Skip to main content
NCBI home page
Molecular Biology of the Cell logoLink to Molecular Biology of the Cell
. 1992 Dec;3(12):1309–1315. doi: 10.1091/mbc.3.12.1309

Compare and contrast actin filaments and microtubules.

T J Mitchison 1
PMCID: PMC275701  PMID: 1493331

Full text

PDF
1309

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Beese L., Stubbs G., Cohen C. Microtubule structure at 18 A resolution. J Mol Biol. 1987 Mar 20;194(2):257–264. doi: 10.1016/0022-2836(87)90373-1. [DOI] [PubMed] [Google Scholar]
  2. Bourne H. R., Sanders D. A., McCormick F. The GTPase superfamily: a conserved switch for diverse cell functions. Nature. 1990 Nov 8;348(6297):125–132. doi: 10.1038/348125a0. [DOI] [PubMed] [Google Scholar]
  3. Brinkley B. R. Microtubule organizing centers. Annu Rev Cell Biol. 1985;1:145–172. doi: 10.1146/annurev.cb.01.110185.001045. [DOI] [PubMed] [Google Scholar]
  4. Brylawski B. P., Caplow M. Rate for nucleotide release from tubulin. J Biol Chem. 1983 Jan 25;258(2):760–763. [PubMed] [Google Scholar]
  5. Buss F., Temm-Grove C., Henning S., Jockusch B. M. Distribution of profilin in fibroblasts correlates with the presence of highly dynamic actin filaments. Cell Motil Cytoskeleton. 1992;22(1):51–61. doi: 10.1002/cm.970220106. [DOI] [PubMed] [Google Scholar]
  6. Caplow M. Microtubule dynamics. Curr Opin Cell Biol. 1992 Feb;4(1):58–65. doi: 10.1016/0955-0674(92)90059-l. [DOI] [PubMed] [Google Scholar]
  7. Carlier M. F. Role of nucleotide hydrolysis in the dynamics of actin filaments and microtubules. Int Rev Cytol. 1989;115:139–170. doi: 10.1016/s0074-7696(08)60629-4. [DOI] [PubMed] [Google Scholar]
  8. Carlsson L., Nyström L. E., Sundkvist I., Markey F., Lindberg U. Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells. J Mol Biol. 1977 Sep 25;115(3):465–483. doi: 10.1016/0022-2836(77)90166-8. [DOI] [PubMed] [Google Scholar]
  9. Condeelis J., Bresnick A., Demma M., Dharmawardhane S., Eddy R., Hall A. L., Sauterer R., Warren V. Mechanisms of amoeboid chemotaxis: an evaluation of the cortical expansion model. Dev Genet. 1990;11(5-6):333–340. doi: 10.1002/dvg.1020110504. [DOI] [PubMed] [Google Scholar]
  10. Cooley L., Verheyen E., Ayers K. chickadee encodes a profilin required for intercellular cytoplasm transport during Drosophila oogenesis. Cell. 1992 Apr 3;69(1):173–184. doi: 10.1016/0092-8674(92)90128-y. [DOI] [PubMed] [Google Scholar]
  11. Dabiri G. A., Sanger J. M., Portnoy D. A., Southwick F. S. Listeria monocytogenes moves rapidly through the host-cell cytoplasm by inducing directional actin assembly. Proc Natl Acad Sci U S A. 1990 Aug;87(16):6068–6072. doi: 10.1073/pnas.87.16.6068. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Drechsel D. N., Hyman A. A., Cobb M. H., Kirschner M. W. Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol Biol Cell. 1992 Oct;3(10):1141–1154. doi: 10.1091/mbc.3.10.1141. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Drubin D., Kobayashi S., Kellogg D., Kirschner M. Regulation of microtubule protein levels during cellular morphogenesis in nerve growth factor-treated PC12 cells. J Cell Biol. 1988 May;106(5):1583–1591. doi: 10.1083/jcb.106.5.1583. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Gelfand V. I., Bershadsky A. D. Microtubule dynamics: mechanism, regulation, and function. Annu Rev Cell Biol. 1991;7:93–116. doi: 10.1146/annurev.cb.07.110191.000521. [DOI] [PubMed] [Google Scholar]
  15. Goldschmidt-Clermont P. J., Furman M. I., Wachsstock D., Safer D., Nachmias V. T., Pollard T. D. The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cells. Mol Biol Cell. 1992 Sep;3(9):1015–1024. doi: 10.1091/mbc.3.9.1015. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Goldschmidt-Clermont P. J., Machesky L. M., Doberstein S. K., Pollard T. D. Mechanism of the interaction of human platelet profilin with actin. J Cell Biol. 1991 Jun;113(5):1081–1089. doi: 10.1083/jcb.113.5.1081. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Haarer B. K., Lillie S. H., Adams A. E., Magdolen V., Bandlow W., Brown S. S. Purification of profilin from Saccharomyces cerevisiae and analysis of profilin-deficient cells. J Cell Biol. 1990 Jan;110(1):105–114. doi: 10.1083/jcb.110.1.105. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Heacock C. S., Bamburg J. R. The quantitation of G- and F-actin in cultured cells. Anal Biochem. 1983 Nov;135(1):22–36. doi: 10.1016/0003-2697(83)90725-x. [DOI] [PubMed] [Google Scholar]
  19. Heidemann S. R., Buxbaum R. E. Tension as a regulator and integrator of axonal growth. Cell Motil Cytoskeleton. 1990;17(1):6–10. doi: 10.1002/cm.970170103. [DOI] [PubMed] [Google Scholar]
  20. Holmes K. C., Popp D., Gebhard W., Kabsch W. Atomic model of the actin filament. Nature. 1990 Sep 6;347(6288):44–49. doi: 10.1038/347044a0. [DOI] [PubMed] [Google Scholar]
  21. Joshi H. C., Palacios M. J., McNamara L., Cleveland D. W. Gamma-tubulin is a centrosomal protein required for cell cycle-dependent microtubule nucleation. Nature. 1992 Mar 5;356(6364):80–83. doi: 10.1038/356080a0. [DOI] [PubMed] [Google Scholar]
  22. Kabsch W., Mannherz H. G., Suck D., Pai E. F., Holmes K. C. Atomic structure of the actin:DNase I complex. Nature. 1990 Sep 6;347(6288):37–44. doi: 10.1038/347037a0. [DOI] [PubMed] [Google Scholar]
  23. Kirschner M., Mitchison T. Beyond self-assembly: from microtubules to morphogenesis. Cell. 1986 May 9;45(3):329–342. doi: 10.1016/0092-8674(86)90318-1. [DOI] [PubMed] [Google Scholar]
  24. Kocks C., Gouin E., Tabouret M., Berche P., Ohayon H., Cossart P. L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell. 1992 Feb 7;68(3):521–531. doi: 10.1016/0092-8674(92)90188-i. [DOI] [PubMed] [Google Scholar]
  25. Kolodney M. S., Wysolmerski R. B. Isometric contraction by fibroblasts and endothelial cells in tissue culture: a quantitative study. J Cell Biol. 1992 Apr;117(1):73–82. doi: 10.1083/jcb.117.1.73. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Korn E. D. Actin polymerization and its regulation by proteins from nonmuscle cells. Physiol Rev. 1982 Apr;62(2):672–737. doi: 10.1152/physrev.1982.62.2.672. [DOI] [PubMed] [Google Scholar]
  27. Korn E. D. Biochemistry of actomyosin-dependent cell motility (a review). Proc Natl Acad Sci U S A. 1978 Feb;75(2):588–599. doi: 10.1073/pnas.75.2.588. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Maciver S. K., Zot H. G., Pollard T. D. Characterization of actin filament severing by actophorin from Acanthamoeba castellanii. J Cell Biol. 1991 Dec;115(6):1611–1620. doi: 10.1083/jcb.115.6.1611. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Mandelkow E. M., Mandelkow E., Milligan R. A. Microtubule dynamics and microtubule caps: a time-resolved cryo-electron microscopy study. J Cell Biol. 1991 Sep;114(5):977–991. doi: 10.1083/jcb.114.5.977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Matsudaira P. Modular organization of actin crosslinking proteins. Trends Biochem Sci. 1991 Mar;16(3):87–92. doi: 10.1016/0968-0004(91)90039-x. [DOI] [PubMed] [Google Scholar]
  31. McIntosh J. R., Hering G. E. Spindle fiber action and chromosome movement. Annu Rev Cell Biol. 1991;7:403–426. doi: 10.1146/annurev.cb.07.110191.002155. [DOI] [PubMed] [Google Scholar]
  32. Mitchison T. J., Kirschner M. W. Some thoughts on the partitioning of tubulin between monomer and polymer under conditions of dynamic instability. Cell Biophys. 1987 Dec;11:35–55. doi: 10.1007/BF02797111. [DOI] [PubMed] [Google Scholar]
  33. Mitchison T. J. Microtubule dynamics and kinetochore function in mitosis. Annu Rev Cell Biol. 1988;4:527–549. doi: 10.1146/annurev.cb.04.110188.002523. [DOI] [PubMed] [Google Scholar]
  34. Mitchison T. J. Polewards microtubule flux in the mitotic spindle: evidence from photoactivation of fluorescence. J Cell Biol. 1989 Aug;109(2):637–652. doi: 10.1083/jcb.109.2.637. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Mockrin S. C., Korn E. D. Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5'-triphosphate. Biochemistry. 1980 Nov 11;19(23):5359–5362. doi: 10.1021/bi00564a033. [DOI] [PubMed] [Google Scholar]
  36. Neidl C., Engel J. Exchange of ADP, ATP and 1: N6-ethenoadenosine 5'-triphosphate at G-actin. Equilibrium and kinetics. Eur J Biochem. 1979 Nov 1;101(1):163–169. doi: 10.1111/j.1432-1033.1979.tb04228.x. [DOI] [PubMed] [Google Scholar]
  37. Oakley B. R. Gamma-tubulin: the microtubule organizer? Trends Cell Biol. 1992 Jan;2(1):1–5. doi: 10.1016/0962-8924(92)90125-7. [DOI] [PubMed] [Google Scholar]
  38. Pollard T. D. Assembly and dynamics of the actin filament system in nonmuscle cells. J Cell Biochem. 1986;31(2):87–95. doi: 10.1002/jcb.240310202. [DOI] [PubMed] [Google Scholar]
  39. Pollard T. D. Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J Cell Biol. 1986 Dec;103(6 Pt 2):2747–2754. doi: 10.1083/jcb.103.6.2747. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Purich D. L., Kristofferson D. Microtubule assembly: a review of progress, principles, and perspectives. Adv Protein Chem. 1984;36:133–212. doi: 10.1016/s0065-3233(08)60297-1. [DOI] [PubMed] [Google Scholar]
  41. Ruhnau K., Gaertner A., Wegner A. Kinetic evidence for insertion of actin monomers between the barbed ends of actin filaments and barbed end-bound insertin, a protein purified from smooth muscle. J Mol Biol. 1989 Nov 5;210(1):141–148. doi: 10.1016/0022-2836(89)90296-9. [DOI] [PubMed] [Google Scholar]
  42. Safer D., Elzinga M., Nachmias V. T. Thymosin beta 4 and Fx, an actin-sequestering peptide, are indistinguishable. J Biol Chem. 1991 Mar 5;266(7):4029–4032. [PubMed] [Google Scholar]
  43. Safer D., Golla R., Nachmias V. T. Isolation of a 5-kilodalton actin-sequestering peptide from human blood platelets. Proc Natl Acad Sci U S A. 1990 Apr;87(7):2536–2540. doi: 10.1073/pnas.87.7.2536. [DOI] [PMC free article] [PubMed] [Google Scholar]
  44. Shariff A., Luna E. J. Diacylglycerol-stimulated formation of actin nucleation sites at plasma membranes. Science. 1992 Apr 10;256(5054):245–247. doi: 10.1126/science.1373523. [DOI] [PubMed] [Google Scholar]
  45. Shariff A., Luna E. J. Dictyostelium discoideum plasma membranes contain an actin-nucleating activity that requires ponticulin, an integral membrane glycoprotein. J Cell Biol. 1990 Mar;110(3):681–692. doi: 10.1083/jcb.110.3.681. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Small J. V. The actin cytoskeleton. Electron Microsc Rev. 1988;1(1):155–174. doi: 10.1016/s0892-0354(98)90010-7. [DOI] [PubMed] [Google Scholar]
  47. Theriot J. A., Mitchison T. J. Actin microfilament dynamics in locomoting cells. Nature. 1991 Jul 11;352(6331):126–131. doi: 10.1038/352126a0. [DOI] [PubMed] [Google Scholar]
  48. Theriot J. A., Mitchison T. J. The nucleation-release model of actin filament dynamics in cell motility. Trends Cell Biol. 1992 Aug;2(8):219–222. doi: 10.1016/0962-8924(92)90298-2. [DOI] [PubMed] [Google Scholar]
  49. Theriot J. A., Mitchison T. J., Tilney L. G., Portnoy D. A. The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization. Nature. 1992 May 21;357(6375):257–260. doi: 10.1038/357257a0. [DOI] [PubMed] [Google Scholar]
  50. Tilney L. G., Bonder E. M., DeRosier D. J. Actin filaments elongate from their membrane-associated ends. J Cell Biol. 1981 Aug;90(2):485–494. doi: 10.1083/jcb.90.2.485. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Tilney L. G., DeRosier D. J., Weber A., Tilney M. S. How Listeria exploits host cell actin to form its own cytoskeleton. II. Nucleation, actin filament polarity, filament assembly, and evidence for a pointed end capper. J Cell Biol. 1992 Jul;118(1):83–93. doi: 10.1083/jcb.118.1.83. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Tilney L. G., Portnoy D. A. Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes. J Cell Biol. 1989 Oct;109(4 Pt 1):1597–1608. doi: 10.1083/jcb.109.4.1597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Tilney L. G. The polymerization of actin. III. Aggregates of nonfilamentous actin and its associated proteins: a storage form of actin. J Cell Biol. 1976 Apr;69(1):73–89. doi: 10.1083/jcb.69.1.73. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Walker R. A., O'Brien E. T., Pryer N. K., Soboeiro M. F., Voter W. A., Erickson H. P., Salmon E. D. Dynamic instability of individual microtubules analyzed by video light microscopy: rate constants and transition frequencies. J Cell Biol. 1988 Oct;107(4):1437–1448. doi: 10.1083/jcb.107.4.1437. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Wang Y. L. Exchange of actin subunits at the leading edge of living fibroblasts: possible role of treadmilling. J Cell Biol. 1985 Aug;101(2):597–602. doi: 10.1083/jcb.101.2.597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Wegner A. Head to tail polymerization of actin. J Mol Biol. 1976 Nov;108(1):139–150. doi: 10.1016/s0022-2836(76)80100-3. [DOI] [PubMed] [Google Scholar]

Articles from Molecular Biology of the Cell are provided here courtesy of American Society for Cell Biology

RESOURCES