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Protein motors

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. ... [Pg.124]

Motor proteins, also known as molecular motors, use chemical energy (ATP) to orchestrate all these movements, transforming ATP energy into the mechanical energy of motion. In all cases, ATP hydrolysis is presumed to drive and... [Pg.533]

Hoenger, A., Sablin, E., Vale, R., et al., 1995. Three-dimensional structure of a tnbnlin-motor-protein complex. Nature... [Pg.564]

Vallee, R., and Shpetner, H., 1990. Motor proteins of cytoplasmic microtnbnles. Annual Review of Biochemistry 59 909—932. [Pg.564]

Utilization of a similar [Sc(OTf)3-promoted)] approach by Overman on the ger-anylgeraniol-derived cyclization substrate 98 provided the desired tetracyclization product 99, in which the terminator of the cationic cyclization is an arene group. Compound 99 is then transformed into the kinesin motor protein inhibitor adocia-sulfate 1 (Scheme 8.27) [47]. [Pg.288]

Motor proteins move along MTs in an ATP-dependent manner. Members of the superfamily of kinesin motors move only to the plus ends and dynein motors only to the minus ends. The respective motor domains are linked via adaptor proteins to their cargoes. The binding activity of the motors to MTs is regulated by kinases and phosphatases. When motors are immobilized at their cargo-binding area, they can move MTs. [Pg.415]

Dynein, kinesin, and myosin are motor proteins with ATPase activity that convert the chemical bond energy released by ATP hydrolysis into mechanical work. Each motor molecule reacts cyclically with a polymerized cytoskeletal filament in this chemomechanical transduction process. The motor protein first binds to the filament and then undergoes a conformational change that produces an increment of movement, known as the power stroke. The motor protein then releases its hold on the filament before reattaching at a new site to begin another cycle. Events in the mechanical cycle are believed to depend on intermediate steps in the ATPase cycle. Cytoplasmic dynein and kinesin walk (albeit in opposite... [Pg.16]

Even though dynein, kinesin, and myosin serve similar ATPase-dependent chemomechanical functions and have structural similarities, they do not appear to be related to each other in molecular terms. Their similarity lies in the overall shape of the molecule, which is composed of a pair of globular heads that bind microtubules and a fan-shaped tail piece (not present in myosin) that is suspected to carry the attachment site for membranous vesicles and other cytoplasmic components transported by MT. The cytoplasmic and axonemal dyneins are similar in structure (Hirokawa et al., 1989 Holzbaur and Vallee, 1994). Current studies on mutant phenotypes are likely to lead to a better understanding of the cellular roles of molecular motor proteins and their mechanisms of action (Endow and Titus, 1992). [Pg.17]

Microtubule-Based Motor Proteins The Meiotic and Mitotic Spindles Microfilament-Based Intracellular Motility Cytokinesis... [Pg.78]

Just as myosins are able to move along microfilaments, there are motor proteins that move along microtubules. Microtubules, like microfilaments, are polar polymeric assemblies, but unlike actin-myosin interactions, microtubule-based motors exist that move along microtubules in either direction. A constant traffic of vesicles and organelles is visible in cultured cells especially using time-lapse photography. The larger part of this movement takes place on micrombules and is stimulated by phorbol ester (an activator of protein kinase C), and over-expression of N-J aj oncoprotein (Alexandrova et al., 1993). [Pg.99]

Skoufias, D.A., Scholey, J.M. (1993). Cytoplasmic micrombule-based motor proteins. Curr. Opinion Cell Biol. 5,95-104. [Pg.105]

Howard J Mechanics of Motor Proteins and the Cytoskeleton. Sinauer, 2001. [Pg.579]

Zecevic M, Catling AD, Eblen ST et al 1998 Active MAP kinase in mitosis localization at kinetochores and association with the motor protein CENP-E. J Cell Biol 142 1547—1558... [Pg.73]

Dynein Motor protein mediating microtubule-based synaptic vesicle transport. May be involved in retrograde axonal transport to the cell body. [Pg.159]

Kinesins Motor proteins for microtubule-based synaptic vesicle transport. In Caenorhabditis elegans, akinesin encoded by unc-104 is essential for transport of synaptic vesicles to nerve terminals. [Pg.159]

Yonekawa, Y., Harada, A., Okada, Y. et al. Defect in synaptic vesicle precursor transport and neuronal cell death in KIF1A motor protein-deficient mice. /. Cell Biol. 141 431—441, 1998. [Pg.165]

Motor proteins of the large kinesin family all have well... [Pg.496]

Although the last family of motor proteins to be discovered, the kinesins have proved to be remarkably diverse. So far, there are at least 14 distinct subfamilies in the kinesin family and more are likely to emerge, all with homology in their motor domain [53], Within a subfamily, however, the more extensive sequence similarities are presumed to reflect related functions. At present, many questions remain about the function of these various motors in the nervous system. [Pg.497]

Although many motor proteins are found in nervous tissue, there are few instances in which we hilly understand their cellular functions. The proliferation of different motor molecules and the existence of numerous isoforms raises the possibility that some physiological activities require multiple motors. There may be cases in which motors serve a redundant role to ensure that the physiological activity is maintained in the event of a loss of one motor protein. Finally, the existence of so many different types of motor molecule suggests that novel physiological activities requiring molecular motors may be as yet unrecognized. [Pg.499]

Hirokawa, N. and Takemura, R. Biochemical and molecular characterization of diseases linked to motor proteins. Trends Biochem. Sci. 28 558-565, 2003. [Pg.500]

Lines of mice with mutant genes encoding motor proteins develop an amyotrophic-lateral-sclerosis-like phenotype 736... [Pg.731]


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Globular proteins motors

Kinesin motor protein inhibitor

Microtubules Microtubule-based motor proteins

Model proteins motors

Molecular motors Motor proteins

Motor interaction protein

Motor protein mitotic kinesin

Motor protein potential

Motor proteins dynein

Motor proteins kinesin

Motor proteins myosin

Motor proteins structure

Motors, molecular protein, actin-binding

Outer motor protein

Oxidative phosphorylation protein motor

Protein motors rotary motion

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