Skip to main content
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1994 Dec 2;127(6):1779–1782. doi: 10.1083/jcb.127.6.1779

Regulation of Dictyostelium myosin II by phosphorylation: what is essential and what is important?

PMCID: PMC2120310  PMID: 7806558

Full Text

The Full Text of this article is available as a PDF (538.5 KB).

Selected References

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

  1. Berlot C. H., Devreotes P. N., Spudich J. A. Chemoattractant-elicited increases in Dictyostelium myosin phosphorylation are due to changes in myosin localization and increases in kinase activity. J Biol Chem. 1987 Mar 15;262(8):3918–3926. [PubMed] [Google Scholar]
  2. Berlot C. H., Spudich J. A., Devreotes P. N. Chemoattractant-elicited increases in myosin phosphorylation in Dictyostelium. Cell. 1985 Nov;43(1):307–314. doi: 10.1016/0092-8674(85)90036-4. [DOI] [PubMed] [Google Scholar]
  3. Chen P., Ostrow B. D., Tafuri S. R., Chisholm R. L. Targeted disruption of the Dictyostelium RMLC gene produces cells defective in cytokinesis and development. J Cell Biol. 1994 Dec;127(6 Pt 2):1933–1944. doi: 10.1083/jcb.127.6.1933. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Côte G. P., Bukiejko U. Purification and characterization of a myosin heavy chain kinase from Dictyostelium discoideum. J Biol Chem. 1987 Jan 25;262(3):1065–1072. [PubMed] [Google Scholar]
  5. Côté G. P., McCrea S. M. Selective removal of the carboxyl-terminal tail end of the Dictyostelium myosin II heavy chain by chymotrypsin. J Biol Chem. 1987 Sep 25;262(27):13033–13038. [PubMed] [Google Scholar]
  6. De Lozanne A., Spudich J. A. Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination. Science. 1987 May 29;236(4805):1086–1091. doi: 10.1126/science.3576222. [DOI] [PubMed] [Google Scholar]
  7. Egelhoff T. T., Brown S. S., Spudich J. A. Spatial and temporal control of nonmuscle myosin localization: identification of a domain that is necessary for myosin filament disassembly in vivo. J Cell Biol. 1991 Feb;112(4):677–688. doi: 10.1083/jcb.112.4.677. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Egelhoff T. T., Lee R. J., Spudich J. A. Dictyostelium myosin heavy chain phosphorylation sites regulate myosin filament assembly and localization in vivo. Cell. 1993 Oct 22;75(2):363–371. doi: 10.1016/0092-8674(93)80077-r. [DOI] [PubMed] [Google Scholar]
  9. Griffith L. M., Downs S. M., Spudich J. A. Myosin light chain kinase and myosin light chain phosphatase from Dictyostelium: effects of reversible phosphorylation on myosin structure and function. J Cell Biol. 1987 May;104(5):1309–1323. doi: 10.1083/jcb.104.5.1309. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hammer J. A., 3rd The structure and function of unconventional myosins: a review. J Muscle Res Cell Motil. 1994 Feb;15(1):1–10. doi: 10.1007/BF00123827. [DOI] [PubMed] [Google Scholar]
  11. Knecht D. A., Loomis W. F. Antisense RNA inactivation of myosin heavy chain gene expression in Dictyostelium discoideum. Science. 1987 May 29;236(4805):1081–1086. doi: 10.1126/science.3576221. [DOI] [PubMed] [Google Scholar]
  12. Korn E. D., Hammer J. A., 3rd Myosins of nonmuscle cells. Annu Rev Biophys Biophys Chem. 1988;17:23–45. doi: 10.1146/annurev.bb.17.060188.000323. [DOI] [PubMed] [Google Scholar]
  13. Kron S. J., Spudich J. A. Fluorescent actin filaments move on myosin fixed to a glass surface. Proc Natl Acad Sci U S A. 1986 Sep;83(17):6272–6276. doi: 10.1073/pnas.83.17.6272. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kuczmarski E. R., Palivos L., Aguado C., Yao Z. L. Stopped-flow measurement of cytoskeletal contraction: Dictyostelium myosin II is specifically required for contraction of amoeba cytoskeletons. J Cell Biol. 1991 Sep;114(6):1191–1199. doi: 10.1083/jcb.114.6.1191. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kuczmarski E. R., Spudich J. A. Regulation of myosin self-assembly: phosphorylation of Dictyostelium heavy chain inhibits formation of thick filaments. Proc Natl Acad Sci U S A. 1980 Dec;77(12):7292–7296. doi: 10.1073/pnas.77.12.7292. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Kuczmarski E. R., Tafuri S. R., Parysek L. M. Effect of heavy chain phosphorylation on the polymerization and structure of Dictyostelium myosin filaments. J Cell Biol. 1987 Dec;105(6 Pt 2):2989–2997. doi: 10.1083/jcb.105.6.2989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Lück-Vielmetter D., Schleicher M., Grabatin B., Wippler J., Gerisch G. Replacement of threonine residues by serine and alanine in a phosphorylatable heavy chain fragment of Dictyostelium myosin II. FEBS Lett. 1990 Aug 20;269(1):239–243. doi: 10.1016/0014-5793(90)81163-i. [DOI] [PubMed] [Google Scholar]
  18. Manstein D. J., Titus M. A., De Lozanne A., Spudich J. A. Gene replacement in Dictyostelium: generation of myosin null mutants. EMBO J. 1989 Mar;8(3):923–932. doi: 10.1002/j.1460-2075.1989.tb03453.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Ostrow B. D., Chen P., Chisholm R. L. Expression of a myosin regulatory light chain phosphorylation site mutant complements the cytokinesis and developmental defects of Dictyostelium RMLC null cells. J Cell Biol. 1994 Dec;127(6 Pt 2):1945–1955. doi: 10.1083/jcb.127.6.1945. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Pasternak C., Flicker P. F., Ravid S., Spudich J. A. Intermolecular versus intramolecular interactions of Dictyostelium myosin: possible regulation by heavy chain phosphorylation. J Cell Biol. 1989 Jul;109(1):203–210. doi: 10.1083/jcb.109.1.203. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Pasternak C., Spudich J. A., Elson E. L. Capping of surface receptors and concomitant cortical tension are generated by conventional myosin. Nature. 1989 Oct 12;341(6242):549–551. doi: 10.1038/341549a0. [DOI] [PubMed] [Google Scholar]
  22. Ravid S., Spudich J. A. Membrane-bound Dictyostelium myosin heavy chain kinase: a developmentally regulated substrate-specific member of the protein kinase C family. Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):5877–5881. doi: 10.1073/pnas.89.13.5877. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Ravid S., Spudich J. A. Myosin heavy chain kinase from developed Dictyostelium cells. Purification and characterization. J Biol Chem. 1989 Sep 5;264(25):15144–15150. [PubMed] [Google Scholar]
  24. Rayment I., Rypniewski W. R., Schmidt-Bäse K., Smith R., Tomchick D. R., Benning M. M., Winkelmann D. A., Wesenberg G., Holden H. M. Three-dimensional structure of myosin subfragment-1: a molecular motor. Science. 1993 Jul 2;261(5117):50–58. doi: 10.1126/science.8316857. [DOI] [PubMed] [Google Scholar]
  25. Ruppel K. M., Uyeda T. Q., Spudich J. A. Role of highly conserved lysine 130 of myosin motor domain. In vivo and in vitro characterization of site specifically mutated myosin. J Biol Chem. 1994 Jul 22;269(29):18773–18780. [PubMed] [Google Scholar]
  26. Sellers J. R. Regulation of cytoplasmic and smooth muscle myosin. Curr Opin Cell Biol. 1991 Feb;3(1):98–104. doi: 10.1016/0955-0674(91)90171-t. [DOI] [PubMed] [Google Scholar]
  27. Spudich J. A. In pursuit of myosin function. Cell Regul. 1989 Nov;1(1):1–11. doi: 10.1091/mbc.1.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Tan J. L., Ravid S., Spudich J. A. Control of nonmuscle myosins by phosphorylation. Annu Rev Biochem. 1992;61:721–759. doi: 10.1146/annurev.bi.61.070192.003445. [DOI] [PubMed] [Google Scholar]
  29. Tan J. L., Spudich J. A. Characterization and bacterial expression of the Dictyostelium myosin light chain kinase cDNA. Identification of an autoinhibitory domain. J Biol Chem. 1991 Aug 25;266(24):16044–16049. [PubMed] [Google Scholar]
  30. Tan J. L., Spudich J. A. Dictyostelium myosin light chain kinase. Purification and characterization. J Biol Chem. 1990 Aug 15;265(23):13818–13824. [PubMed] [Google Scholar]
  31. Truong T., Medley Q. G., Côté G. P. Actin-activated Mg-ATPase activity of Dictyostelium myosin II. Effects of filament formation and heavy chain phosphorylation. J Biol Chem. 1992 May 15;267(14):9767–9772. [PubMed] [Google Scholar]
  32. Trybus K. M. Filamentous smooth muscle myosin is regulated by phosphorylation. J Cell Biol. 1989 Dec;109(6 Pt 1):2887–2894. doi: 10.1083/jcb.109.6.2887. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Trybus K. M., Waller G. S., Chatman T. A. Coupling of ATPase activity and motility in smooth muscle myosin is mediated by the regulatory light chain. J Cell Biol. 1994 Mar;124(6):963–969. doi: 10.1083/jcb.124.6.963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Uyeda T. Q., Spudich J. A. A functional recombinant myosin II lacking a regulatory light chain-binding site. Science. 1993 Dec 17;262(5141):1867–1870. doi: 10.1126/science.8266074. [DOI] [PubMed] [Google Scholar]
  35. Vaillancourt J. P., Lyons C., Côté G. P. Identification of two phosphorylated threonines in the tail region of Dictyostelium myosin II. J Biol Chem. 1988 Jul 25;263(21):10082–10087. [PubMed] [Google Scholar]
  36. Wessels D., Soll D. R., Knecht D., Loomis W. F., De Lozanne A., Spudich J. Cell motility and chemotaxis in Dictyostelium amebae lacking myosin heavy chain. Dev Biol. 1988 Jul;128(1):164–177. doi: 10.1016/0012-1606(88)90279-5. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES