-diameter tubule is known as the B-tubule. 

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