By Pekka Lappalainen

The actin cytoskeleton performs a principal function in lots of mobile approaches together with mobile motility, cytokinesis, endocytosis and phagocytosis. The constitution and dynamics of the actin cytoskeleton is regulated by means of a great number of proteins that have interaction with monomeric and/or filamentous actin. Actin monomer binding proteins offers a entire view on actin monomer-binding proteins and the mechanisms in which they give a contribution to actin dynamics and diverse actin-dependent mobile methods. This new name comprises chapters that describe the fundamental mechanisms of actin dynamics in addition to the structural rules in which numerous actin-binding proteins have interaction with actin.

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Nature 1998; 393(6687):809-812. 62. Rosso S, BoUati F, Bisbal M et al. LIMKl regulates Golgi dynamics, traffic of Golgi-derived vesicles, and process extension in primary cultured neurons. Mol Biol Cell 2004; 15(7):3433-3449. 63. Foletta V C , Moussi N , Sarmiere P D et al. LIM kinase 1, a key regulator of actin dynamics, is widely expressed in embryonic and adult tissues. Exp Cell Res 2004; 294(2):392-405. G^. Bernard O, Ganiatsas S, Kannourakis G et al. Kiz-1, a protein with LIM zinc finger and kinase domains, is expressed mainly in neurons.

102. Gunning PW, Schevzov G, Kee AJ et al. Tropomyosin isoforms: Divining rods for actin cytoskeleton function. Trends Cell Biol 2005; 15(6):333-341. 103. Bryce NS, Schevzov G, Ferguson V et al. Specification of actin filament function and molecular composition by tropomyosin isoforms. Mol Biol Cell 2003; 14(3): 1002-1016. 104. Rodal AA, Tetreault JW, Lappalainen P et al. A i p l p interacts with cofilin to disassemble actin filaments. J Cell Biol 1999; 145(6):1251-1264. 105. Okada K, Blanchoin L, Abe H et al.

In support of this, movement o^Listeria in an in vitro reconstituted system is enhanced by the presence of profilin and VASP,^^^ and the concentration of VASP at the cell edge appears to correlate directly w^ith the rate by w^hich the edge advances. ^^^ The second profilinractin-dependent actin polymerization mechanism is represented by the formin family of proteins. ^^^ One of the most potent actin polymerizing members of this 36 Actin-Monomer-Binding Proteins family is mDia. A fragment of mDia containing the F H l and FH2 domains polymerizes actin, with an efficienq^ greatly enhanced by profilin, leading to formation of long filaments in parallel arrays, which rapidly elongate.

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