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. 1984 Jul 1;99(1 Pt 2):33s–37s. doi: 10.1083/jcb.99.1.33s

Interaction of actin filaments with microtubules

T D Pollard, S C Selden, P Maupin
PMCID: PMC2275605  PMID: 6430911

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Selected References

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

  1. Aubin J. E., Weber K., Osborn M. Analysis of actin and microfilament-associated proteins in the mitotic spindle and cleavage furrow of PtK2 cells by immunofluorescence microscopy. A critical note. Exp Cell Res. 1979 Nov;124(1):93–109. doi: 10.1016/0014-4827(79)90260-x. [DOI] [PubMed] [Google Scholar]
  2. Barak L. S., Nothnagel E. A., DeMarco E. F., Webb W. W. Differential staining of actin in metaphase spindles with 7-nitrobenz-2-oxa-1,3-diazole-phallacidin and fluorescent DNase: is actin involved in chromosomal movement? Proc Natl Acad Sci U S A. 1981 May;78(5):3034–3038. doi: 10.1073/pnas.78.5.3034. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Buckley I., Stewart M. Ciliary but not saltatory movements are inhibited by vanadate microinjected into living cultured cells. Cell Motil. 1983;3(2):167–184. doi: 10.1002/cm.970030206. [DOI] [PubMed] [Google Scholar]
  4. Burns R. G., Islam K. Characterisation of the chick brain high molecular weight multiply phosphorylated microtubule associated protein. Eur J Biochem. 1982 Feb;122(1):25–29. doi: 10.1111/j.1432-1033.1982.tb05843.x. [DOI] [PubMed] [Google Scholar]
  5. Burns R. G., Pollard T. D. A dynein-like protein from brain. FEBS Lett. 1974 Apr 1;40(2):274–280. doi: 10.1016/0014-5793(74)80243-7. [DOI] [PubMed] [Google Scholar]
  6. Cande W. Z., Lazarides E., McIntosh J. R. A comparison of the distribution of actin and tubulin in the mammalian mitotic spindle as seen by indirect immunofluorescence. J Cell Biol. 1977 Mar;72(3):552–567. doi: 10.1083/jcb.72.3.552. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Cande W. Z., Wolniak S. M. Chromosome movement in lysed mitotic cells is inhibited by vanadate. J Cell Biol. 1978 Nov;79(2 Pt 1):573–580. doi: 10.1083/jcb.79.2.573. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Forer A., Behnke O. An actin-like component in spermatocytes of a crane fly (Nephrotoma suturalis Loew). I. The spindle. Chromosoma. 1972;39(2):145–173. doi: 10.1007/BF00319840. [DOI] [PubMed] [Google Scholar]
  9. Forman D. S., Brown K. J., Promersberger M. E. Selective inhibition of retrograde axonal transport by erythro-9-[3-(2-hydroxynonyl)]adenine. Brain Res. 1983 Aug 1;272(1):194–197. doi: 10.1016/0006-8993(83)90381-5. [DOI] [PubMed] [Google Scholar]
  10. Gibbons I. R., Cosson M. P., Evans J. A., Gibbons B. H., Houck B., Martinson K. H., Sale W. S., Tang W. J. Potent inhibition of dynein adenosinetriphosphatase and of the motility of cilia and sperm flagella by vanadate. Proc Natl Acad Sci U S A. 1978 May;75(5):2220–2224. doi: 10.1073/pnas.75.5.2220. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Gibbons I. R., Fronk E. A latent adenosine triphosphatase form of dynein 1 from sea urchin sperm flagella. J Biol Chem. 1979 Jan 10;254(1):187–196. [PubMed] [Google Scholar]
  12. Goldberg D. J., Harris D. A., Lubit B. W., Schwartz J. H. Analysis of the mechanism of fast axonal transport by intracellular injection of potentially inhibitory macromolecules: evidence for a possible role of actin filaments. Proc Natl Acad Sci U S A. 1980 Dec;77(12):7448–7452. doi: 10.1073/pnas.77.12.7448. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Griffith L. M., Pollard T. D. Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins. J Cell Biol. 1978 Sep;78(3):958–965. doi: 10.1083/jcb.78.3.958. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Griffith L. M., Pollard T. D. The interaction of actin filaments with microtubules and microtubule-associated proteins. J Biol Chem. 1982 Aug 10;257(15):9143–9151. [PubMed] [Google Scholar]
  15. Herman I. M., Pollard T. D. Comparison of purified anti-actin and fluorescent-heavy meromyosin staining patterns in dividing cells. J Cell Biol. 1979 Mar;80(3):509–520. doi: 10.1083/jcb.80.3.509. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Hinkley R., Telser A. Heavy meromyosin-binding filaments in the mitotic apparatus of mammaliam cells. Exp Cell Res. 1974 May;86(1):161–164. doi: 10.1016/0014-4827(74)90662-4. [DOI] [PubMed] [Google Scholar]
  17. Isenberg G., Schubert P., Kreutzberg G. W. Experimental approach to test the role of actin in axonal transport. Brain Res. 1980 Aug 4;194(2):588–593. doi: 10.1016/0006-8993(80)91247-0. [DOI] [PubMed] [Google Scholar]
  18. Lehrer S. S. Damage to actin filaments by glutaraldehyde: protection by tropomyosin. J Cell Biol. 1981 Aug;90(2):459–466. doi: 10.1083/jcb.90.2.459. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. MacLean-Fletcher S. D., Pollard T. D. Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors. J Cell Biol. 1980 May;85(2):414–428. doi: 10.1083/jcb.85.2.414. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Maupin-Szamier P., Pollard T. D. Actin filament destruction by osmium tetroxide. J Cell Biol. 1978 Jun;77(3):837–852. doi: 10.1083/jcb.77.3.837. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Maupin P., Pollard T. D. 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. 1983 Jan;96(1):51–62. doi: 10.1083/jcb.96.1.51. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Murphy D. B., Wallis K. T., Hiebsch R. R. Identity and origin of the ATPase activity associated with neuronal microtubules. II. Identification of a 50,000-dalton polypeptide with ATPase activity similar to F-1 ATPase from mitochondria. J Cell Biol. 1983 May;96(5):1306–1315. doi: 10.1083/jcb.96.5.1306. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Nishida E., Kuwaki T., Sakai H. Phosphorylation of microtubule-associated proteins (MAPs) and pH of the medium control interaction between MAPs and actin filaments. J Biochem. 1981 Aug;90(2):575–578. doi: 10.1093/oxfordjournals.jbchem.a133510. [DOI] [PubMed] [Google Scholar]
  24. Owaribe K., Masuda H. Isolation and characterization of circumferential microfilament bundles from retinal pigmented epithelial cells. J Cell Biol. 1982 Oct;95(1):310–315. doi: 10.1083/jcb.95.1.310. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Porter M. E., Johnson K. A. Transient state kinetic analysis of the ATP-induced dissociation of the dynein-microtubule complex. J Biol Chem. 1983 May 25;258(10):6582–6587. [PubMed] [Google Scholar]
  26. Pratt M. M. The identification of a dynein ATPase in unfertilized sea urchin eggs. Dev Biol. 1980 Feb;74(2):364–378. doi: 10.1016/0012-1606(80)90438-8. [DOI] [PubMed] [Google Scholar]
  27. Sanger J. W. Presence of actin during chromosomal movement. Proc Natl Acad Sci U S A. 1975 Jun;72(6):2451–2455. doi: 10.1073/pnas.72.6.2451. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Sattilaro R. F., Dentler W. L., LeCluyse E. L. Microtubule-associated proteins (MAPs) and the organization of actin filaments in vitro. J Cell Biol. 1981 Aug;90(2):467–473. doi: 10.1083/jcb.90.2.467. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Schibler M. J., Pickett-Heaps J. D. Mitosis in Oedogonium: spindle microfilaments and the origin of the kinetochore fiber. Eur J Cell Biol. 1980 Oct;22(2):687–698. [PubMed] [Google Scholar]
  30. Selden S. C., Pollard T. D. Phosphorylation of microtubule-associated proteins regulates their interaction with actin filaments. J Biol Chem. 1983 Jun 10;258(11):7064–7071. [PubMed] [Google Scholar]
  31. Sheetz M. P., Spudich J. A. Movement of myosin-coated fluorescent beads on actin cables in vitro. Nature. 1983 May 5;303(5912):31–35. doi: 10.1038/303031a0. [DOI] [PubMed] [Google Scholar]
  32. Tsukita S., Usukura J., Tsukita S., Ishikawa H. The cytoskeleton in myelinated axons: a freeze-etch replica study. Neuroscience. 1982;7(9):2135–2147. doi: 10.1016/0306-4522(82)90125-7. [DOI] [PubMed] [Google Scholar]
  33. Vallee R. Structure and phosphorylation of microtubule-associated protein 2 (MAP 2). Proc Natl Acad Sci U S A. 1980 Jun;77(6):3206–3210. doi: 10.1073/pnas.77.6.3206. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Wolosewick J. J., Porter K. R. Microtrabecular lattice of the cytoplasmic ground substance. Artifact or reality. J Cell Biol. 1979 Jul;82(1):114–139. doi: 10.1083/jcb.82.1.114. [DOI] [PMC free article] [PubMed] [Google Scholar]

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