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      • Record: found
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      Conformational Dynamics of Actin: Effectors and Implications for Biological Function

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          Abstract

          Actin is a protein abundant in many cell types. Decades of investigations have provided evidence that it has many functions in living cells. The diverse morphology and dynamics of actin structures adapted to versatile cellular functions is established by a large repertoire of actin-binding proteins. The proper interactions with these proteins assume effective molecular adaptations from actin, in which its conformational transitions play essential role. This review attempts to summarise our current knowledge regarding the coupling between the conformational states of actin and its biological function.

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          Actin, a central player in cell shape and movement.

          Thomas Pollard, John Cooper (2009)
          The protein actin forms filaments that provide cells with mechanical support and driving forces for movement. Actin contributes to biological processes such as sensing environmental forces, internalizing membrane vesicles, moving over surfaces, and dividing the cell in two. These cellular activities are complex; they depend on interactions of actin monomers and filaments with numerous other proteins. Here, we present a summary of the key questions in the field and suggest how those questions might be answered. Understanding actin-based biological phenomena will depend on identifying the participating molecules and defining their molecular mechanisms. Comparisons of quantitative measurements of reactions in live cells with computer simulations of mathematical models will also help generate meaningful insights.
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            Dystrophin protects the sarcolemma from stresses developed during muscle contraction.

            B Petrof, J Shrager, H H Stedman … (1993)
            The protein dystrophin, normally found on the cytoplasmic surface of skeletal muscle cell membranes, is absent in patients with Duchenne muscular dystrophy as well as mdx (X-linked muscular dystrophy) mice. Although its primary structure has been determined, the precise functional role of dystrophin remains the subject of speculation. In the present study, we demonstrate that dystrophin-deficient muscle fibers of the mdx mouse exhibit an increased susceptibility to contraction-induced sarcolemmal rupture. The level of sarcolemmal damage is directly correlated with the magnitude of mechanical stress placed upon the membrane during contraction rather than the number of activations of the muscle. These findings strongly support the proposition that the primary function of dystrophin is to provide mechanical reinforcement to the sarcolemma and thereby protect it from the membrane stresses developed during muscle contraction. Furthermore, the methodology used in this study should prove useful in assessing the efficacy of dystrophin gene therapy in the mdx mouse.
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              Mechanism and function of formins in the control of actin assembly.

              Bruce L. Goode, Michael Eck (2007)
              Formins are a widely expressed family of proteins that govern cell shape, adhesion, cytokinesis, and morphogenesis by remodeling the actin and microtubule cytoskeletons. These large multidomain proteins associate with a variety of other cellular factors and directly nucleate actin polymerization through a novel mechanism. The signature formin homology 2 (FH2) domain initiates filament assembly and remains persistently associated with the fast-growing barbed end, enabling rapid insertion of actin subunits while protecting the end from capping proteins. On the basis of structural and mechanistic work, an integrated model is presented for FH2 processive motion. The adjacent FH1 domain recruits profilin-actin complexes and accelerates filament elongation. The most predominantly expressed formins in animals and fungi are autoinhibited through intramolecular interactions and appear to be activated by Rho GTPases and additional factors. Other classes of formins lack the autoinhibitory and/or Rho-binding domains and thus are likely to be controlled by alternative mechanisms.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Cytoskeleton (Hoboken)
                Journal ID (publisher-id): cm
                Title: Cytoskeleton (Hoboken, N.j.)
                Publisher: John Wiley & Sons, Inc.
                ISSN (Print): 1949-3584
                ISSN (Electronic): 1949-3592
                Publication date (Print): October 2010
                Publication date (Electronic): 29 July 2010
                Volume: 67
                Issue: 10
                Pages: 609-629
                Affiliations
                simpleDepartment of Biophysics, University of Pécs, Faculty of Medicine Pécs, Szigeti str. 12, H-7624, Hungary
                Author notes
                *Address correspondence to: Miklós Nyitrai, Department of Biophysics, Faculty of Medicine, University of Pécs, Pécs, Szigeti u. 12, H-7624, Hungary. E-mail: miklos.nyitrai@ 123456aok.pte.hu

                Monitoring Editor: Roberto Dominguez

                The first two authors contributed equally to this work.

                Article
                DOI: 10.1002/cm.20473
                PMC ID: 3038201
                PubMed ID: 20672362
                SO-VID: 67c0141c-4650-4146-8c61-9789633831b8
                Copyright © Copyright © 2010 Wiley-Liss, Inc., A Wiley Company
                License:

                Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation.

                History
                Date received : 20 February 2010
                Date accepted : 15 July 2010
                Categories
                Subject: Review Article

                ScienceOpen disciplines: Cell biology
                Keywords: protein structure,diseases,actin,actin-binding proteins,mutations,cytoskeleton
                Data availability:
                ScienceOpen disciplines: Cell biology
                Keywords: protein structure, diseases, actin, actin-binding proteins, mutations, cytoskeleton

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