Actin structure and function

Annual Review of Biophysics

Volumn 40, Issue 1, 2011, Pages 169-186

  Dominguez, Roberto ^a   Holmes, Kenneth C ^b  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

Author keywords

actin binding proteins; electron microscopy; fiber diffraction; X ray crystallography

Indexed keywords

ACTIN BINDING PROTEIN; COFILIN; CYTOCHALASIN D; DEOXYRIBONUCLEASE I; F ACTIN; G ACTIN; GELSOLIN; MONOMER; PROFILIN;

ARTICLE; CLOSTRIDIUM BOTULINUM; CLOSTRIDIUM PERFRINGENS; CRYOELECTRON MICROSCOPY; LISTERIA; MOLECULAR LIBRARY; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; REVERSE TRANSCRIPTION; SALMONELLA; SHIGELLA; TOXOPLASMA GONDII;

ACTINS; BINDING SITES; COMPUTER SIMULATION; MODELS, BIOLOGICAL; MODELS, CHEMICAL; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP;

EUKARYOTA;

EID: 79955859521     PISSN: 1936122X     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev-biophys-042910-155359     Document Type: Article

References (59)

1. Barth H, Stiles BG. 2008. Binary actin-ADP-ribosylating toxins and their use as molecular Trojan horses for drug delivery into eukaryotic cells. Curr. Med. Chem. 15:459-69 (Pubitemid 351472412)
2. Bernstein BW, Bamburg JR. 2010. ADF/cofilin: a functional node in cell biology. Trends Cell Biol. 20:187-95
3. Bork P, Sander C, Valencia A. 1992. An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc. Natl. Acad. Sci. USA 89:7290-94
4. Breitsprecher D, Kiesewetter AK, Linkner J, Urbanke C, Resch GP, et al. 2008. Clustering of VASP actively drives processive, WH2 domain-mediated actin filament elongation. EMBO J. 27:2943-54
5. Burtnick LD, Koepf EK, Grimes J, Jones EY, Stuart DI, et al. 1997. The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation. Cell 90:661-70 (Pubitemid 27357958)
6. Campellone KG, Welch MD. 2010. A nucleator arms race: cellular control of actin assembly. Nat. Rev. Mol. Cell Biol. 11:237-51
7. Carlier MF, Laurent V, Santolini J, Melki R, Didry D, et al. 1997. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J. Cell. Biol. 136:1307-22 (Pubitemid 27421917)
8. Carlier MF, Valentin-Ranc C, Combeau C, Fievez S, Pantoloni D. 1994. Actin polymerization: regulation by divalent metal ion and nucleotide binding, ATP hydrolysis and binding of myosin. Adv. Exp. Med. Biol. 358:71-81 (Pubitemid 24284913)
9. De la Cruz EM. 2009. How cofilin severs an actin filament. Biophys. Rev. 1:51-59
10. Dominguez R. 2004. Actin-binding proteins-a unifying hypothesis. Trends Biochem. Sci. 29:572-78
11. Dominguez R. 2007. The beta-thymosin/WH2 fold: multifunctionality and structure. Ann. N. Y. Acad. Sci. 1112:86-94
12. Dominguez R. 2010. Structural insights into de novo actin polymerization. Curr. Opin. Struct. Biol. 20:217-25
13. Dos Remedios CG, Chhabra D, Kekic M, Dedova IV, Tsubakihara M, et al. 2003. Actin binding proteins: regulation of cytoskeletal microfilaments. Physiol. Rev. 83:433-73 (Pubitemid 36378678)
14. Drees F, Gertler FB. 2008. Ena/VASP: proteins at the tip of the nervous system. Curr. Opin. Neurobiol. 18:53-59
15. Ferron F, Rebowski G, Lee SH, Dominguez R. 2007. Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP. EMBO J. 26:4597-606 (Pubitemid 350036631)
16. Fujii T, Iwane AH, Yanagida T, Namba K. 2010. Direct visualization of secondary structures of F-actin by electron cryomicroscopy. Nature 467:724-28
17. Galkin VE, Orlova A, Rivera C, Mullins RD, Egelman EH. 2009. Structural polymorphism of the ParM filament and dynamic instability. Structure 17:1253-64
18. Galkin VE, VanLoock MS, Orlova A, Egelman EH. 2002. A new internal mode in F-actin helps explain the remarkable evolutionary conservation of actin's sequence and structure. Curr. Biol. 12:570-75 (Pubitemid 34271371)
19. Goode BL, Eck MJ. 2007. Mechanism and function of formins in the control of actin assembly. Annu. Rev. Biochem. 76:593-627
20. Gouin E, Welch MD, Cossart P. 2005. Actin-based motility of intracellular pathogens. Curr. Opin. Microbiol. 8:35-45 (Pubitemid 40203224)
21. Graceffa P, Dominguez R. 2003. Crystal structure of monomeric actin in the ATP state: structural basis of nucleotide-dependent actin dynamics. J. Biol. Chem. 278:34172-80 (Pubitemid 37553259)
22. Hanson J, Lowy J. 1963. The structure of F-actin and the actin filaments isolated from muscle. J. Mol. Biol. 6:46-60
23. Herman IM. 1993. Actin isoforms. Curr. Opin. Cell Biol. 5:48-55
24. Holmes KC, Angert I, Kull FJ, Jahn W, Schroder RR. 2003. Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide. Nature 425:423-27 (Pubitemid 37187274)
25. Holmes KC, Popp D, Gebhard W, Kabsch W. 1990. Atomic model of the actin filament. Nature 347:44-49
26. Iwasa M, Maeda K, Narita A, Maeda Y, Oda T. 2008. Dual roles of Gln137 of actin revealed by recombinant human cardiac muscle alpha-actin mutants. J. Biol. Chem. 283:21045-53
27. Kabsch W, Mannherz HG, Suck D, Pai EF, Holmes KC. 1990. Atomic structure of the actin:DNase I complex. Nature 347:37-44
28. Kovar DR, Harris ES, Mahaffy R, Higgs HN, Pollard TD. 2006. Control of the assembly of ATP- and ADP-actin by formins and profilin. Cell 124:423-35 (Pubitemid 43121988)
29. Lang AE, Schmidt G, Schlosser A, Hey TD, Larrinua IM, et al. 2010. Photorhabdus luminescens toxins ADP-ribosylate actin and RhoA to force actin clustering. Science 327:1139-42
30. Lee WM, Galbraith RM. 1992. The extracellular actin-scavenger system and actin toxicity. N. Engl. J. Med. 326:1335-41
31. Lorenz M, Holmes KC. The actin-myosin interface. Proc. Natl. Acad. Sci. USA 107:12529-34
32. Lorenz M, Popp D, Holmes KC. 1993. Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234:826-36 (Pubitemid 24007803)
33. Mannherz HG, Goody RS, Konrad M, Nowak E. 1980. The interaction of bovine pancreatic deoxyri-bonuclease I and skeletal muscle actin. Eur. J. Biochem. 104:367-79 (Pubitemid 10115576)
34. Miralles F, Visa N. 2006. Actin in transcription and transcription regulation. Curr. Opin. Cell Biol. 18:261-66
35. Oda T, Iwasa M, Aihara T, Maeda Y, Narita A. 2009. The nature of the globular- to fibrous-actin transition. Nature 457:441-45
36. Oda T, Maeda Y. 2010. Multiple conformations of F-actin. Structure 18:761-67
37. Olson EN, Nordheim A. 2010. Linking actin dynamics and gene transcription to drive cellular motile functions. Nat. Rev. Mol. Cell Biol. 11:353-65
38. Otomo T, Tomchick DR, Otomo C, Panchal SC, Machius M, Rosen MK. 2005. Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature 433:488-94 (Pubitemid 40204299)
39. Otterbein LR, Graceffa P, Dominguez R. 2001. The crystal structure of uncomplexed actin in the ADP state. Science 293:708-11 (Pubitemid 32728675)
40. Paavilainen VO, Oksanen E, Goldman A, Lappalainen P. 2008. Structure of the actin-depolymerizing factor homology domain in complex with actin. J. Cell Biol. 182:51-59 (Pubitemid 352008621)
41. Paunola E, Mattila PK, Lappalainen P. 2002. WH2 domain: a small, versatile adapter for actin monomers. FEBS Lett. 513:92-97 (Pubitemid 34242984)
42. Polka JK, Kollman JM, Agard DA, Mullins RD. 2009. The structure and assembly dynamics of plasmid actin AlfA imply a novel mechanism of DNA segregation. J. Bacteriol. 191:6219-30
43. Pollard TD. 2007. Regulation of actin filament assembly by Arp2/3 complex and formins. Annu. Rev. Biophys. Biomol. Struct. 36:451-77 (Pubitemid 47007562)
44. Pollard TD, Borisy GG. 2003. Cellular motility driven by assembly and disassembly of actin filaments. Cell 112:453-65 (Pubitemid 36263079)
45. Popp D, Lednev VV, Jahn W. 1987. Methods of preparing well-orientated sols of F-actin containing filaments suitable for X-ray diffraction. J. Mol. Biol. 197:679-84
46. Popp D, Narita A, Ghoshdastider U, Maeda K, Maeda Y, et al. 2010. Polymeric structures and dynamic properties of the bacterial actin AlfA. J. Mol. Biol. 397:1031-41
47. Popp D, Narita A, Oda T, Fujisawa T, Matsuo H, et al. 2008. Molecular structure of the ParM polymer and the mechanism leading to its nucleotide-driven dynamic instability. EMBO J. 27:570-79 (Pubitemid 351225678)
48. Robinson RC, Turbedsky K, Kaiser DA, Marchand JB, Higgs HN, et al. 2001. Crystal structure of Arp2/3 complex. Science 294:1679-84 (Pubitemid 33104831)
49. Rohr G, Mannherz HG. 1978. Isolation and characterization of secretory actin. DNAase I complex from rat pancreatic juice. Eur. J. Biochem. 89:151-57 (Pubitemid 8402089)
50. Sawaya MR, Kudryashov DS, Pashkov I, Adisetiyo H, Reisler E, Yeates TO. 2008. Multiple crystal structures of actin dimers and their implications for interactions in the actin filament. Acta Crystallogr. D 64:454-65 (Pubitemid 351507808)
51. Silacci P, Mazzolai L, Gauci C, Stergiopulos N, Yin HL, Hayoz D. 2004. Gelsolin superfamily proteins: key regulators of cellular functions. Cell Mol. Life Sci. 61:2614-23 (Pubitemid 39586521)
52. Tirion MM, ben-Avraham D, Lorenz M, Holmes KC. 1995. Normal modes as refinement parameters for the F-actin model. Biophys. J. 68:5-12
53. Van den Ent F, Amos LA, Lowe J. 2001. Prokaryotic origin of the actin cytoskeleton. Nature 413:39-44 (Pubitemid 32843480)
54. van den Ent F, Møller-Jensen J, Amos LA, Gerdes K, Lowe J. 2002. F-actin-like filaments formed by plasmid segregation protein ParM. EMBO J. 21:6935-43 (Pubitemid 36014565)
55. Wegner A, Isenberg G. 1983. 12-fold difference between the critical monomer concentrations of the two ends of actin filaments in physiological salt conditions. Proc. Natl. Acad. Sci. USA 80:4922-25
56. Xu Y, Moseley JB, Sagot I, Poy F, Pellman D, et al. 2004. Crystal structures of a Formin homology-2 domain reveal a tethered dimer architecture. Cell 116:711-23 (Pubitemid 38326729)
57. Yarmola EG, Somasundaram T, Boring TA, Spector I, Bubb MR. 2000. Actin-latrunculin A structure and function. Differential modulation of actin-binding protein function by latrunculin A. J. Biol. Chem. 275:28120-27
58. Yeung KS, Paterson I. 2002. Actin-binding marine macrolides: total synthesis and biological importance. Angew. Chem. Int. Ed. Engl. 41:4632-53 (Pubitemid 36061428)
59. Lodoen MB, Gerke C, Boothroyd JC. 2010. A highly sensitive FRET-based approach reveals secretion of the actin-binding protein toxofilin during Toxoplasma gondii infection. Cell Microbiol. 12(1):55-66