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Physiological Reviews, Vol. 83, No. 2, April 2003, pp. 433-473; 10.1152/physrev.00026.2002.
Copyright ©2003 by the American Physiological Society
Institute for Biomedical Research, Muscle Research Unit, Department of Anatomy and Histology, University of Sydney, Sydney, Australia
Dos Remedios, C. G.,
D. Chhabra,
M. Kekic,
I. V. Dedova,
M. Tsubakihara,
D. A. Berry, and
N. J. Nosworthy.
Actin Binding Proteins: Regulation of Cytoskeletal
Microfilaments. Physiol. Rev. 83: 433-473, 2003.
The actin cytoskeleton is a complex
structure that performs a wide range of cellular functions. In 2001, significant advances were made to our understanding of the structure
and function of actin monomers. Many of these are likely to help us
understand and distinguish between the structural models of actin
microfilaments. In particular, 1) the structure of actin was
resolved from crystals in the absence of cocrystallized actin binding
proteins (ABPs), 2) the prokaryotic ancestral gene of actin
was crystallized and its function as a bacterial cytoskeleton was
revealed, and 3) the structure of the Arp2/3 complex was
described for the first time. In this review we selected several ABPs
(ADF/cofilin, profilin, gelsolin, thymosin 
4, DNase I, CapZ,
tropomodulin, and Arp2/3) that regulate actin-driven assembly,
i.e., movement that is independent of motor proteins. They were chosen
because 1) they represent a family of related proteins,
2) they are widely distributed in nature, 3) an
atomic structure (or at least a plausible model) is available for each
of them, and 4) each is expressed in significant quantities
in cells. These ABPs perform the following cellular functions:
1) they maintain the population of unassembled but assembly-ready actin monomers (profilin), 2) they
regulate the state of polymerization of filaments (ADF/cofilin,
profilin), 3) they bind to and block the growing ends of
actin filaments (gelsolin), 4) they nucleate actin assembly
(gelsolin, Arp2/3, cofilin), 5) they sever actin filaments
(gelsolin, ADF/cofilin), 6) they bind to the sides of actin
filaments (gelsolin, Arp2/3), and 7) they cross-link
actin filaments (Arp2/3). Some of these ABPs are essential, whereas
others may form regulatory ternary complexes. Some play crucial roles
in human disorders, and for all of them, there are good reasons why
investigations into their structures and functions should continue.
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