1932

Abstract

This is the story of someone who has been fortunate to work in a field of research where essentially nothing was known at the outset but that blossomed with the discovery of profound insights about two basic biological processes: cell motility and cytokinesis. The field started with no molecules, just a few people, and primitive methods. Over time, technological advances in biophysics, biochemistry, and microscopy allowed the combined efforts of scientists in hundreds of laboratories to explain mysterious processes with molecular mechanisms that can be embodied in mathematical equations and simulated by computers. The success of this field is a tribute to the power of the reductionist strategy for understanding biology.

Loading

Article metrics loading...

/content/journals/10.1146/annurev-cellbio-100818-125427
2019-10-06
2024-03-28
Loading full text...

Full text loading...

/deliver/fulltext/cellbio/35/1/annurev-cellbio-100818-125427.html?itemId=/content/journals/10.1146/annurev-cellbio-100818-125427&mimeType=html&fmt=ahah

Literature Cited

  1. Adams RJ, Pollard TD. 1986. Propulsion of organelles isolated from Acanthamoeba along actin filaments by myosin-I. Nature 322:754–56
    [Google Scholar]
  2. Adams RJ, Pollard TD. 1989. Binding of myosin I to membrane lipids. Nature 340:565–68
    [Google Scholar]
  3. Adelman MR, Taylor EW. 1969. Further purification and characterization of slime mold myosin and slime mold actin. Biochemistry 8:4976–88
    [Google Scholar]
  4. Adelstein RS, Pollard TD, Kuehl WM 1971. Isolation and characterization of myosin and two myosin fragments from human blood platelets. PNAS 68:2703–7
    [Google Scholar]
  5. Akamatsu MS, Berro J, Pu K-M, Tebbs IR, Pollard TD 2014. Cytokinetic nodes in fission yeast arise from two distinct types of nodes that merge during interphase. J. Cell Biol. 204:977–88
    [Google Scholar]
  6. Alberts BM, Amodio FJ, Jenkins M, Gutmann ED, Ferris FL 1968. Studies with DNA-cellulose chromatography. I. DNA-binding proteins from Escherichia coli. Cold Spring Harb. Symp. Quant. Biol 33:289–305
    [Google Scholar]
  7. Allen RD, Kamiya N. 1964. Primitive Motile Systems in Cell Biology New York: Academic
  8. Amann KJ, Pollard TD. 2001. Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy. PNAS 98:15009–13
    [Google Scholar]
  9. Arasada R, Pollard TD. 2011. Distinct roles for F-BAR proteins Cdc15p and Bzz1p in actin polymerization at sites of endocytosis in fission yeast. Curr. Biol. 21:1450–59
    [Google Scholar]
  10. Arasada R, Sayyad WA, Berro J, Pollard TD 2018. High-speed super-resolution imaging of the organization of the proteins in fission yeast clathrin-mediated endocytic actin patches. Mol. Biol. Cell 29:295–303
    [Google Scholar]
  11. Aydin F, Courtemanche N, Pollard TD, Voth GA 2018. Gating mechanisms during actin filament elongation by formins. eLife 7:e37342
    [Google Scholar]
  12. Bamburg JR, Harris HE, Weeds AG 1980. Partial purification and characterization of an actin depolymerizing factor from brain. FEBS Lett 121:178–82
    [Google Scholar]
  13. Beltzner CC, Pollard TD. 2008. Pathway of actin filament branch formation by Arp2/3 complex. J. Biol. Chem. 283:7135–44
    [Google Scholar]
  14. Berro J, Pollard TD. 2014. Local and global analysis of endocytic patch dynamics in fission yeast using a new “temporal super-resolution” realignment method. Mol. Biol. Cell 25:3501–14
    [Google Scholar]
  15. Berro J, Sirotkin V, Pollard TD 2010. Mathematical modeling of endocytic actin patch kinetics in fission yeast: Disassembly requires release of actin filament fragments. Mol. Biol. Cell 21:2905–15
    [Google Scholar]
  16. Bezanilla M, Forsburg SL, Pollard TD 1997. Identification of a second myosin-II in Schizosaccharomyces pombe: Myp2p is conditionally required for cytokinesis. Mol. Biol. Cell 8:2693–705
    [Google Scholar]
  17. Bezanilla M, Pollard TD. 2000. Myosin-II tails confer unique functions in Schizosaccharomyces pombe: characterization of a novel myosin-II tail. Mol. Biol. Cell 11:79–91
    [Google Scholar]
  18. Blanchoin L, Pollard TD. 1998. Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin. J. Biol. Chem. 273:25106–11
    [Google Scholar]
  19. Blanchoin L, Pollard TD. 1999. Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments. J. Biol. Chem. 274:15538–46
    [Google Scholar]
  20. Borisy GG, Taylor EW. 1967. The mechanism of action of colchicine: binding of colchicine-3H to cellular protein. J. Cell Biol. 34:525–34
    [Google Scholar]
  21. Burns RG, Pollard TD. 1974. A dynein-like protein from brain. FEBS Lett 40:274–80
    [Google Scholar]
  22. Carlier MF, Pantaloni D. 1986. Direct evidence for ADP–inorganic phosphate–F-actin as the major intermediate in ATP-actin polymerization. Rate of dissociation of inorganic phosphate from actin filaments. Biochemistry 25:7789–92
    [Google Scholar]
  23. Carlsson L, Nyström LE, Sundkvist I, Markey F, Lindberg U 1977. Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells. J. Mol. Biol. 115:465–83
    [Google Scholar]
  24. Chan C, Beltzner CC, Pollard TD 2009. Cofilin dissociates Arp2/3 complex and branches from actin filaments. Curr. Biol. 19:537–45
    [Google Scholar]
  25. Chang F, Drubin D, Nurse P 1997. Cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin. J. Cell Biol. 137:169–82
    [Google Scholar]
  26. Chen Q, Pollard TD. 2011. Actin filament severing by cofilin is more important for assembly than constriction of the cytokinetic contractile ring. J. Cell Biol. 195:485–98
    [Google Scholar]
  27. Chen Q, Pollard TD. 2013. Actin filament severing by cofilin contributes to both assembly and disassembly of endocytic actin patches. Curr. Biol. 23:1154–62
    [Google Scholar]
  28. Chou S, Pollard TD. 2019. Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides. PNAS 116:104265–74
    [Google Scholar]
  29. Cooper JA, Blum JD, Pollard TD 1984. Acanthamoeba castellanii capping protein: properties, mechanism of action, immunologic cross-reactivity, and localization. J. Cell Biol. 99:217–25
    [Google Scholar]
  30. Cooper JA, Blum JD, Williams RC Jr., Pollard TD 1986. Purification and characterization of actophorin, a new 15,000 dalton actin binding protein from Acanthamoeba castellanii. J. Biol. Chem 261:477–85
    [Google Scholar]
  31. Cooper JA, Buhle EL Jr., Walker SB, Tsong TY, Pollard TD 1983a. Kinetic evidence for a monomer activation step in actin polymerization. Biochemistry 22:2193–202
    [Google Scholar]
  32. Cooper JA, Walker SB, Pollard TD 1983b. Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization. J. Muscle Res. Cell Motil. 4:253–62
    [Google Scholar]
  33. Courtemanche N, Lee J, Pollard TD, Greene E 2013. Tension modulates actin filament polymerization mediated by formin and profilin. PNAS 110:9752–57
    [Google Scholar]
  34. Courtemanche N, Pollard TD. 2012. Structural determinants of formin FH1 domain function in actin filament elongation. J. Biol. Chem. 287:7812–20
    [Google Scholar]
  35. Courtemanche N, Pollard TD, Chen Q 2016. Avoiding artefacts when counting polymerized actin in live cells with LifeAct fused to fluorescent proteins. Nat. Cell Biol. 18:676–83
    [Google Scholar]
  36. Dalhaimer P, Pollard TD. 2010. Molecular dynamics simulations of Arp2/3 complex activation. Biophys. J. 99:2568–76
    [Google Scholar]
  37. De La Cruz EM, Pollard TD 1995. Nucleotide-free actin: stabilization by sucrose and nucleotide binding kinetics. Biochemistry 34:5452–61
    [Google Scholar]
  38. Dey SK, Pollard TD. 2018. Involvement of the septation initiation network (SIN) in events during cytokinesis in fission yeast. J. Cell Sci. 131:jcs216895
    [Google Scholar]
  39. Doberstein SK, Baines I, Weigand G, Korn ED, Pollard TD 1993. Inhibition of contractile vacuole function in vivo by myosin-I antibodies. Nature 365:841–43
    [Google Scholar]
  40. Doberstein SK, Pollard TD. 1992. Localization and specificity of the phospholipid and actin binding sites on the tail of Acanthamoeba myosin-IC. J. Cell Biol. 117:1241–49
    [Google Scholar]
  41. Drenckhahn D, Pollard TD. 1986. Elongation of actin filaments is a diffusion-limited reaction at the barbed end and is accelerated by inert macromolecules. J. Biol. Chem. 261:12754–58
    [Google Scholar]
  42. Dujardin F. 1835. Recherches sur les organismes inférieurs. Ann. Sci. Nat. Zool. 4:343–77
    [Google Scholar]
  43. Egile C, Loisel TP, Laurent V, Li R, Pantaloni D et al. 1999. Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. J. Cell Biol. 146:1319–32
    [Google Scholar]
  44. Espinoza S, Metskas LA, Chou SZ, Rhoades E, Pollard TD 2018. Conformational changes in Arp2/3 complex induced by WASp-VCA and actin filaments. PNAS 115:E8642–51
    [Google Scholar]
  45. Evangelista M, Klebl BM, Tong AH, Webb BA, Leeuw T et al. 2000. A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex. J. Cell Biol. 148:353–62
    [Google Scholar]
  46. Evangelista M, Pruyne D, Amberg DC, Boone C, Bretscher A 2002. Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat. Cell Biol. 4:32–41
    [Google Scholar]
  47. Frey-Wyssling A. 1948. Submicroscopic Morphology of Protoplasm and its Derivatives New York: Elsevier
  48. Frieden C. 1983. Polymerization of actin: mechanism of the Mg2+-induced process at pH 8 and 20°C. PNAS 80:6513–17
    [Google Scholar]
  49. Fruton JS, Simmonds S. 1958. General Biochemistry New York: John Wiley & Sons1077
  50. Fujiwara K, Pollard TD. 1976. Fluorescent antibody localization of myosin in the cytoplasm, cleavage furrow, and mitotic spindle of human cells. J. Cell Biol. 71:848–75
    [Google Scholar]
  51. Gibbons IR, Rowe AJ. 1965. Dynein: a protein with adenosine triphosphatase activity from cilia. Science 149:424–26
    [Google Scholar]
  52. Goldschmidt-Clermont PJ, Machesky LM, Baldassare JJ, Pollard TD 1990. The actin–binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C. Science 247:1575–78
    [Google Scholar]
  53. Goss JW, Kim S, Bledsoe H, Pollard TD 2014. Characterization the roles of Blt1p in fission yeast cytokinesis. Mol. Biol. Cell 25:1946–57
    [Google Scholar]
  54. Griffith LM, Pollard TD. 1978. Evidence for actin filament–microtubule interaction mediated by microtubule-associated proteins. J. Cell Biol. 78:958–65
    [Google Scholar]
  55. Guertin DA, Trautmann S, McCollum D 2002. Cytokinesis in eukaryotes. Microbiol. Mol. Biol. Rev. 66:155–78
    [Google Scholar]
  56. Hammer JA III, Jung G, Korn ED 1986. Genetic evidence that Acanthamoeba myosin-I is a true myosin. PNAS 83:4655–59
    [Google Scholar]
  57. Hatano S, Oosawa F. 1966. Isolation and characterization of plasmodium actin. Biochim. Biophys. Acta 127:488–98
    [Google Scholar]
  58. Hatano S, Tazawa M. 1968. Isolation, purification and characterization of myosin B from myxomycete plasmodium. Biochim. Biophys. Acta 154:507–19
    [Google Scholar]
  59. Higgs HN, Pollard TD. 2000. Activation by Cdc42 and PIP2 of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex. J. Cell Biol. 150:1311–20
    [Google Scholar]
  60. Holmes KC, Popp D, Gebhard W, Kabsch W 1990. Atomic model of the actin filament. Nature 347:44–49
    [Google Scholar]
  61. Huxley HE. 1963. Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle. J. Mol. Biol. 7:281–308
    [Google Scholar]
  62. Huxley HE. 1969. Mechanism of muscular contraction. Science 164:1356–66
    [Google Scholar]
  63. Isenberg GH, Aebi U, Pollard TD 1980. An actin binding protein from Acanthamoeba regulates actin filament polymerization and interactions. Nature 288:455–59
    [Google Scholar]
  64. Ishikawa H, Bischoff R, Holtzer H 1969. Formation of arrowhead complexes with heavy meromyosin in a variety of cell types. J. Cell Biol. 43:312–28
    [Google Scholar]
  65. Jochova J, Rupes I, Streiblova E 1991. F-actin contractile rings in protoplasts of the yeast Schizosaccharomyces. Cell Biol. Int. Rep 15:607–10
    [Google Scholar]
  66. Kabsch W, Mannherz HG, Suck D, Pai EF, Holmes KC 1990. Atomic structure of the actin:DNase I complex. Nature 347:37–44
    [Google Scholar]
  67. Kaiser DA, Pollard TD. 1996. Characterization of actin and poly-l-proline binding sites of Acanthamoeba profilin with monoclonal antibodies and by mutagenesis. J. Mol. Biol. 256:89–107
    [Google Scholar]
  68. Kaiser DA, Vinson VK, Murphy DB, Pollard TD 1999. Profilin is predominantly associated with monomeric actin in Acanthamoeba. J. Cell Sci 112:3779–90
    [Google Scholar]
  69. Kane RE. 1975. Preparation and purification of polymerized actin from sea-urchin egg extracts. J. Cell Biol. 66:305–15
    [Google Scholar]
  70. Kelleher JF, Atkinson SJ, Pollard TD 1995. Sequences, structural models, and cellular localization of the actin-related proteins Arp2 and Arp3 from Acanthamoeba. J. Cell Biol 131:385–97 https://doi.org/10.1083/jcb.131.2.385
    [Crossref] [Google Scholar]
  71. Kiehart DP, Pollard TD. 1984. Stimulation of Acanthamoeba actomyosin ATPase activity by myosin-II polymerization. Nature 308:864–66
    [Google Scholar]
  72. Kitayama C, Sugimoto A, Yamamoto M 1997. Type II myosin heavy chain encoded by the myo2 gene composes the contractile ring during cytokinesis in Schizosaccharomyces pombe. J. Cell Biol 137:1309–19
    [Google Scholar]
  73. Korn ED, Wright PL. 1973. Macromolecular composition of an amoeba plasma membrane. J. Biol. Chem. 248:439–47
    [Google Scholar]
  74. Kouyama T, Mihashi K. 1981. Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. FEBS J 114:33–38
    [Google Scholar]
  75. 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
    [Google Scholar]
  76. Kovar DR, Kuhn JR, Tichy AL, Pollard TD 2003. The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin. J. Cell Biol. 161:875–87
    [Google Scholar]
  77. Kovar DR, Pollard TD. 2004. Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces. PNAS 101:14725–30
    [Google Scholar]
  78. Laplante C, Berro J, Karatekin E, Lee R, Hernandez-Leyva A, Pollard TD 2015. Three myosins contribute uniquely to the assembly and constriction of the cytokinetic contractile ring in fission yeast. Curr. Biol. 25:1955–65
    [Google Scholar]
  79. Laplante C, Huang F, Tebbs IR, Bewersdorf J, Pollard TD 2016. Molecular organization of cytokinesis nodes and contractile rings by super-resolution fluorescence microscopy of live fission yeast. PNAS 113:E5876–85
    [Google Scholar]
  80. Lassing I, Lindberg U. 1985. Specific interaction between phosphatidylinositol 4,5 bisphosphate and profilactin. Nature 314:472–74
    [Google Scholar]
  81. Lazarides E, Weber K. 1974. Actin antibody: the specific visualization of actin filaments in non-muscle cells. PNAS 71:2268–72
    [Google Scholar]
  82. Lechler T, Shevchenko A, Li R 2000. Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization. J. Cell Biol. 148:363–73
    [Google Scholar]
  83. Lee WL, Bezanilla M, Pollard TD 2000. Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASp. J. Cell Biol. 151:789–800
    [Google Scholar]
  84. Loisel TP, Boujemaa R, Pantaloni D, Carlier MF 1999. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature 401:613–16
    [Google Scholar]
  85. Lord M, Laves E, Pollard TD 2005. Cytokinesis depends on the motor domains of myosin-II in fission yeast but not in budding yeast. Mol. Biol. Cell 16:5346–55
    [Google Scholar]
  86. Lord M, Pollard TD. 2004. UCS protein Rng3p activates actin filament gliding by fission yeast myosin-II. J. Cell Biol. 167:315–25
    [Google Scholar]
  87. Ma L, Rohatgi R, Kirschner MW 1998. The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42. PNAS 95:15362–67
    [Google Scholar]
  88. Mabuchi I, Okuno M. 1977. The effect of myosin antibody on the division of starfish blastomeres. J. Cell Biol. 74:251–63
    [Google Scholar]
  89. Machesky LM, Atkinson SJ, Ampe C, Vandekerckhove J, Pollard TD 1994. Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin agarose. J. Cell Biol. 127:107–15
    [Google Scholar]
  90. Machesky LM, Goldschmidt-Clermont PJ, Pollard TD 1990. The affinities of human platelet and Acanthamoeba profilin isoforms for polyphosphoinositides account for their relative abilities to inhibit phospholipase C. Cell Regul 1:937–50
    [Google Scholar]
  91. Machesky LM, Insall RH. 1998. Scar1 and the related Wiskott-Aldrich syndrome protein WASP regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 8:1347–56
    [Google Scholar]
  92. Machesky LM, Mullins DM, Higgs HN, Kaiser DA, Blanchoin L et al. 1999. Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex. PNAS 96:3739–44
    [Google Scholar]
  93. Maciver SK, Zot HG, Pollard TD 1991. Characterization of actin filament severing by actophorin from Acanthamoeba castellanii. J. Cell Biol 115:1611–20
    [Google Scholar]
  94. MacLean-Fletcher SD, Pollard TD. 1980. Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors. J. Cell Biol. 85:414–28
    [Google Scholar]
  95. Marchand JB, Kaiser DA, Pollard TD, Higgs HN 2001. Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex. Nat. Cell Biol. 3:76–82
    [Google Scholar]
  96. Maruta H, Korn ED. 1977a. Acanthamoeba cofactor protein is a heavy-chain kinase required for actin activation of Mg2+-ATPase activity of Acanthamoeba myosin-I. J. Biol. Chem. 252:8329–32
    [Google Scholar]
  97. Maruta H, Korn ED. 1977b. Acanthamoeba myosin-II. J. Biol. Chem. 252:6501–9
    [Google Scholar]
  98. Maupin P, Pollard TD. 1983. Improved preservation and staining of HeLa cell actin filaments, clathrin coated membranes and other cytoplasmic structures by tannic acid–glutaraldehyde–saponin fixation. J. Cell Biol. 96:51–62
    [Google Scholar]
  99. Maupin P, Pollard TD. 1986. Arrangement of actin filaments and myosin-like filaments in the contractile ring and of actin-like filaments in the mitotic spindle of dividing HeLa cells. J. Ultrastruct. Mol. Struct. Res. 94:92–103
    [Google Scholar]
  100. Maupin-Szamier P, Pollard TD. 1978. Actin filament destruction by osmium tetroxide. J. Cell Biol. 77:837–52
    [Google Scholar]
  101. McIntosh JR. 2017. Assessing the contributions of motor enzymes and microtubule dynamics to mitotic chromosome motions. Annu. Rev. Cell Dev. Biol. 33:1–22
    [Google Scholar]
  102. Mockrin SC, Korn ED. 1980. Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5′-triphosphate. Biochemistry 19:5359–62
    [Google Scholar]
  103. Mogilner A, Oster G. 1996. Cell motility driven by actin polymerization. Biophys. J. 71:3030–45
    [Google Scholar]
  104. Motegi F, Nakano K, Kitayama C, Yamamoto M, Mabuchi I 1997. Identification of Myo3, a second type-II myosin heavy chain in the fission yeast Schizosaccharomyces pombe. FEBS Lett 420:161–66
    [Google Scholar]
  105. Mullins RD, Heuser JA, Pollard TD 1998. The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. PNAS 95:6181–86
    [Google Scholar]
  106. Mullins RD, Stafford WF, Pollard TD 1997. Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba. J. Cell Biol 136:331–43
    [Google Scholar]
  107. Niederman R, Pollard TD. 1975. Human platelet myosin. II. In vitro assembly and structure of myosin filaments. J. Cell Biol. 67:72–92
    [Google Scholar]
  108. Nishida E, Maekawa S, Muneyuki E, Sakai H 1984. Action of a 19K protein from porcine brain on actin polymerization: a new functional class of actin-binding proteins. J. Biochem. 95:387–98
    [Google Scholar]
  109. Nolen BJ, Pollard TD. 2007. Insights into the influence of nucleotides on actin family proteins from seven structures of Arp2/3 complex. Mol. Cell 26:449–57
    [Google Scholar]
  110. Nolen BJ, Tomasevic N, Russell A, Pierce DW, Jia Z et al. 2009. Characterization of two classes of small molecule inhibitors of Arp2/3 complex. Nature 460:1031–34
    [Google Scholar]
  111. Odronitz F, Kollmar M. 2007. Drawing the tree of eukaryotic life based on the analysis of 2,269 manually annotated myosins from 328 species. Genome Biol 8:R196
    [Google Scholar]
  112. Ostap EM, Pollard TD. 1996. Biochemical kinetic characterization of the Acanthamoeba myosin-I ATPase. J. Cell Biol. 132:1053–60
    [Google Scholar]
  113. 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
    [Google Scholar]
  114. Pantaloni D, Boujemaa R, Didry D, Gounon P, Carlier MF 2000. The Arp2/3 complex branches filament barbed ends: functional antagonism with capping proteins. Nat. Cell Biol. 2:385–91
    [Google Scholar]
  115. Paul AS, Pollard TD. 2008. The role of the FH1 domain and profilin in formin-mediated actin-filament elongation and nucleation. Curr. Biol. 18:9–19
    [Google Scholar]
  116. Paul AS, Pollard TD. 2009. Energetic requirements for processive elongation of actin filaments by FH1FH2-formins. J. Biol. Chem. 284:12533–40
    [Google Scholar]
  117. Petrella EC, Machesky LM, Kaiser DA, Pollard TD 1996. Structural requirements and thermodynamics of the interaction of proline peptides with profilin. Biochemistry 35:16535–43
    [Google Scholar]
  118. Pollard TD. 1976a. Cytoskeletal functions of cytoplasmic contractile proteins. J. Supramol. Struct. 5:317–34
    [Google Scholar]
  119. Pollard TD. 1976b. The role of actin in the temperature-dependent gelation and contraction of extracts of Acanthamoeba. J. Cell Biol 68:579–601
    [Google Scholar]
  120. Pollard TD. 1982. Structure and polymerization of Acanthamoeba myosin-II filaments. J. Cell Biol. 95:816–25
    [Google Scholar]
  121. Pollard TD. 1986. Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J. Cell Biol. 103:2747–54 https://doi.org/10.1083/jcb.103.6.2747
    [Crossref] [Google Scholar]
  122. Pollard TD. 2003. Functional genomics of cell morphology using RNA interference: Pick your style, broad or deep. J. Biol. 2:25
    [Google Scholar]
  123. Pollard TD. 2012. Political advocacy by the American Society for Cell Biology and its partners. Mol. Biol. Cell 23:4171–74
    [Google Scholar]
  124. Pollard TD. 2017. Nine unanswered questions about cytokinesis. J. Cell Biol. 216:3007–16
    [Google Scholar]
  125. Pollard TD, Bhandari D, Maupin P, Wachsstock D, Weeds AG, Zot HG 1993. Direct visualization by electron microscopy of the weakly bound intermediates in the actomyosin adenosine triphosphatase cycle. Biophys. J. 64:454–71
    [Google Scholar]
  126. Pollard TD, Blanchoin L, Mullins RD 2000. Molecular mechanisms controlling actin filament dynamics in nonmuscle cells. Annu. Rev. Biophys. Biomol. Struct. 29:545–76
    [Google Scholar]
  127. Pollard TD, Borisy GG. 2003. Cellular motility driven by assembly and disassembly of actin filaments. Cell 112:453–65
    [Google Scholar]
  128. Pollard TD, Cooper JA. 1984. Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation. Biochemistry 23:6631–41
    [Google Scholar]
  129. Pollard TD, Ito S. 1970. Cytoplasmic filaments of Amoeba proteus. I. The role of filaments in consistency changes and movement. J. Cell Biol. 46:267–89
    [Google Scholar]
  130. Pollard TD, Korn ED. 1971. Filaments of Amoeba proteus. II. Binding of heavy meromyosin by thin filaments in motile cytoplasmic extracts. J. Cell Biol. 48:216–19
    [Google Scholar]
  131. Pollard TD, Korn ED. 1973a. Acanthamoeba myosin. I. Isolation from Acanthamoeba castellanii of an enzyme similar to muscle myosin. J. Biol. Chem. 248:4682–90
    [Google Scholar]
  132. Pollard TD, Korn ED. 1973b. Acanthamoeba myosin. II. Interaction with actin and with a new cofactor protein required for actin activation of Mg2+ adenosine triphosphatase activity. J. Biol. Chem. 248:4691–97
    [Google Scholar]
  133. Pollard TD, Korn ED. 1973c. Electron microscopic identification of actin associated with isolated amoeba plasma membranes. J. Biol. Chem. 248:448–50
    [Google Scholar]
  134. Pollard TD, Mooseker MS. 1981. Direct measurement of actin polymerization rate constants by electron microscopy of actin filaments nucleated by isolated microvillus cores. J. Cell Biol. 88:654–59
    [Google Scholar]
  135. Pollard TD, Shelton E, Weihing RR, Korn ED 1970. Ultrastructural characterization of F-actin isolated from Acanthamoeba castellanii and identification of cytoplasmic filaments as F-actin by reaction with rabbit heavy meromyosin. J. Mol. Biol. 50:91–97
    [Google Scholar]
  136. Pollard TD, Stafford WF, Porter ME 1978. Characterization of a second myosin from Acanthamoeba castellanii. J. Biol. Chem 253:4798–808
    [Google Scholar]
  137. Pollard TD, Thomas SM, Niederman R 1974. Human platelet myosin. I. Purification by a rapid method applicable to other nonmuscle cells. Anal. Biochem. 60:258–66
    [Google Scholar]
  138. Pollard TD, Weeds AG. 1984. The rate constant for ATP hydrolysis by polymerized actin. FEBS Lett 170:94–98
    [Google Scholar]
  139. Pollard TD, Wu J-Q. 2010. Understanding cytokinesis: lessons from fission yeast. Nat. Rev. Mol. Cell Biol. 11:149–55
    [Google Scholar]
  140. Pomerat CM, Rounds DE, Raiborn CW, Pollard TD 1964. Observations on newborn rat dorsal root ganglia in vitro following gamma irradiation. Response of the Nervous System to Ionizing Radiation TJ Haley, RS Solomon 175–200 New York: Little, Brown
    [Google Scholar]
  141. Pu K-M, Akamatsu M, Pollard TD 2015. The fission yeast septation initiation network controls type 1 cytokinesis nodes. J. Cell Sci. 128:441–46
    [Google Scholar]
  142. Rappaport R. 1967. Cell division: direct measurement of maximum tension exerted by furrow of echinoderm eggs. Science 156:1241–43
    [Google Scholar]
  143. Robinson RC, Turbedsky K, Kaiser DA, Marchand JB, Higgs HN et al. 2001. Crystal structure of Arp2/3 complex. Science 294:1679–84
    [Google Scholar]
  144. Rohatgi R, Ma L, Miki H, Lopez M, Kirchhausen T et al. 1999. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97:221–31
    [Google Scholar]
  145. Rouiller I, Xu XP, Amann KJ, Egile C, Nickell S et al. 2008. The structural basis of actin filament branching by the Arp2/3 complex. J. Cell Biol. 180:887–95
    [Google Scholar]
  146. Sagot I, Rodal AA, Moseley J, Goode BL, Pellman D 2002. An actin nucleation mechanism mediated by Bni1 and profilin. Nat. Cell Biol. 4:626–31
    [Google Scholar]
  147. Saha S, Pollard TD. 2012a. Anillin-related protein Mid1p coordinates the assembly of the cytokinetic contractile ring in fission yeast. Mol. Biol. Cell 23:3982–92
    [Google Scholar]
  148. Saha S, Pollard TD. 2012b. Characterization of structural and functional domains of anillin-related protein Mid1p that contribute to cytokinesis in fission yeast. Mol. Biol. Cell 23:3993–4007
    [Google Scholar]
  149. Sato M, Schwarz WH, Pollard TD 1987. Dependence of the mechanical-properties of actin alpha-actinin gels on deformation rate. Nature 325:828–30
    [Google Scholar]
  150. Schroeder TE. 1973. Actin in dividing cells: Contractile ring filaments bind heavy meromyosin. PNAS 70:1688–92
    [Google Scholar]
  151. Schutt CE, Myslik JC, Rozycki MD, Goonesekere NC, Lindberg U 1993. The structure of crystalline profilin-beta-actin. Nature 365:810–16
    [Google Scholar]
  152. Selden SC, Pollard TD. 1983. Phosphorylation of microtubule associated proteins regulates their interaction with actin filaments. J. Biol. Chem 258:7064–71
    [Google Scholar]
  153. Simanis V 2015. Pombe's thirteen: control of fission yeast cell division by the septation initiation network. J. Cell Sci 128:1465–74
    [Google Scholar]
  154. Sinard JH, Pollard TD. 1989. Microinjection into Acanthamoeba castellanii of monoclonal antibodies to myosin-II slows but does not stop cell locomotion. Cell Motil. Cytoskel. 12:42–53
    [Google Scholar]
  155. Sinard JH, Pollard TD. 1990. Acanthamoeba myosin-II minifilaments assemble on a millisecond time scale with rate constants greater than those expected for a diffusion limited reaction. J. Biol. Chem. 265:3654–60
    [Google Scholar]
  156. Sinard JH, Rimm DL, Pollard TD 1990. Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. II. Assembly properties of tails with NH2- and COOH-terminal deletions. J. Cell Biol. 111:2417–26
    [Google Scholar]
  157. Sinard JH, Stafford WF, Pollard TD 1989. The mechanism of assembly of Acanthamoeba myosin-II minifilaments: Minifilaments assemble by 3 successive dimerization steps. J. Cell Biol. 109:1537–47
    [Google Scholar]
  158. Sirotkin V, Berro J, Macmillan K, Zhao-Law L, Yuan S, Pollard TD 2010. Quantitative analysis of the mechanism of actin patch assembly and disassembly in fission yeast. Mol. Biol. Cell 21:2894–904
    [Google Scholar]
  159. Stachowiak MR, Laplante C, Chin HF, Guirao B, Karatekin E et al. 2014. Mechanism of cytokinetic contractile ring constriction in fission yeast. Dev. Cell 29:547–61
    [Google Scholar]
  160. Straub FB, Feuer G. 1950. Adenosinetriphosphate. The functional group of actin. Biochim. Biophys. Acta 4:455–70
    [Google Scholar]
  161. Svitkina TM, Borisy GG. 1999. Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 145:1009–26
    [Google Scholar]
  162. Svitkina TM, Verkhovsky AB, McQuade KM, Borisy GG 1997. Analysis of the actin–myosin II system in fish epidermal keratocytes: mechanism of cell body translocation. J. Cell Biol. 139:397–415
    [Google Scholar]
  163. Tanaka M, Shibata H. 1985. Poly(l-proline)-binding proteins from chick embryos are a profilin and a profilactin. Eur. J. Biochem. 151:291–97
    [Google Scholar]
  164. Tebbs IR, Pollard TD. 2013. Separate roles of IQGAP Rng2p in forming and constricting the S. pombe cytokinetic contractile ring. Mol. Biol. Cell 24:1904–17
    [Google Scholar]
  165. Theriot JA, Mitchison TJ. 1991. Actin microfilament dynamics in locomoting cells. Nature 352:126–31
    [Google Scholar]
  166. Thompson CM, Wolpert L. 1963. Isolation of motile cytoplasm from Amoeba proteus. Exp. Cell Res 32:156–60
    [Google Scholar]
  167. Ti S-C, Jurgenson C, Nolen BJ, Pollard TD 2011. Structural and biochemical characterization of two binding sites for nucleation promoting factor WASp-VCA on Arp2/3 complex. PNAS 108:E463–71
    [Google Scholar]
  168. Ti S-C, Pollard TD. 2011. Purification of actin from fission yeast S. pombe and characterization of functional differences from muscle actin. J. Biol. Chem. 286:5784–92
    [Google Scholar]
  169. Tilney LG. 1978. Polymerization of actin. V. A new organelle, the actomere, that initates the assembly of actin filaments in Thyone sperm. J. Cell Biol. 77:551–64
    [Google Scholar]
  170. Tobacman LS, Korn ED. 1983. The kinetics of actin nucleation and polymerization. J. Biol. Chem. 258:3207–14
    [Google Scholar]
  171. Tseng PC, Pollard TD. 1982. Mechanism of action of Acanthamoeba profilin: demonstration of actin species specificity and regulation by micromolar concentrations of MgCl2. J. Cell Biol. 94:213–18
    [Google Scholar]
  172. Vandekerckhove J, Kaiser DA, Pollard TD 1989. Acanthamoeba actin and profilin can be crosslinked between glutamic acid 364 of actin and lysine 115 of profilin. J. Cell Biol. 109:619–26
    [Google Scholar]
  173. Vavylonis D, Wu J-Q, Hao S, O'Shaughnessy B, Pollard TD 2008. Assembly mechanism of the contractile ring for cytokinesis by fission yeast. Science 319:97–100
    [Google Scholar]
  174. Vinson VK, Archer SJ, Lattman EE, Pollard TD, Torchia DA 1993. Three-dimensional solution structure of Acanthamoeba profilin-I. J. Cell Biol. 122:1277–83
    [Google Scholar]
  175. Vinson VK, De La Cruz EM, Higgs HN, Pollard TD 1998. Interactions of Acanthamoeba profilin with actin and nucleotides bound to actin. Biochemistry 37:10871–80
    [Google Scholar]
  176. Wachsstock DH, Schwarz WH, Pollard TD 1994. Cross-linker dynamics determine the mechanical-properties in actin gels. Biophys. J. 66:801–9
    [Google Scholar]
  177. Wang Y. 1985. Exchange of actin subunits at the leading edge of living fibroblasts: possible role of treadmilling. J. Cell Biol. 101:597–602
    [Google Scholar]
  178. Weihing RR, Korn ED. 1969. Amoeba actin: the presence of 3-methylhistidine. Biochem. Biophys. Res. Commun. 35:906–12
    [Google Scholar]
  179. Welch MD, Iwamatsu A, Mitchison TJ 1997. Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature 385:265–69
    [Google Scholar]
  180. Winter D, Lechler T, Li R 1999. Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein. Curr. Biol. 9:501–4
    [Google Scholar]
  181. Winter D, Podtelejnikov AV, Mann M, Li R 1997. The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches. Curr. Biol. 7:519–29
    [Google Scholar]
  182. Woodrum DT, Rich SA, Pollard TD 1975. Evidence for biased bidirectional polymerization of actin filaments using heavy meromyosin prepared by an improved method. J. Cell Biol. 67:231–37
    [Google Scholar]
  183. Wu JQ, Kuhn JR, Kovar DR, Pollard TD 2003. Spatial and temporal pathway for assembly and constriction of the contractile ring in fission yeast cytokinesis. Dev. Cell 5:723–34
    [Google Scholar]
  184. Wu JQ, Pollard TD. 2005. Counting cytokinesis proteins globally and locally in fission yeast. Science 310:310–14
    [Google Scholar]
  185. Wu JQ, Sirotkin V, Kovar DR, Lord M, Beltzner CC et al. 2006. Assembly of the cytokinetic contractile ring from a broad band of nodes in fission yeast. J. Cell Biol. 174:391–402
    [Google Scholar]
  186. Xu J, Wirtz D, Pollard TD 1998. Dynamic cross-linking by alpha-actinin determines the mechanical properties of actin filament networks. J. Biol. Chem. 273:9570–76
    [Google Scholar]
  187. 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
    [Google Scholar]
  188. Yarar D, To W, Abo A, Welch MD 1999. The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex. Curr. Biol. 9:555–58
    [Google Scholar]
  189. Zot HG, Doberstein SK, Pollard TD 1992. Myosin-I moves actin filaments on a phospholipid substrate: implications for membrane targeting. J. Cell Biol. 116:367–76
    [Google Scholar]
/content/journals/10.1146/annurev-cellbio-100818-125427
Loading
/content/journals/10.1146/annurev-cellbio-100818-125427
Loading

Data & Media loading...

  • Article Type: Review Article
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error