Actin structure and function.

Actin is the most abundant protein in most eukaryotic cells. It is highly conserved and participates in more protein-protein interactions than any known protein. These properties, along with its ability to transition between monomeric (G-actin) and filamentous (F-actin) states under the control of nucleotide hydrolysis, ions, and a large number of actin-binding proteins, make actin a critical player in many cellular functions, ranging from cell motility and the maintenance of cell shape and polarity to the regulation of transcription. Moreover, the interaction of filamentous actin with myosin forms the basis of muscle contraction. Owing to its central role in the cell, the actin cytoskeleton is also disrupted or taken over by numerous pathogens. Here we review structures of G-actin and F-actin and discuss some of the interactions that control the polymerization and disassembly of actin.

[1]  E. M. De La Cruz.  How cofilin severs an actin filament , 2009, Biophysical reviews.

[2]  W. Kabsch,et al.  Atomic structure of the actin: DNase I complex , 1990, Nature.

[3]  Alfred Nordheim,et al.  Linking actin dynamics and gene transcription to drive cellular motile functions , 2010, Nature Reviews Molecular Cell Biology.

[4]  Edward H. Egelman,et al.  A New Internal Mode in F-Actin Helps Explain the Remarkable Evolutionary Conservation of Actin's Sequence and Structure , 2002, Current Biology.

[5]  R. Dominguez.  Structural insights into de novo actin polymerization. , 2010, Current opinion in structural biology.

[6]  Michael J. Eck,et al.  Crystal Structures of a Formin Homology-2 Domain Reveal a Tethered Dimer Architecture , 2004, Cell.

[7]  L. Otterbein,et al.  The Crystal Structure of Uncomplexed Actin in the ADP State , 2001, Science.

[8]  Guenter P. Resch,et al.  Clustering of VASP actively drives processive, WH2 domain‐mediated actin filament elongation , 2008, The EMBO journal.

[9]  R. Dominguez,et al.  Structural basis for the recruitment of profilin–actin complexes during filament elongation by Ena/VASP , 2007, The EMBO journal.

[10]  E. Yarmola,et al.  Actin-latrunculin A structure and function. Differential modulation of actin-binding protein function by latrunculin A. , 2000, The Journal of biological chemistry.

[11]  Kenneth C Holmes,et al.  The actin-myosin interface , 2010, Proceedings of the National Academy of Sciences.

[12]  G. Isenberg,et al.  12-fold difference between the critical monomer concentrations of the two ends of actin filaments in physiological salt conditions. , 1983, Proceedings of the National Academy of Sciences of the United States of America.

[13]  P. Cossart,et al.  Actin-based motility of intracellular pathogens. , 2005, Current opinion in microbiology.

[14]  T. Pollard,et al.  Crystal Structure of Arp2/3 Complex , 2001, Science.

[15]  Jessica K. Polka,et al.  The Structure and Assembly Dynamics of Plasmid Actin AlfA Imply a Novel Mechanism of DNA Segregation , 2009, Journal of bacteriology.

[16]  J. Boothroyd,et al.  A highly sensitive FRET‐based approach reveals secretion of the actin‐binding protein toxofilin during Toxoplasma gondii infection , 2010, Cellular microbiology.

[17]  W. Kabsch,et al.  Atomic model of the actin filament , 1990, Nature.

[18]  Jan Löwe,et al.  F‐actin‐like filaments formed by plasmid segregation protein ParM , 2002, The EMBO journal.

[19]  N. Stergiopulos,et al.  Gelsolin superfamily proteins: key regulators of cellular functions , 2004, Cellular and Molecular Life Sciences CMLS.

[20]  H. Matsuo,et al.  Molecular structure of the ParM polymer and the mechanism leading to its nucleotide‐driven dynamic instability , 2008, The EMBO journal.

[21]  M. Konrad,et al.  The interaction of bovine pancreatic deoxyribonuclease I and skeletal muscle actin. , 1980, European journal of biochemistry.

[22]  J. Bamburg,et al.  ADF/cofilin: a functional node in cell biology. , 2010, Trends in cell biology.

[23]  Marie-France Carlier,et al.  Actin Depolymerizing Factor (ADF/Cofilin) Enhances the Rate of Filament Turnover: Implication in Actin-based Motility , 1997, The Journal of cell biology.

[24]  A. Goldman,et al.  Structure of the actin-depolymerizing factor homology domain in complex with actin , 2008, The Journal of cell biology.

[25]  Pekka Lappalainen,et al.  WH2 domain: a small, versatile adapter for actin monomers , 2002, FEBS letters.

[26]  T. Pollard,et al.  Cellular Motility Driven by Assembly and Disassembly of Actin Filaments , 2003, Cell.

[27]  Matthew D. Welch,et al.  A nucleator arms race: cellular control of actin assembly , 2010, Nature Reviews Molecular Cell Biology.

[28]  Yuichiro Maéda,et al.  The nature of the globular- to fibrous-actin transition , 2009, Nature.

[29]  F. Gertler,et al.  Ena/VASP: proteins at the tip of the nervous system , 2008, Current Opinion in Neurobiology.

[30]  Hilla Peretz,et al.  Ju n 20 03 Schrödinger ’ s Cat : The rules of engagement , 2003 .

[31]  W. Jahn,et al.  Methods of preparing well-orientated sols of f-actin containing filaments suitable for X-ray diffraction. , 1987, Journal of molecular biology.

[32]  J. Lowy,et al.  The structure of F-actin and of actin filaments isolated from muscle , 1963 .

[33]  C. D. dos Remedios,et al.  Actin binding proteins: regulation of cytoskeletal microfilaments. , 2003, Physiological reviews.

[34]  Jan Löwe,et al.  Prokaryotic origin of the actin cytoskeleton , 2001, Nature.

[35]  H. Mannherz,et al.  Isolation and characterization of secretory actin . DNAase I complex from rat pancreatic juice. , 1978, European journal of biochemistry.

[36]  U. Ghoshdastider,et al.  Polymeric structures and dynamic properties of the bacterial actin AlfA. , 2010, Journal of molecular biology.

[37]  M. Carlier,et al.  Actin polymerization: regulation by divalent metal ion and nucleotide binding, ATP hydrolysis and binding of myosin. , 1994, Advances in experimental medicine and biology.

[38]  H. Barth,et al.  Binary actin-ADP-ribosylating toxins and their use as molecular Trojan horses for drug delivery into eukaryotic cells. , 2008, Current medicinal chemistry.

[39]  N. Visa,et al.  Actin in transcription and transcription regulation. , 2006, Current opinion in cell biology.

[40]  K C Holmes,et al.  Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. , 1993, Journal of molecular biology.

[41]  T. Pollard,et al.  Control of the Assembly of ATP- and ADP-Actin by Formins and Profilin , 2006, Cell.

[42]  M. Eck,et al.  Mechanism and function of formins in the control of actin assembly. , 2007, Annual review of biochemistry.

[43]  Thomas D Pollard,et al.  Regulation of actin filament assembly by Arp2/3 complex and formins. , 2007, Annual review of biophysics and biomolecular structure.

[44]  Michael K. Rosen,et al.  Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain , 2005, Nature.

[45]  Roberto Dominguez,et al.  Actin-binding proteins--a unifying hypothesis. , 2004, Trends in biochemical sciences.

[46]  Jonathan Grimes,et al.  The Crystal Structure of Plasma Gelsolin: Implications for Actin Severing, Capping, and Nucleation , 1997, Cell.

[47]  T. Yeates,et al.  Multiple crystal structures of actin dimers and their implications for interactions in the actin filament , 2008, Acta crystallographica. Section D, Biological crystallography.

[48]  R. Dominguez.  The beta-thymosin/WH2 fold: multifunctionality and structure. , 2007, Annals of the New York Academy of Sciences.

[49]  E. D. L. Cruz.  How cofilin severs an actin filament , 2009, Biophysical Reviews.

[50]  Yuichiro Maéda,et al.  Multiple Conformations of F-actin. , 2010, Structure.

[51]  Y. Maéda,et al.  Dual Roles of Gln137 of Actin Revealed by Recombinant Human Cardiac Muscle α-Actin Mutants* , 2008, Journal of Biological Chemistry.

[52]  W. Lee,et al.  The extracellular actin-scavenger system and actin toxicity. , 1992, The New England journal of medicine.

[53]  Roberto Dominguez,et al.  Crystal Structure of Monomeric Actin in the ATP State , 2003, Journal of Biological Chemistry.

[54]  Direct Visualization of Secondary Structures of F-actin by Electron Cryomicroscopy , 2011 .

[55]  P Bork,et al.  An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[56]  Rasmus R. Schröder,et al.  Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide , 2003, Nature.

[57]  H. Mannherz,et al.  Photorhabdus luminescens Toxins ADP-Ribosylate Actin and RhoA to Force Actin Clustering , 2010, Science.

[58]  I. Herman.  Actin isoforms. , 1993, Current opinion in cell biology.

[59]  K C Holmes,et al.  Normal modes as refinement parameters for the F-actin model. , 1995, Biophysical journal.

[60]  E. Egelman,et al.  Structural polymorphism of the ParM filament and dynamic instability. , 2009, Structure.