Motile proteins

Alpha helices are sufficiently versatile to produce many very different classes of structures. In membrane-bound proteins, the regions inside the membranes are frequently a helices whose surfaces are covered by hydrophobic side chains suitable for the hydrophobic environment inside the membranes. Membrane-bound proteins are described in Chapter 12. Alpha helices are also frequently used to produce structural and motile proteins with various different properties and functions. These can be typical fibrous proteins such as keratin, which is present in skin, hair, and feathers, or parts of the cellular machinery such as fibrinogen or the muscle proteins myosin and dystrophin. These a-helical proteins will be discussed in Chapter 14. 

Contractile and motile proteins Actin Myosin Tubulin Dyne in Kinesin... 

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. ... 

Wilson, M.L. and Macnab, R.M. (1990). Co-overproduction and localization of the Escherichia coli motility proteins MotA and MotB. J. Bacteriol. 172, 3932-3939. 

Purification of bovine sperm forward motility protein... 

Analysis of human sera for carcinoembryonic antigen-binding proteins Isolation by immunoadsorption of a carcino-embryonic antigen-binding human immunoglobulin G from normal sera Purification of bovine sperm forward motility protein... 

Contractile and motile proteins Mediate motion and muscle contraction Actin and myosin (provide muscle contraction)... 

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. 

Phosphorylation is the reversible process of introducing a phosphate group onto a protein. Phosphorylation occurs on the hydroxyamino acids serine and threonine or on tyrosine residues targeted by Ser/Thr kinases and tyrosine kinases respectively. Dephosphorylation is catalyzed by phosphatases. Phosphorylation is a key mechanism for rapid posttranslational modulation of protein function. It is widely exploited in cellular processes to control various aspects of cell signaling, cell proliferation, cell differentiation, cell survival, cell metabolism, cell motility, and gene transcription. 

Studies on muscle contraction carried out between 1930 and 1960 heralded the modem era of research on cytoskeletal stmctures. Actin and myosin were identified as the major contractile proteins of muscle, and detailed electron microscopic studies on sarcomeres by H.E. Huxley and associates in the 1950s produced the concept of the sliding filament model, which remains the keystone to an understanding of the molecular mechanisms responsible for cytoskeletal motility. 

Proteins that cross-link actin filaments bind to their sides to produce bundles or three-dimensional networks (Otto, 1994). In microvilli, approximately 20 actin filaments of the core are cross-linked by villin (95 kD) and fimbrin (68 kD) in helical array to form a compact bundle (Figure 5). Filamin (2 x 250 kD) induces the formation of an actin network with gel formation. By immunofluorescence microscopy, this ABP is found in the ruffled, motile edge of cultured cells, where only actin filaments are abundant. 

It is of interest that proteins termed motility factors (55-70 kD) are secreted by fetal cells and some tumor cells. These proteins act as autocrine factors and stimulate rapid movement by these cells. Motility factors induce the formation of cell processes that are packed with actin filaments and have an increased number of receptors for the matrix proteins laminin and fibronectin. The latter enhance the ability of the cells to bind to the extracellular matrix. Thus, it is likely that motility factors influence the organization of the cytoskeleton through changes taking place at the cell surface (reviewed by Warn and Dowrick, 1989). 

Vale, R.D., Reese, T.S., Sheetz, M.P. (1985a). Identification of a novel force generating protein, kinesin, involved in microtubule-based motility. Cell 42,39-50. 

The Role of Myosins in Cell Locomotion The Role of Actin-Binding Proteins in Cell Locomotion The Transduction of Extracellular Motility Signals to the Cytoskeleton Lipid Flow and Cell Locomotion The Role of Cell Locomotion in Metastasis Intracellular Motility Microtubule-Based Intracellular Motility... 

Microtubule-Based Motor Proteins The Meiotic and Mitotic Spindles Microfilament-Based Intracellular Motility Cytokinesis... 

Andre, E., Brink, M., Gerisch, G., Isenberg, G., Noegel, A., Schleicher, M., Segall, J.E., Wallraff, E. (1989). A Dictyostelium mutant deficient in severin, an F-actin fragmenting protein, shows normal motility and chemotaxis. J. Cell Biol. 108, 985-995. 

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