Actin-Monomer-Binding Proteins by Pekka Lappalainen

By Pekka Lappalainen

This publication presents a entire view on actin monomer-binding proteins and the mechanisms through which they give a contribution to actin dynamics and numerous actin-dependent mobile procedures. This new name comprises chapters that describe the elemental mechanisms of actin dynamics in addition to the structural rules through which a variety of actin-binding proteins have interaction with actin. The e-book is acceptable extra studying for college kids in complex telephone biology classes.

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Determining the differences in actin binding by human A D F and cofilin. J Mol Biol 2002; 315(4):911-925. 26 Actin-Monomer-Binding Proteins 89. Kusano K, Abe H , O b i n a t a T . D e t e c t i o n of a sequence involved in a c t i n - b i n d i n g a n d phosphoinositide-binding in the N-terminal side of cofilin. Mol Cell Biochem 1999; 190(1-2): 133-141. 90. Yonezawa N , Nishida E, lida K et al. Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides.

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. Cell Growth Differ 1994; 5(11):1159-1171. 65. Mizuno K, Okano I, Ohashi K et al. Identification of a human c D N A encoding a novel protein kinase with two repeats of the LIM/double zinc finger motif. Oncogene 1994; 9(6): 1605-1612.

For a listing of proline-rich profilin ligands (see ref 22). The poly-(L-proline) binding site is formed by residues in the N- and C-terminal a-helices and overlaps partly with surfaces on the molecule engaged in binding phosphoinositide lipids. The stability of the packing of the two terminal helices in profilin I is in part contributed for by a cluster of aromatic residues comprised of the side chains of W3, Y6, W31, Y139, and H133, (Fig. 1). ^^' ' The function of profilin is sensitive to modifications of the terminal helices and interference with these side chain-interactions influences its capacity to interact with its partners.

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