Calcium regulation of the actin-myosin interaction of Physarum polycephalum

International Review of Cytology

Volumn 191, Issue , 1999, Pages 53-98

  Nakamura, Akio ^a   Kohama, Kazuhiro ^a  

^a GUNMA UNIVERSITY   (Japan)

Author keywords

Actin; Actin myosin interaction; Calcium ion; Cytoplasmic streaming; Inhibitory effect of Ca2+; Myosin; Phosphorylation; Physarum polycephalum

Indexed keywords

ACTIN; CALCIUM BINDING PROTEIN; CALCIUM ION; MYOSIN; MYOSIN LIGHT CHAIN;

ACTIN MYOSIN INTERACTION; CELL MOTION; DEPHOSPHORYLATION; EUKARYOTE; MUSCLE CELL; NONHUMAN; NUCLEOTIDE SEQUENCE; PHYSARUM POLYCEPHALUM; PLANT CELL; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN PHOSPHORYLATION; REVIEW;

ANIMALIA; CHONDROMYCES; EUKARYOTA; PHYSARUM; PHYSARUM POLYCEPHALUM;

EID: 0033004788     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0074-7696(08)60157-6     Document Type: Review

References (138)

1. Achenbach, F., and Wohlfarth-Bottermann, K.-E. (1986a). Reactivation of cell-free models of endoplasmic drops from Physariim polycephaliim after glycerol extraction at low ionic strength. Eur. J. Cell Biol. 40, 135-138.
2. Achenbach, F., and Wohlfarth-Bottermann, K.-E. (1986b). Successive contraction-relaxation cycles experimentally induced in cell-free models of Physariim polycephaliim. Eur. J. Cell Biol. 42, 111-117.
3. Anderson, R. W., Cooke, D. J., and Dee, J. (1976). Apogamie development of plasmodia in the Myxomycete Physariim polycephaliim: A cinematographic analysis. Protoplasma 87, 29.
4. Anderson, T. P. (1964). Regional differences in ion concentration in migrating plasmodia. In "Primitive Motile System in Cell Biology" (R. E. Alien and N. Kamiya, Eds.), pp. 128-176. Academic Press, New York.
5. Chacko, S., Jacob, S. S., and Horiuchi, K. Y. (1994). Myosin I from mammalian smooth muscle is regulated by caldesmon-calmodulin. J. Biol. Chem. 269, 15803-15807.
6. Cheney, R. E., O'Shea, M. K., Heuser, J. E., Coelho, M. V., Wolenski, J. S., and Mooseker, M. S. (1993). Brain myosin-V is a two-headed unconventional myosin with motor activity. Cell 75, 13-23.
7. Churchill, P. C. (1985). Second messengers in renin secretion. Am. J. Physiol. 249, F175-F184.
8. Citi, S., and Kendrick-Jones, J. (1987). Regulation of non-muscle myosin structure and function. BioEssays 7, 155-159.
9. 2+-sensitive myosin II from Acanthamoeba. J. Bio!. Chem. 256, 2586-2595.
10. Collins, K., Sellers, J. R., and Matsudaira, P. (1990). Calmodulin dissociation regulates brush border myosin I (110-KD-calmoduIin) mechanochemical activity in vitro. J. Cell Biol. 110, 1137-1147.
11. Colvin, R. A., Oibo, J. A., and Alien, R. A. (1991). Calcium inhibition of cardiac adenylyl cyclase. Evidence for two distinct sites of inhibition. Cell Calcium 12, 19-27.
12. Ebashi, S., and Endo, M. (1968). Calcium ion and muscle contraction. Progr. Biophys. Mol. Biol. 18, 123-183.
13. Felsenstein, J. (1993). PHYLIP (Phylogenetic Inference Package) Version 3.5c. Distributed by author, Department of Genetics, University of Washington, Seattle.
14. Fromherz, S., and Szent-Gyorgyi, A. G. (1995). Role of essential light chain EF hand domains in calcium binding and regulation of scallop myosin. Proc. Natl. Acad. Sei. USA 92, 7652-7656.
15. 2+-sensitive way. J. Biochem, 106, 311-318.
16. Furuhashi, K., and Hatano, S. (1990). Control of actin filament length by phosphorylation of fragmin-actin complex. J. Cell Biol. 111, 1081-1087.
17. Furuhashi, K., and Hatano, S. (1992). Actin kinase: A protein kinase that phosphorylates actin of fragmin-actin complex. J. Biochem. Ill, 366-370.
18. Furuhashi, K., Hatano, S., Ando, S., Nishizawa, K., and Inagaki, M. (1992). Phosphorylation by actin kinase of pointed end-domain on the actin molecule. J. Biol. Cliem. 267, 9326-9330.
19. Gassner, D., Shraideh, Z., and Wohlfarth-Bottermann, K. E. (1985). A giant titin-like protein in Physarum polycephalum: Evidence for its candidacy as a major component of an elastic cytoskeletal super thin filament lattice. Eur. J. Cell Biol. 37, 44-62.
20. Gettemans, J., De Ville, Y., Vandekerckhove, J., and Waelkens, E. (1992). Physarum actin is phosphorylated as the actin-fragmin complex at residues Thr203 and Thr202 by a specific 80 kDa kinase. EMBO J. 11, 3185-3191.
21. Gettemans, J., De Ville, Y., Vandekerckhove, J., and Waelkens, E. (1993). Purification and partial amino acid sequence of the actin-fragmin kinase from Physarum polycephalum. Eur. J. Biochem. 214, 111-119.
22. Harada, Y., Noguchi, A., Kishino, A., and Yanagida, T. (1987). Sliding movement of single actin filaments on one-headed myosin filaments. Nature 326, 805-808.
23. Hasegawa, T., Takahashi, S., Hayashi, H., and Hatano, S. (1980). Fragmin: A calcium ion sensitive regulatory factor on the formation of actin filaments. Biochemistry 19, 2677-2683.
24. Hasegawa, Y., Kikuta, T., and Okamoto, T. (1996). Isolation and identification of myosin I from porcine aorta media smooth muscle. J. Biochem. 120, 901-907.
25. 2+ on movement of plasmodial fragment obtained by caffeine treatment. Exp. Cell Res. 61, 199-203.
26. Hatano, S. (1973). Contractile proteins from the myxomycete plasmodium. Adv. Biophys. 5, 143-176.
27. Hatano, S., and Owaribe, K. (1977). A simple method for the isolation of actin from myxomycete plasmodia. J. Biochem. 82, 201-205.
28. Hatano, S., and Tazawa, M. (1968). Isolation, purification and characterization of myosin B from myxomycete plasmodium. Biochem. Biophys. Acta 154, 507-519.
29. Hinssen, H. (1981a). An actin-modulating protein from Physarum polycephalum. I. Isolation and purification. Eur. J. Cell Biol. 23, 225-233.
30. 2+-dependence and other properties. Eur. J. Cell Biol. 23, 234-240.
31. Hong, C. E., Chiang, B. N., Ku, J., Wei, Y. H., and Fong, J. C. (1991). Calcium antagonists stimulate sperm motility in executed human semen. Er. J. Clin. Pharmacol. 19, 45-49.
32. Ishigami, M., Yoshiyama, S., and Furuhashi, K. (1996). Calcium waves corresponding to the contraction-relaxation cycle of Physarum polycephalum. Cell. Struct. Fund. 21, 628. [Abstract]
33. Ishikawa, R., Okagaki, T., Higashi-Fujime, S., and Kohama, K. (1991). Stimulation of the interaction between actin and myosin by Physarum caldesmon-like protein and smooth muscle caldesmon. J. Biol. Chem. 166, 21784-21790.
34. 2+-calmodulin of the actin-bundling activity of Physarum 210-kDa protein. /. Muscle Res. Cell Motil. 13, 321-328.
35. Ishikawa, R., Sasaki, Y., Nakamura, A., Takagi, T., and Kohama, K. (1995). Purification of an ATP-dependent actin-binding protein from a lower eukaryote, Physarum polycephalum. Biochem. Biophys. Res. Commun. 212, 347-352.
36. Itano, N., and Hatano, S. (1991). F-actin bundling protein from Physamm polycephalum: Purification and its capacity for co-bundling of actin filaments and microtubules. Cell Motil. Cytoskel. 19, 244-254.
37. Jancso, A., and Szent-Gyorgyi, A. G. (1994). Regulation of scallop myosin by the regulatory light chain depends on a single glycine residue. Proc. Natl. Acad. Sei. USA 91, 8762-8766.
38. Kamiya, N. (1981). Physical and chemical basis of cytoplasmic streaming. Anna. Rev. Plant Physiol. 32, 205-236.
39. Kalo, T., and Tonomura, Y. (1975). Ca2*-sensitivity of actomyosin ATPase purified from Physaruin polycephalum. J. Biochem. 77, 1127-1134.
40. Kawamura, M., and Nagano, K. (1975). Calcium ion-dependent ATP pyrophosphohydrolase in Physaruin polycephalum. Biochim. Biophys. Ada 397, 207-219.
41. Kawamura, S., Hisatomi, O., Kayada, S., Tokunaga, F., and Kuo, C.-H. (1993). Recoverin has S-modulin activity in frog rods. J. Biol. Chem. 268, 14579-14582.
42. Kellermayer, M. S., and Granzier, H. L. (1996). Calcium-dependent inhibition of in vitro thinfilament motility by native titin. FEBS Lett. 380, 281-286.
43. Kendrick-Jones, J., Lehman, W., and Szent-Gyorgyi, A. G. (1970). Regulation in molluscan muscles. J. Mol. Biol. 54, 313-326.
44. Kessler, D., Eisenlohr, L. C, Lathwell, M. J., Huang, J., Taylor, H. C, Godfrey, S. D., and Spady, M. L. (1980). Physaruin myosin light chain binds calcium. Cell Motil. 1, 63-71.
45. + induced cessation. Protoplasma 113, 241-243.
46. Kishimoto, U., and Akahori, H. (1959). Protoplasmic streaming of an internodal cell of Nitella flexilis. J. Gen. Physiol. 42, 1167-1183.
47. Kobayashi, T., Takagi, K., Konishi, K., Hamada, Y., Kawaguchi, M., and Kohama, K. (1988). Amino acid sequence of the calcium-binding light chain of myosin from the lower eukaryote, Physarwn polycephalum. J. Biol. Chem. 263, 305-313.
48. Kohama, K. (1981). Ca-dependent inhibitory factor for the actin-myosin-ATP interaction of Physarwn polycephalum. J. Biochem. 90, 1829-1832.
49. Kohama, K. (1987). Ca-inhibitory myosins: Their structure and function. Adv. Biophys. 23, 149-182.
50. 2+ regulation. Trends Pharmacol. Sei. 11, 433-435.
51. 2+ Regulation" (K. Kohama, Ed.). Japan Sei. Soc. Press/CRC Press, Tokyo, Boca Raton, FL.
52. 2+-regulation of the Physarwn actomyosin system. In "The Molecular Biology of Physarwn polycephalum" (N. F. Dove, J. Dec, S. Hatano, F. B. Haugli, and K.-E. Wohlfarth-Bttormann, Eds.), pp. 175-190. Plenum Press, New York.
53. 2+-regulation of the actin-activated Mg-ATPase activity of myosin from Physaruin polycephalum plasmodia. J. Biochem. 99, 1433-1446.
54. 2+-sensitivity on actinmyosin-ATP interaction of Physarwn polycephalum under physiological conditions. Proc. Jpn. Acad. 60B, 435-439.
55. 2+-control of movement of beads coated with Physarwn myosin along actin-cables in Chara internodal cells. Protoplasma 129, 88-91.
56. Kohama, K., and Takano-Ohmuro, H. (1984). Stage specific myosins from amoeba and plasmodium of slime mold, Physarwn polycephalum. Proc. Jpn. Acad. 60B, 431-434.
57. Kohama, K., Kobayashi, K., and Mitani, S. (1980). Effects of Ca ion and ADP on superprecipitation of myosin B from slime mold, Physarwn polycephalum. Proc. Jpn. Acad. 56B, 591-596.
58. 31P nuclear magnetic resonance studies of intact plasmodia of Physarwn polycephalum. FEBS Lett. 76, 161-165.
59. 2+-sensitivity on actin-myosin-ATP interaction via actin. Proc. Jpn. Acad. 61B, 501-505.
60. Kohama, K., Takano-Ohmuro, H., Tanaka, T., Yamaguchi, Y., and Kohama, T. (1986a). Isolation and characterization of myosin from amoebae ol Physarwn polycephalum. J. Biol. Chem. 261, 8022-8027.
61. Kohama, K., Saida, K., Hirata, M., Kitaura, T., and Ebashi, S. (1986b). Superprecipitation is a model for in vitro contraction superior to ATPase activity. Jpn. J. Pharmacol. 42, 253-260.
62. Kohama, K., Kohama, T., and Kendrick-Jones, J. (1987). Effect of N-ethylmaleimide on Ca inhibition of Physarum myosin. J. Biochem. 102, 17-23.
63. 2+-dependent manner. J. Biochem. 104, 995-998.
64. Kohama, K., Sohda, M., Murayama, K., and Okamoto, Y. (19S8b). Domain structure of Physanun myosin heavy chain. Protoplasma (Suppl. 2), 37-47.
65. 2+-regulation of ATP-dependent interaction between actin and myosin of a lower eukaryote, Physanun polycephahun. J. Biochem. 110, 508-513.
66. 2+-receptive subunit of Physarum myosin. J. Biochem. 110, 566-570.
67. Kohama, K., Lin, Y., Takano-Ohmuro, H., and Ishikawa, R. (1991c). A myosin like protein from smooth muscle. J. Cell Sei. (Suppl. 14), 59-61.
68. Kohama, K., Ishikawa, R., and Okagaki, T. (1992). Calcium inhibition oi Physanun actomyosin system: Myosin-linked and actin-linked natures. In "Calcium Inhibition" (K. Kohama, Ed.), pp. 91-107. Japan Sei. Soc. Press/CRC Press, Tokyo/Boca Raton, FL.
69. Kohama, K., Ye, L.-H., and Nakamura, A. (1993). Calcium-binding proteins that are involved in the calcium inhibition of the actomyosin system of a lower eukaryote, Physanun polycephalum. Biomed. Res. 14:(Suppl. 2), 57-62.
70. Kohama, K., Ishikawa, R., and Ishigami, M. (1998). Large scale culture of Physarum: A simple way of growing plasmodia to purify actomyosin and myosin. In "Cell Biology Hand Book" (J. E. Celis, Ed.), 2nd ed., Vol. 1, pp. 466-471. Academic Press, San Diego.
71. 2+. J. Cell. Biol. 106, 1539-1543.
72. Kretsinger, R. H. (1980). Structure and evolution of calcium-modulated proteins. CRC Crit. Rev. Biochem. 8, 119-174.
73. Kron, S. J., and Spudich, J. A. (1986). Fluorescent actin filaments move on myosin fixed to a glass surface. Proc. Natl. Acad. Sei. USA 83, 6272-6276.
74. Kuczmarski, E. R., and Spudich, J. A. (1980). Regulation of myosin self-assembly: Phosphorylation of Dictyostelium heavy chain inhibits formation of thick filaments. Proc. Natl. Acad. Sei. USA 77, 7292-7296.
75. Kuroda, R., Hatano, S., Hiramoto, Y., and Kuroda, H. (1988). Changes of cytosolic Ca-ion concentration in the contraction and relaxation cycle of Physarum plasmodia. Protoplasma (Suppl. 1), 72-80.
76. Kwon, H., Goodwin, E. B., Nyitray, L., Berliner, E., O'Neall-Hennessey, E., Medandri, F. D., and Szent-Gyorgyi, A. G. (1990). Isolation of the regulatory domain of scallop myosin: Role of the essential light chain in calcium binding. Proc. Natl. Acad. Sei. USA 87, 4771-4775.
77. Laroche, A., Lemieux, G., and Pollotta, D. (1989). The nucleotide sequence of a developmentally regulated cDNA for Physarum polycephahun. Nucleic Acids Res. 17, 10502.
78. Lin, Y., Ishikawa, R., Okagaki, T., Ye, L.-H., and Kohama, K. (1994). Stimulation of the ATP-dependent interaction between actin and myosin by a myosin-binding fragment of smooth muscle caldesmon. Cell Motil. Cytoskel. 29, 250-258.
79. Mabuchi, I., Tsukita, Sh., Tsukita, Sc., and Sawai, T. (1988). Cleavage furrow isolated from newt eggs: Contraction, organization of the actin filaments, and protein components of the furrow. Proc. Natl. Acad. Sei. USA 85, 5966-5970.
80. 2+/calmodulin from aggregating cells of Dictyostelium discoideum. EMBO J. 2, 535-542.
81. 2+/actin-dependent inhibition of its phosphorylation. J. Biol. Cliem. 258, 10144-10150.
82. Maruyama, K., Natori, R., and Nonomura, Y. (1976). New elastic protein from muscle. Nature (London) 262, 58-59.
83. Mittal, C. K., and Jadhav, A. L. (1994). Calcium-dependent inhibition of constitutive nitric oxide synthase. Biochem. Biophys. Res. Commun. 203, 8-15.
84. Mooseker, M. S., and Cheney, R. (1995). Unconventional myosins. Annu. Rev. Cell Dev. Biol. 11, 633-675.
85. Morisawa, M., and Steinhardt, R. A. (1982). Changes in intracellular pH of Physarum plasmodium during the cell cycle and in response to starvation. Exp. Cell Res. 140, 341-351.
86. Nachmias, V. T., and Asch, A. (1974). Actin mediated calcium dependency of actomyosin in a myxomycete. Biochem. Biophys. Res. Commun. 60, 656-664.
87. Nakamura, A., and Kohama, K. (1995). Calcium inhibition of actin-myosin interaction. In "Calcium as Cell Signal (K. Maruyama, Y. Nonomura, and K. Kohama, Eds.), pp. 270-276. Igaku-shoin, Tokyo/New York.
88. 2+-binding protein that inhibits myosin light chain kinase activity in lower eukaryote Physarum polycephalum. Jpn. J. Pharmacol. 64, 112. [Abstract]
89. Nakamura, J., and Bannai, S. (1997). Gultathione alters the mode of calcium-mediated regulation of adenylyl cyclase in membranes from mouse brain. Biochem. Biophys. Acta 1339, 239-246.
90. 2+-inhibitory superprecipitation. J. Biochem. 93, 205-223.
91. 2+ activates actin-filament sliding on scallop myosin but inhibits that on Physarum myosin. J. Biochem. 106, 955-957.
92. 2+-dependent inhibitory factor. Eur. J. Cell Biol. 56, 113-122.
93. Okagaki, T., Ishikawa, R., and Kohama, K. (1991b). Purification of a novel Ca-binding protein that inhibits myosin light chain kinase activity in lower eukaryote Physarum polycephalum. Biochem. Biophys. Res. Commun. 176, 564-570.
94. Ozaki, K., and Maruyama, K. (1980). Connection, an elastic protein of muscle. A connectin-like protein from the plasmodium Physarum polycephalum. J. Biochem. 88, 883-888.
95. Ozaki, K., Sugino, H., Hasegawa, T., Takahashi, S., and Hatano, S. (1983). Isolation and characterization of Physarum profilin. J. Biochem. 93, 295-298.
96. 2+ on cytoplasmic actomyosin contraction. Eur. J. Cell Biol. 40, 139-149.
97. Pollard, T. D., and Weihing, R. R. (1974). Actin and myosin and cell motility. CRC Crit. Rev. Biochem. 2, 1-65.
98. Ridgway, E. B., and Durham, A. C. H. (1976). Oscillations of calcium ion concentrations in Physarum polycephalum. J. Cell Biol. 69, 223-226.
99. Robbins, J., Dilorth, S. M., Laskey, R. A., and Dingwall, C. (1991). Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequence. Cell 64, 615-623.
100. Sasaki, K., and Uchida, M. K. (1980). A calcium reversal phenomenon: Differentiation of excitatory and inhibitory roles of Ca in uterine smooth muscle contraction. Jpn. J. Pharmacol. 30, 394-396.
101. Schallreuter, K. H., and Wood, J. M. (1989). Calcium regulates thioredoxin reductase in human metastatic melanoma. Biochem. Biophys. Ada 997, 242-247.
102. Sekine, T., and Kielly, \V. W. (1964). The enzymatic properties of N-ethylmaleimide modified myosin. Biochhn. Biophys. Ada 81, 336-345.
103. 2+-sensitive sliding of latex beads coated with Physarum or scallop myosin along actin bundles in Characeae cells. Abstracts of the papers presented at the Third International Congress on Cell Biology, Tokyo, p. 504.
104. Shimmen, T., and Yano, Y. (1984). Active sliding movement of latex beads coated with skeletal muscle myosin on Chara actin bundles. Protoplasma 121, 132-137.
105. 2+and PTH release in dispersed bovine parathyroid cells. Endocrinology 113, 424-426.
106. Simokawa, N., and Yamaguchi, M. (1993). Molecular cloning and sequencing of the cDNA coding for a calcium-binding protein regucalcin from rat liver. FEES Lett. 327, 251-255.
107. Sobue, K., and Sellers, J. R. (1991). Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin system. J. Biol. Chem. 266, 12115-12118.
108. Sonobe, S., Hatano, S., and Kuroda, K. (1985). Cytoplasmic movement in a glycerinated model of Amoeba proteus. In "Cell Motility: Mechanism and Regulation" (H. Ishikawa, S. Hatano, and H. Sato, Eds.), pp. 271-282. Univ. of Tokyo Press, Tokyo.
109. Sugino, H., and Hatano, S. (1982). Effect of fragmin on actin polymerization: Evidence for enhancement of nucleation and capping of the barbed end. Cell Motil. Cytoskel. 2, 457-470.
110. 2+. J. Cell Biol. 96, 199-203.
111. Sutoh, K., Iwane, M., Matsuzaki, F., Kikuchi, M., and Ikai, A. (1984). Isolation and characterization of a high molecular weight actin-binding protein from Physarum polycephalum plasmodia. J. Cell Biol. 98, 1611-1618.
112. 2+-ATPase activity of brush border myosin I with three or four calmodulin light chains but inhibits with less than two bound. J. Biol. Chem. 266, 1312-1319.
113. Takagi, S. (1993). Photoregulation of cytoplasmic streaming. Cell Struct. Fund. 18, 498. [Abstract]
114. Takagi, S., and Nagai, R. (1985). Light-controlled cytoplasmic streaming in Vallisneria mesophyll cells. Plant Cell Physiol. 26, 941-951.
115. 2+ concentration and cytoplasmic streaming in Valisneria mesophyll cells. Plant Cell Physiol. 27, 953-959.
116. Taylor, D. L., Condeelis, J. S., Moore, P. L., and Allen, R. D. (1973). The contractile basis of amoeboid movement. I. The chemical control of motility in isolated cytoplasm. J. Cell Biol. 59, 378-394.
117. Tazawa, M., and Kishimoto, U. (1968). Cessation of cytoplasmic streaming of Chara internodes during action potential. Plant Cell Physiol. 9, 361-368.
118. Toda, H., Okagaki, T., and Kohama, K. (1990). Amino acid sequence of calmodulin from lower eukaryote; Physarum polycephalum. In "Advances in Second Messenger and Phosphoprotein Research Vol. 24. The Biology and Medicine of Signal Transduction" (Y. Nishizuka, M. Endo, and T. Tanaka, Eds.). Raven Press, New York. [Abstract]
119. 2+ in permeabilized Nitella cells. Protoplasma 116, 75-77.
120. Ueda, T., Gotz von Olenhusen, K., and Ohlfarth-Bottermann, K.-E. (1978). Reaction of the contractile apparatus in Pliysarum to injected calcium, ATP, ADP, and 5′-AMP. Cytobiologie 18, 76-94.
121. Uyeda, T. Q. P., and Kohama, K. (1987). Myosin switching during amoebo-plasmodial differentiation of slime mold, Pliysarum polycephalum. Exp. Cell Res. 169, 74-84.
122. Uyeda, T. Q. P., Hatano, S., Kohama, K., and Furuya, M. (1988). Purification of myxamoebal fragmin, and switching of myxamoebal fragmin to plasmodial fragmin during differentiation of Pliysarum polycephalum. J. Muscle Res. Cell Motil. 9, 233-240.
123. Vale, R. P., Szent-Gyorgyi, A. G., and Sheetz, M. P. (1984). Movement of scallop myosin on Nitella actin filaments: Regulation by calcium. Proc. Natl. Acad. Sei. USA 81, 6775-6778.
124. Wang, K. (1977). Filamin, a new high-molecular-weight protein found in smooth muscle and nonmuscle cells. Purifications and properties of chicken gizzard filamin. Biochemistry 16, 1857-1865.
125. Williamson, R. E. (1975). Cytoplasmic streaming in Chara: A cell model activated by ATP and inhibited by cytochalasin B. J. Cell Sei. 17, 655-688.
126. 2+ and cytoplasmic streaming in the alga Chara. Nature 296, 647-651.
127. Womack, F. C., and Colowic, S. P. (1973). Rapid measurement of binding of ligands by rate of dialysis. Methods Enzymol. 27, 464-471.
128. Xie, X., Harrison, I., Schlichting, D. H., Sweet, R. M., Kalabokis, V. N., Szent-Gyorgyi, A. G., and Cohen, C. (1994). Structure of the regulatory domain of scallop myosin at 2.8 A resolution. Nature 368, 304-312.
129. Yamamoto, K., and Sekine, T. (1983). Interaction of alkali light chain 1 with actin: Effect of ionicstrength on the cross-linkingofalkali light chain 1 with actin. J. Biochem. 94, 2075-2078.
130. Yamamoto, K., Kikuyama, M., Sutoh-Yamamoto, N., Kamitsubo, E., and Katayama, E. (1995). Myosin from alga Chara: Unique structure revealed by electron microscopy. J. Mol. Biol. 254, 109-112.
131. 2+-activated regulatory protein of macrophages. /. Biol. Chem. 255, 9490-9493.
132. Yokota, E., and Shimmen, T. (1993). Regulation of myosin isolated from pollen tubes of lily by calcium. Cell Funct. 18, 642. [Abstract]
133. Yoshimoto, Y., and Hiramoto, Y. (1985). Cleavage in a saponin model of the sea urchin egg. Cell Struct. Funct. 10, 29-36.
134. Yoshimoto, Y., and Kamiya, N. (1984). ATP and calcium-controlled contraction in a saponin model of Physanun polycephaliun. Cell Struct. Funct. 9, 135-141.
135. 2+ efflux and tension generation in the permeabilized plasmodial strand of Physanun. Cell Motil. 1, 432-443.
136. Yoshimoto, Y., Sakai, T., and Kamiya, N. (1981b). ATP oscillation in Physanun plasmodium. Protoplasma 109, 159-168.
137. Yoshimoto, Y., Iwamatsu, T., and Hiramoto, Y. (1985). Cyclic changes in intracellular free calcium levels associated with cleavage cycles in echinoderm and medaka eggs. Biomed. Res. 6, 387-394.
138. Yukawa, C., Yokota, E., Sonobe, S., Mutoh, T., and Shimmen, T. (1997). Two types of myosin in tobacco cultured cell BY-2. Cell Struct. Funct. 22, 704. [Abstract]