Interaction of cytoskeletal proteins with membrane lipids

International Review of Cytology

Volumn 178, Issue , 1997, Pages 73-125

  Isenberg, G ^a   Niggli, V ^b  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b UNIVERSITY OF BERN   (Switzerland)

Author keywords

Biological interfaces; Cytoskeleton; Lipid modifications; Model membranes; Plasma membrane; Protein lipid interactions; Signal cascades

Indexed keywords

ACTIN; ALPHA ACTININ; ANNEXIN; CALDESMON; CYTOSKELETON PROTEIN; DYNAMIN; DYNEIN ADENOSINE TRIPHOSPHATASE; EZRIN; FILAMIN; LIPOSOME; MARCKS PROTEIN; MEMBRANE ENZYME; MEMBRANE LIPID; MEMBRANE PROTEIN; MICROTUBULE ASSOCIATED PROTEIN 2; MYOSIN; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL; PROFILIN; SPECTRIN; SYNAPSIN; TALIN; TAU PROTEIN; TUBULIN; VINCULIN;

ACTIN FILAMENT; CELL FUNCTION; CELL MEMBRANE; CIRCULAR DICHROISM; CYTOSKELETON; DIFFERENTIAL SCANNING CALORIMETRY; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; HUMAN; HYDROPHOBICITY; INTERMEDIATE FILAMENT; LIPID BILAYER; LIPID MEMBRANE; MICROTUBULE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PHOTOAFFINITY LABELING; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN LIPID INTERACTION; PROTEIN PROCESSING; REVIEW; SIGNAL TRANSDUCTION;

EID: 0030718545     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0074-7696(08)62136-1     Document Type: Article

References (271)

1. Adams, R. J., and Pollard, T. D. (1989). Binding of myosin I to membrane lipids. Nature (London) 340, 565-568.
2. Algrain, M., Turunen, O., Vaheri, A., Louvard, D., and Arpin, M. (1993). Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker. J. Cell Biol. 120, 129-139.
3. Almahbobi, G. (1995). Adhesion of intermediate filaments and lipid droplets in adrenal cells studied by field emission scanning electron microscopy. Cell Tissue Res. 281, 387-390.
4. Almahbobi, G., Williams, L. J., and Hall, P. F. (1992). Attachment of steroidogenic lipid droplets to intermediate filaments in adrenal cells. J. Cell Sei. 101, 383-393.
5. Amatruda, J. F., and Cooper, J. A. (1992). Purification, characterization and immunofluorescence localization of Sacchomyces cerevisae capping protein. J. Cell Biol. 117, 1067-1076.
6. Andreoli, C, Martin, M., Le Borgne, R., Reggio, H., and Mangeat, P. (1994). Ezrin has properties to self-associate at the plasma membrane. J. Cell Sei. 107, 2509-2521.
7. Asch, H. L., Mayhew, E., Lazo, R. O., and Asch, B. B. (1990) Lipids noncovalently associated with keratins and other cytoskeletal proteins of mouse mammary epithelial cells in primary culture. Biocliim. Biopliys. Acta 1034, 303-308.
8. Avila, J., and Nido, J. D. (1995). Control of microtubule polymerization and stability. In "The Cytoskeleton: Structure and Assembly" (J. E. Hesketh and I. F. Pryme, eds.), Vol. 1, pp. 47-86. JAI Press, Greenwich, CT and London.
9. Baines, I. C., Brzeska, H., and Korn, E. D. (1992). Differential localization of Acanthamoeba myosin I isoforms. J. Cell Biol. 119, 1193-1203.
10. Baudier, J., and Cole, R. D. (1987), Phosphorylation of tau proteins to a state like that in Alzheimer's brain is catalyzed by a calcium/calmodulin-dependent kinase and modulated by phospholipids. J. Biol. Cliein. 262, 17577-17583.
11. Bayerl, T. M., Thomas, R. K., Penfold, J., Rennie, A. R., and Sackmann, E. (1990). Specular reflection of neutrons at phospholipid monolayers. Biopliys. J. 57, 1095-1098.
12. Beckerle, M. C, and Yen, R. K. (1990). Talin: Role at sites of eel-substratum adhesion. Cell Motil. Cytoskel. 16, 7-13.
13. Beckerle, M. C, Burridge, K., Demartino, G. N., and Croall, D. E. (1987). Colocalization of calcium-dependent protease II and one of its substrates at sites of cell adhesions. Cell (Cambridge, Mass.) 51, 569-577.
14. Behrisch, A., Dietrich, C, Noegel, A. A., Schleicher, M., and Sackmann, E. (1995). The actin-binding protein hisactophilin binds in vitro to partially charged membranes and mediates actin coupling to membranes. Biochemistry 34, 15182-15190.
15. Beltramo, D. M., Alonso, A. del C., and Barra, H. S. (1992). Tyrosinated, detyrosinated and acetylated tubulin isotypes in rat brain membranes. Their proportions in comparison with those in cytosol. Mol. Cell. Biochem. 112, 173-180.
16. Beltramo, D. M., Nunez, M., Alonso, A. del C, and Barra, H. S. (1994). The relationship of hydrophobic tubulin with membranes in neural tissue. Mol. Cell. Biochem. 141, 57-63.
17. Benfenati, F., Valtorta, F., Rossi, M. C., Onofri, F., and Sihra,T. (1993). Interactions of synapsin I with phospholipids: Possible role in synaptic vesicle clustering and in the maintenance of bilayer structures. J. Cell Biol. 123,1845-1855.
18. Bhattacharyya, B., and Wolff, J. (1975). Membrane-bound tubulin in brain and thyroid tissue. J. Biol. Client. 250, 7639-7646.
19. Bialkowska, K., Zembron, A., and Sikorski, A. F. (1994). Ankyrin inhibits binding of erythrocyte spectrin to phospholipid vesicles. Biocliim. Biopliys. Acta 1191, 21-26.
20. Blanchard, A., Ohanian, V., and Critchley, D. R. (1989). The structure and function of alpha-actinin. J. Muscle Res. Cell Motil. 10, 280-289.
21. Bockholt, S. M., and Burridge, M. (1996). Focal adhesions and integrin-mediated cell signaling. In "The Cytoskeleton" ( J. E. Hesketh and I. F. Pryme eds.), Vol. 2, pp. 167-206. Jai Press, Greenwich, CT.
22. Bogatcheva, N. V., and Gusev, N. B. (1995). Computer-assistant prediction of phospholipid binding sites of caldesmon and calponin. FEBS Lett. 363, 269-272.
23. Bogatcheva, N. V., Huber, P. A. J., Fraser, I. D. C, Marston, S. B., and Gusev, N. B. (1994). Localization of phospholipid-binding sites of caldesmon. FEBS Lett. 342, 176-180.
24. Brandt, R., Leger, J., and Lee, G. (1995). Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain. J. Cell Biol. 131, 1327-1340.
25. Brumm, T., Naumann, C., Sackmann, E., Rennie, A. R., Thomas, R. K., Kanellas, D., Penfold, J., and Bayerl, T. M. (1994). Conformational changes of the lecithin head group in monolayers at the air/water interface. A netron reflection study. Eur. Biopliys. J. 23, 289-296.
26. Brunner, J. (1993). New photolabeling and crosslinking methods. Annii. Rev. Biochem. 62, 483-514.
27. Brzeska, H., Lynch, T. J., and Korn, E. D. (1990). Acanthamoeba myosin I heavy chain kinase is activated by phosphatidylserine-enhancedphosphorylation. J. Biol. Cliem. 265,3591-3594.
28. Brzeska, H., Lynch, T. J., Martin, B., Corigliano-Murphy, A., and Korn, E. D. (1992). Substrate specificity of Acanthamoeba myosin I heavy chain kinase as determined by synthetic peptides. J. Biol. Chem. 265, 16138-16144.
29. Burn, P., and Burger, M. M. (1987). The cytoskeletal protein vinculin contains transformation sensitive covalently bound lipid. Science 235, 476-479.
30. Burn, P., Rotman, A., Meyer, R. K., and Burger, M. M. (1985). Diacylglycerol in large alpha-actinin/actin complexes and in the cytoskeleton of activated platelets. Nature (London) 314, 469-472.
31. Burns, R. G., and Surridge, C. D. (1995). The phosphatidylinositol-binding site of microtubule-associated protein MAP2. Biochem. Soc. Trans. 23, 41-46.
32. Burridge, K., and Connell, L. (1983a). A new protein of adhesion plaques and ruffling membrane membranes. J. Cell Biol. 97, 359-367.
33. Burridge, K., and Connell, L. (1983b). Talin: A cytoskeletal component concentrated in adhesion plaques and other sites of actin-membrane interaction. Cell Motil. 3, 405-417.
34. Caceres, A., Mautino, J., and Kosik, K. S. (1992). Suppression of MAP2 in cultured cerebellar macroneurons inhibits minor neurite formation. Neuron 9, 607-618.
35. Caron, J. M., and Berlin, R. D. (1979). Interaction of microtubule proteins with phospholipid vesicles. J. Cell Biol. 81, 665-671.
36. Caron, J. M., and Berlin, R. D. (1987). Dynamic interactions between microtubules and artificial membranes. Biochemistry 26, 3681-3688.
37. Carpenter, C. L. (1996). Intracellular signals and the cytoskeleton: The interactions of phospho-inositide kinases and small G proteins in adherence, ruffling and motility. Semin. Cell Dev. Biol. 7, 691-697.
38. Casella, J. F., Maack, D. J., and Lin, S. (1986). Purification and initial characterization of a protein from a skeletal muscle that caps the barbed ends of actinfilaments. J. Biol. Chem. 261, 10915-10921.
39. Celia, H., Jontes, J. D., Whittaker, M., and Milligan, R. A. (1996). Two-dimensional crystallization of brush border myosin I. J. Struct. Biol. 117, 236-241.
40. Chia, C. P., Shariff, A., Savage, S. A., and Luna, E. J. (1993). The integral membrane protein ponticulin acts as a monomer in nucleating actin assembly. J. Cell Biol. 120, 909-922.
41. Chou, P. Y., and Fasman, G. D. (1978). Empirical predictions of protein conformation. Annii. Rev. Biochem. 47, 251-276.
42. Condeelis, J. (1992). Are all pseudopods created equal? Cell Motil. Cytoskel. 22, 1-6.
43. Correas, L, Padilla, R., and Avila, J. (1990). The tubulin-binding sequence of brain microtubule-associated proteins, tau and MAP-2, is also involved in actin binding. Biochem. J. 269,61-64.
44. Cortese, J. D., Schwab, B., Ill, Frieden, C, and Elson, E. L. (1989). Actin polymerization induces a shape change in actin containing vesicles. Proc. Natl. Acad. Sei. U.S.A. 86,5773-5777.
45. Czurylo, E. A., Zborowski, J., arid Dabrowska, R. (1993). Interaction of caldesmon with phospholipids. Biochem. J. 291, 403-408.
46. De Camilli, P., Emr, S. D., McPherson, P. S., and Novick, P. (1996). Phosphoinositides as regulators in membrane traffic. Science 271, 1533-1538.
47. DePasquale, J. A., and Izzard, C. S. (1991). Accumulation of talin in nodes at the edge of lamellipodium and separate incorporation into adhesion plaques at focal contacts in fibroblasts. J. Cell Biol. 113, 1351-1359.
48. Detmers, P., Weber, A., Elzinga, M., and Stephens, R. E. (1981). 7-chloro-4-nitrobenzeno-2-oxa-1,3-diazole actin as a probe for actin polymerization. J. Biol. Chem. 256, 99-104.
49. Diakowski, W., and Sikorski, A. F. (1995). Interaction of brain spectrin (Fodrin) with phospholipids. Biochemistry 34, 13252-13258.
50. Dietrich, D., Goldmann, W. H., Sackmann, E., and Isenberg, G. (1993). Interaction of NBD-talin with lipid monolayers. FEBS Lett. 324, 99-104.
51. Ding, A., Sanchez, E., Tancinco, M., and Nathan, C. (1992). Interactions of bacterial lipopolysaccharide with microtubule proteins. J. Immunol. 148, 2853-2858.
52. ++-dependent F-actin fragmenting protein. Biochemistry 31, 4779-4786.
53. Eisenberg, D., Schwarz, E., Komaromy, M., and Wall, R. (1984). Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 170, 125-142.
54. Esmaili-Azad, B., McCarty, J. H., and Feinstein, S. C. (1994). Sense and antisense transfection analysis of tau function: Tau influences net microtubule assembly, neurite outgrowth and neurite stability. J. Cell Sei. 107, 869-879.
55. Evans, T. C., Jr., and Nelsestuen, G. L. (1994). Calcium and membrane-binding properties of monomeric and multimeric Annexin II. Biochemistry 33, 13231-13238.
56. Ferguson, M. A. J., and Williams, A. F. (1988). Cell surface anchoring of proteins via glycosylphosphatidylinositol structures. Anna. Rev. Biochem. 57, 285-320.
57. Ferro, K. L., and Collins, C. A. (1995). Microtubule-independent phospholipid stimulation of cytoplasmic dynein ATPase activity. J. Biol. Chem. 270, 4492-4496.
58. Flanagan, L. A., Cunningham, C. C., Kosik, K. S., and Janmey, P. A. (1996). The microtubule associated protein tau binds to inositol phospholipids. Soc. Neurosci. 22, 1984 (abstr.).
59. Franke, W. W., Hergt, M., and Grund, C. (1987). Rearrangement of the vimentin cytoskeleton during adipose conversion: Formation of an intermediate filament cage around lipid globules. Cell (Cambridge, Mass.) 49, 131-141.
60. Fringeli, U. P., Leutert, P., Thurnhofer, H., Fringeli, M., and Burger, M. M. (1986). Structure-activity relationship in vinculin: An IR/attenuated total reflection spectroscopic and film balance study. Proc. Nail. Acad. Sei. U.S.A. 83, 1315-1319.
61. Fritz, M., Zimmermann, R. M., Bärmann, M., and Gaub, H. E. (1993). Actin binding to lipid-inserted alpha-actinin. Biophys. J. 65,1878-1885.
62. Fukami, K., Furuhashi, K., Inagaki, M., Endo, T., Hatano, S., and Takenawa, T. (1992). Requirement of phosphatidylinositol 4,5-biphosphate for alpha-actinin function. Nature (London) 359, 150-152.
63. Fukami, K., Endo, T., Imamura, M., and Takenawa, T. (1994). Alpha-actinin and vinculin are PIP2-binding proteins involved in signaling by tyrosinekinase.y. Biol. Chem. 269,1518-1522.
64. Fukami, K., Sawada, N., Endo, T., and Takenawa, T. (1996). Identification of a phosphatidyl-inositol 4,5-bisphosphate-binding site in chicken skeletal muscle α-actinin. J. Biol. Chem. 271(5), 2646-2650.
65. Furuhashi, K., Inagaki, M., Hatano, S., Fukami, K., and Takenawa, T. (1992). Inositolphospholipid-induced suppression of F-actin-gelating activity of smooth muscle filamin. Biochem. Biophys. Res. Commun. 184, 1261-1265.
66. Gass, G. V., Lin, J. J.-L., Scaife, R., and Wu, C.-F. (1995). Two isoforms of drosophila dynamin in wild-type and shibire15 neural tissue: Different subcellular localization and association mechanisms. J. Neurogenet. 10, 169-191.
67. Gicquaud, C. (1995). Does actin bind to membrane lipids under conditions compatible with those existing in vivo? Biochem. Biophys. Res. Commun. 208, 1154-1158.
68. Gillard, B. K., Heath, J. P., Thurmon, L. T., and Marcus, D. M. (1991). Association of glycosphingolipids with intermediate filaments of human umbilical vein endothelial cells. Exp. Cell Res. 192, 433-444.
69. Gillard, B. K., Thurmon, L. T., and Marcus, D. M. (1992). Association of glycosphingolipids with intermediate filaments of mesenchymal, epithelial, glial and muscle cells. Cell Motil. Cytoskel. 21, 255-271.
70. Gilmore, A. P., and Burridge, K. (1996). Regulation of vinculin binding to talin and actin by phosphatidylinositol-4-5-biphosphate. Nature (London) 381, 531-535.
71. Glaser, M., Wanaski, S., Buser, C. A., Boguslavsky, V., Rashidzada, W., Morris, A., Rebecchi, M., Scarlata, S. F., Runnels, L. W., Prestwich, G. D., Chen, J., Aderem, A., Ahn, J., and McLaughlin, S. (1996). Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol 4,5-biphosphate in lateral domains. J. Biol. Chem. 271, 26187-26193.
72. Goldmann, W. H., and Isenberg, G. (1991). Kinetic determination of talin-actin binding. Biochem. Biophys. Res. Commun. 178, 718-723.
73. Goldmann, W. H., and Isenberg, G. (1993). Analysis of filamin and alpha-actinin binding to actin by the stopped-flow method. FEBS Lett. 336, 408-410.
74. Goldmann, W. H., Niggli, V., Kaufmann, S., and Isenberg, G. (1992). Probing actin and liposome interaction of talin and talin-vinculin complexes. Biochemistry 31, 7665-7671.
75. Goldmann, W. H., Käs, J., and Isenberg, G. (1993a). Talin decreases the bending elasticity of actin filaments. Biochem. Soc. Trans. 22, 46S.
76. Goldmann, W. H., Käs, J., Sackmann, E., and Isenberg, G. (1993b). Direct visualization of lipid vesicle changes on addition of filamin. Biochem. Soc. Trans. 21, 133S.
77. Goldmann, W. H., Bremer, A., Häner, M., Aebi, U., and Isenberg, G. (1994). Native talin is a dumbbell-shaped homodimer when it interacts with actin. J. Struct. Biol. 112, 3-10.
78. Goldmann, W. H., Senger, R., Kaufmann, S., and Isenberg, G. (1995). Determination of the affinity of talin and vinculin to charged lipid vesicles: A light scatter study. FEBS Lett. 368, 516-518.
79. Goldmann, W. H., Ezzel, R. M., Adamson, E. D., Niggli, V., and Isenberg, G. (1996). Vinculin, talin and focal adhesions. J. Muscle Res. Cell Motil. 17, 1-5.
80. Goldschmidt-Clermont, P. J., Machesky, L. M., Baldassare, J. J., and Pollard, T. D. (1990). The actin binding protein profilin binds to PIP-2 and inhibits its hydrolysis by phospholipase C. Science 247, 1575-1578.
81. Goldschmidt-Clermont, P. J., Kirn, J. W., Machesky, L. M., Rhee, S. G., and Pollard, T. D. (1991). Regulation of phospholipase C-yl by profilin and tyrosine phosphorylation. Science 251, 1231-1233.
82. Goldschmidt-Clermont, P. J., Furman, M. L, Wachsstock, D., Safer, D., Nachmias, V. T., and Pollard, T. D. (1992). The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulator mechanism for actin polymerization in cells. Mol. Biol. Cell 3, 1015-1024.
83. Gutkind, J. S., and Vitale-Cross, L. (1996). The pathway linking small GTP-binding proteins of the Rho family to cytoskeletal components and novel signaling kinase cascades. Semin. Cell Dev. Biol. 7, 683-690.
84. Habazettl, J., Gondol, D., Wiltschek, R., Otlewski, J., Schleicher, M., and Holak, T. A. (1992). Structure of hisactophilin is similar to interleukin-1β and fibroblast growth factor. Nature (London) 359, 855-858.
85. Hanakam, F., Eckershorn, C., Lottspeich, F., Müller-Taubenberger, A., Schäfer, W., and Gerisch, G. (1995). The pH-sensitive actin-binding hisactophilin of Dictyostelium exists in two isoforms which both are myristoylated and distributed between plasma membrane and cytoplasm. J. Biol. Chem. 270, 596-602.
86. Hanakam, F., Albrecht, R., Eckerskorn, C., Matzner, M., and Gerisch, G. (1996a). Myristoylated and non-myristoylated forms of the pH sensor protein hiasactophilin II: Intracellular shuttling to plasma membranes and nucleus monitored in real time by a fusion with green fluorescent protein. EMBO J. 15, 2935-2943.
87. Hanakam, F., Gerisch, G., Lotz, S., Alt, T., and Seelig, A. (1996b). Binding of hisactophilin I and II to lipid membranes is controlled by a pH-dependent myristoyl-histidine switch. Biochemistry 34, 11036-11044.
88. Hargreaves, A. J., and McLean, W. G. (1988). The characterization of phospholipids associated with microtubules, purified tubulin and microtubule associated proteins in vitro. Int. J. Biochem. 20, 1133-1138.
89. Hargreaves, A. J., Wandosell, F., and Avila, J. (1986). Phosphorylation of tubulin enhances its association with membranes. Nature (London) 323, 827-828.
90. Hartwig, J. H., Thelen, M, Rosen, A., Janmey, P. A., Nairn, A. C, and Aderem, A. (1992). MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin. Nature (London) 356, 618-622.
91. Hartwig, J. H.', Bokoch, G. M., Carpenter, C. L., Janmey, P. A., Taylor, L. A., Toker, A., and Stossel, T. P. (1995). Thrombin receptor ligation and activated rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell (Cambridge, Mass.) 82, 643-653.
92. Haus, U., Hartmann, H., Trommler, P., Noegel, A. A., and Schleicher, M. (1991). F-actin capping by cap 32/34 requires heterodimeric conformation and can be inhibited with PIP-2. Biochem. Biophys. Res. Commun. 181, 833-839.
93. Hayden, S. M., Wolenski, J. S., and Mooseker, M. S. (1990). Binding of brush border myosin I to phospholipid vesicles. J. Cell Biol. 111, 443-451.
94. Heise, H., Bayere, T., Isenberg, G., and Sackmann, E. (1991). Human platelet P-235, a talin like actin binding protein binds selectively to mixed lipid bilayers. Biochim. Biophys. Ada 1061, 121-131.
95. Heiss, S. G., and Cooper, J. A. (1991). Regulation of capZ, an actin capping protein of chicken muscle by anionic phospholipids. Biochemistry 30, 8753-8758.
96. Hess, D., Sackmann, E., and Isenberg, G. (1998). In preparation.
97. Heyn, S. P., Tillmann, R. W., Egger, M., and Gaub, H. E. (1991). A miniaturized computer controlled micro-fluorescence film balance for protein-lipid monolayers. J. Biochem. Biophys. Methods 22, 145-158.
98. Hock, R. S., Sanger, J. M., and Sanger, J. W. (1989). Talin dynamics in living microinjected non-muscle cells. Cell Motil. Cytoskel. 14, 271-287.
99. Hofmann, A., Eichinger, L., Andre, E., Rieger, D., and Schleicher, M. (1992). Cap100, a novel phosphatidylinositol 4,5-biphosphate regulated protein that caps actin filaments but does not nucleate actin assembly. Cell Motil. Cytoskel. 23, 133-144.
100. Holtz, D., Tanaka, R. A., Hartwig, J., and McKeon (1989). The CAAX motif of lamin A . functions in conjunction with the nuclear localization signal to target assembly to the nuclear envelope. Cell (Cambridge, Mass.) 59, 969-977.
101. Horkovics-Kovats, S., and Traub, P. (1990). Specific interaction of the intermediate filament protein vimentin and its isolated N-terminus with negatively charged phospholipids as determined by vesicle aggregation, fusion and leakage measurements. Biochemistry 29, 8652-8657.
102. Horkovics-Kovats, S., and Traub, P. (1991). A mathematical model for protein induced lipid vesicle leakage: Interaction of the intermediate filament protein vimentin and its isolated N-terminus with phosphatidylinositol vesicles. J. Theor. Biol. 153, 89-110.
103. Horwitz, A., Duggan, K., Buck, C, Beckerle, M. C., and Burridge, K. (1986). Interaction of plasma membrane fibronectin receptor with talin - a transmembrane linkage. Nature (London) 320, 531-533.
104. Hyvönen, M., Macias, M. L., Nilges, M., Oschkinat, H., Saraste, M., and Wilmanns, M. (1995). Structure of the binding site for inositol phosphates in a PH domain. EMBOJ. 14,4676-4685.
105. Isenberg, G. (1991). Actin binding protein-lipid interactions. J. Muscle Res. Cell Motil. 12, 136-144.
106. Isenberg, G. (1996). New concepts of signal perception and transduction by the actin skeleton at cell boundaries. Semin. Cell Dev. Biol. 7, 707-715.
107. Isenberg, G., and Goldmann, W. H. (1992). Actin-membrane coupling: A role for talin. J. Muscle Res. Cell Motil. 13, 587-589.
108. Isenberg, G., and Goldmann, W. H. (1995). Actin binding proteins-lipid interactions. In "The Cytoskeleton" ( J. E. Hesketh and I. F. Pryme, eds.), Vol. 1, pp. 169-204. Jai Press, Greenwich, CT.
109. Isenberg, G., Small, J. V., and Kreutzberg, G. W. (1978). Correlation between actin polymerization and surface receptor segregation in neuroblastoma cells treated with Concanavalin A. J. Neurocytol 7, 649-661.
110. Isenberg, G., Aebi, U., and Pollard, T. D. (1980a). An actin binding protein from Acanthamoeba regulates actin filament polymerization and interactions. Nature (London) 288, 455-459.
111. Isenberg, G., Schubert, P., and Kreutzberg, G. W. (1980b). Experimental approach to test the role of actin in axonal transport. Brain Res. 194, 588-593.
112. Isenberg, G., Leonard, K., and Jockusch, B. M. (1982). Structural aspects of vinculin-actin interactions. J. Mol. Biol. 158, 231-249.
113. Isenberg, G., Niggli, V., Pieper, U., Kaufmann, S., and Goldmann, W. H. (1996). Probing phosphatidylinositolphosphates and adenosinenucleotides on talin nucleated actin polymerization. FEBS Lett. 397, 316-320.
114. Isenberg, G., Frenzel, A., and Seelig, A. (1997a). In preparation.
115. Isenberg, G., Häner, M., Lustig, A., Goldmann, W. H., and Aebi, U. (1997). Peptide specific antibodies localize the major lipid binding sites of talin to the globular 47 kDa, N-terminal subdomain. J. Struct. Biol., in press.
116. Isenberg, H., Kenna, J. G., Green, N. M., and Gratzer, W. B. (1981). Binding of hydrophobic ligands to spectrin. FEBS Lett. 129, 109-112.
117. Ito, S., Werth, D. K., Kichert, N. D., and Pastan, I. (1983). Vinculin phosphorylation by the src-kinase. J. Biol Cliem. 258, 14626-14631.
118. Izzard, C. S., and Lochner, L. R. (1980). Formation of cell-to substrate contacts during fibroblast motility: An interference reflection study. J. Cell Sei. 42, 81-85.
119. Jähnig, F. (1990). Structure predictions of membrane proteins are not that bad. Trends Biochem. Sei. 15, 93-95.
120. Janmey, P. A. (1994). Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly. Annu. Rev. Physiol. 56, 169-191.
121. Janmey, P. A. (1995). Protein regulation by phosphatidylinositol lipids. Cliem. Biol. 2 (2), 61-65.
122. Janmey, P. A., and Stossel, T. P. (1989). Gelsolin-polyphosphoinositide interaction. J. Biol. Chem. 264, 4825-4831.
123. Janmey, P. A., Lamb, J., Allen, P. G., and Matsudaira, P. T. (1992). Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin. J. Biol. Chem. 267,11818-11823.
124. Jockusch, B. M., and Isenberg, G. (1981). Interaction of alpha-actinin and vinculin with actin: Opposite effects on filament network formation. Proc. Natl. Acad. Sei. U.S.A. 78,3005-3009.
125. Jockusch, B. M., Bubeck, P. Giehl, K., Kroemker, M., Moschner, J., Rothkegel, M., Rüdiger, M., Schlüter, K., Stanka, G., and Winkler, J. (1995). The molecular architecture of focal adhesions. Annu. Rev. Cell Dev. Biol. 11, 379-416.
126. Johnson, R. P., and Craig, S. W. (1995a). F-actin binding site masked by the intramolecular association of vinculin head and tail domains. Nature (London) 373, 261-264.
127. Johnson, R. P., and Craig, S. W. (1995b). The carboxy-terminal tail domain of vinculin contains a cryptic binding site for acidic phospholipids. Biochem. Biopliys. Res. Commun. 210, 159-164.
128. Johnson, R. P., Niggli, V., Durrer, P., and Craig, S. W. (1997). In preparation. Joniau, M., and De Cuyper, M. (1984). Tubulin interacts with phospholipid vesicles measured by free-flow electrophoresis: Role of microtubule-associated proteins and polyamines. Colloids Surf. 10, 233-238.
129. 2+-dependent binding of endonexin (annexin IV) to membranes: analysis of the effects of membrane lipid composition and development of a predictive model for the binding interaction. Biochemistry 33, 8930-8940.
130. Kaufmann, S., Pieckenbrock, T., Goldmann, W. H., Bärmann, M., and Isenberg, G. (1991). Talin binds to actin and promotes filament nudeation. FEES Lett. 284, 187-191.
131. Kaufmann, S., Käs, J., Goldmann, W. H., Sackmann, E., and Isenberg, G. (1992). Talin anchors and nucleates actin filaments at lipid membranes-a direct demonstration. FEBS Lett. 314, 203-205.
132. Kellie, S., and Wigglesworth, N. M. (1987). The cytoskeletal protein vinculin is acylated by myristic acid. FEBS Lett. 213, 428-432.
133. Kilimann, M. W., and Isenberg, G. (1982). Actin filament capping protein from bovine brain. EMBO J. 1, 889-894.
134. Kim, J., Blackshear, P. J., Johnson, J. D., and McLaughlin, S. (1994). Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin. Biophys. J. 67, 227-237.
135. Klausner, R. D., Kumar, N., Weinstein, J. N., Blumenthal, R., and Flavin, M. (1981). Interaction of tubulin with phospholipid vesicles. I. Association with vesicles at the phase transition. J. Biol. Chem. 256, 5879-5885.
136. 3, (GP IIb-IIIa) to talin. J. Biol. Chem. 271, 16416-16421.
137. Kotani, M., Hosoya. H., Kubo, H., Itoh, K., Sakuraba, H., Kusubata, M., Inagaki, M., Yazaki, K-, Suzuki, Y., and Tai, T. (1994). Evidence for direct binding of intracellularly distributed ganlioside GM2 to isolated vimentin intermediate filaments in normal and Tay-Sachs disease human fibroblasts. Cell Struct. Fimct. 19, 81-87.
138. Kuleszka-Lipka, D., Baines, I. C, Brzeska, H., and Korn, E. D. (1991). Immunolocalization of myosin I heavy chain kinase in Acanthamoeba castellanii and binding of purified kinase to isolated plasma membranes. J. Cell Biol. 115, 109-119.
139. Kumar, N., Klausner, R. D., Weinstein, J. N., Blumenthal, R., and Flavin, M. (1981). Interaction of tubulin with phospholipid vesicles. II. Physical changes of the protein. J. Biol. Chem. 256, 5886-5889.
140. Kyte, J., and Doolittle, R. F. (1982). A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132.
141. Lacey, M. L., and Haimo, L. T. (1994). Cytoplasmic dynein binds to phospholipid vesicles. Cell Motil. Cytosket. 28, 205-212.
142. Laliberte, A., and Gicquaud, C. (1988). Polymerization of actin by positively charged liposomes. J. Cell Biol. 106, 1221-1227.
143. Lassing, I., and Lindberg, U. (1985). Specific interaction between phosphatidylinositol 4,5-biphosphate and profilactin. Nature (London) 314, 472-474.
144. Lemmon, M. A., Ferguson, K. M., O'Brien, R., Sigler, P. B., and Schlessinger, J. (1995). Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain. Proc. Nail. Acad. Sei. U.S.A. 92, 10472-10476.
145. Leterrier, J. F., Käs, J., Hartwig, J., Vegners, R., and Janmey, P. A. (1996). Mechanical effects of neurofilament crossbridges: Modulation by phosphorylation. Lipids and interactions with F-actin. J. Biol. Chem. 271, 15687-15694.
146. Lewis, S. A., Wang, D., and Cowan, N. J. (1988). Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein. Science 242, 936-939.
147. Li, D., Miller, M., and Chantier, P. D. (1994). Association of cellular myosin II with anionic phospholipids and the neuronal plasma membrane. Proc. Natl. Acad. Sei. U.S.A. 91,853-857.
148. Lieber, J. G., and Evans, R. M. (1996). Disruption of the vimentin intermediate filament system during adipose conversion of 3T3-L1 cells inhibits lipid droplet accumulation. J. Cell Sei. 109, 3047-3058.
149. Lin, H. C., and Oilman, A. G. (1996). Regulation of dynamin I GTPase activity by G protein βγ subunits and phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 271, 27979-27982.
150. 2+-sensitive phospholipid-binding protein with very high affinity for protein kinase C. J. Biol. Chem. 269, 21043-21050.
151. Low, M. G. (1989). The glycosyl-phosphatidylinositol anchor of membrane proteins. Biochim. Biophys. Acta 988, 427-454.
152. Lu, P. J., Shieh, W.-R., Rhee, S. G., Yin, H. L., and Chen, C.-S. (1996). Lipid products of phosphoinoside 3-kinase bind human profilin with high affinity. Biochemistry 35, 14027-14034.
153. Machesky, L. M., and Pollard, T. D. (1993). Profilin as a potential mediator of membrane-cytoskeleton communication. Trends Cell Biol. 3, 381-385.
154. Machesky, L. M., Goldschmidt-Clermont, P. J., and Pollard, T. D. (1990). The affinities of human platelet and Acanthamoeba profilin isoforms for polyphosphoinositides account for their relative abilities to inhibit phospholipase C. Cell Regul. 1, 937-950.
155. MacIver, S. K. (1995). Microfilament organization and actin-binding proteins. In "The Cy-toskeleton" ( J. E. Hesketh and I. F. Pryme, eds.), Vol. I, pp. 1-45. Jai Press,
156. Greenwich, CT. Maekawa, S., and Sakai, H. (1990). Inhibition of actin regulatory activity of the 74 kDa protein from bovine adrenal medulla (Adseverin) by some phospholipids. J. Biol. Client. 265, 10940-10942.
157. Maksymiw, R., Sen-Fang, S., Gaub, H., and Sackmann, E. (1987). Electrostatic coupling of spectrin dimers to phospholipidserine containing lipid lamellae. Biochemistry 26,2983-2990.
158. Manenti, S., Sorokine, O., Van Dorsselaer, A., and Taniguchi, H. (1992). Affinity purification and characterization of myristoylated alanine-rich protein kinase C (MARCKS) from bovine brain. J. Biol. Cliem. 267, 22310-22315.
159. Manenti, S., Sorokine, O., Van Drosselaer, A., and Tanaguchi, H. (1993). Isolation of the non-myristoylated form of a major substrate of protein kinase C (MARCKS) from bovine brain. J. Biol. Chem. 268, 6878-6881.
160. Mariani, M., Maretzki, D., and Lutz, H. U. (1993). A tightly membrane-associated subpopula-tion of spectrin is 3H-palmitoylated. J. Biol. Chem. 268, 12996-13001.
161. Mason, J. T., Huang, C, and Biltonen, R. L. (1981). Calorimetric investigations of saturated mixed-chain phosphatidylcholine bilayer dispersions. Biochemistry 20, 6086-6092.
162. McLachlan, A. D., Stewart, M., Hynes, R. O., and Rees, J. D. G. (1994). Analysis of repeated motifs in the talin rod. J. Mol. Biol. 135, 1278-1290.
163. McLaughlin, S., and Aderem, A. (1995). The myristoyl-electrostatic switch: A modulator of reversible protein. Membrane interactions. Trends Biochem. 20, 272-276.
164. Meers, P., and Mealy, T. (1993). Calcium-dependent annexin V binding to phospholipids : stoi-chiometry, specificity, and the role of negative charge. Biochemistry 32, 11711-11721.
165. Meers, P., and Mealy, T. (1994). Phospholipid determinants for annexin V binding sites and the role of tryptophan 187. Biochemistry 33, 5829-5837.
166. Menkel, A. R., Kroemker, M., Bubeck, P., Ronsiek, M., Nicolai, G., and Jockusch, B. M. (1994). Characterization of an F-actin-binding domain in the cytoskeletal protein vinculin. J. Cell Biol. 126, 1231-1240.
167. Meyer, R. K. (1989). Vinculin-lipid monolayer interactions: A model for focal contact formation. Eur. J. Cell Biol 50, 491-499.
168. Meyer, R. K., and Aebi, U. (1990). Bundling of actin filaments by alpha-actinin depends on its molecular length. J. Cell Biol. 110, 2013-2024.
169. Meyer, R. K., Schindler, H., and Burger, M. M. (1982). Alpha-actinin interacts specifically with model membranes containing glycerides and fatty acids. Proc. Natl. Acad. Sei. U.S.A. 79, 4280-4284.
170. Michalak, K., Bobrowska, M., and Sikorski, A. F. (1993). Interaction of bovine erythrocyte spectrin with aminophospholipid lipposomes. Gen. Physiol. Biophys. 12, 163-170.
171. Miyata, H., Bowers, B., and Korn, E. D. (1989). Plasma membrane association of Acanthamoeba myosin I. J. Cell Biol. 109, 1519-1528.
172. Mohwald, H. (1990). Phospholipid and phospholipid-protein monolayers at the air/water interface. Anna. Rev. Phys. Chem. 41, 441-476.
173. Mombers, C., DeGier, J., Demel, R. A., and Van Deenen, L. L. M. (1980). Spectrin phospholipid interaction-A monolayer study. Biochini. Biophys. Ada 603, 52-62.
174. Muguruma, M., Matsumura, S., and Fukazawa, T. (1990). Direct interaction between talin and actin. Biocliem. Biophys. Res. Commun. 171, 1217-1223.
175. Murakami, N., Elzinga, M., Singh, S. S., and Chauhan, V. P. S. (1994). Direct binding of myosin II to phospholipid vesicles via tail regions and phosphorylation of the heavy chains by protein kinase C. J. Biol. Chem. 269, 16082-16090.
176. Muresan, V., Godek, C. P., Reese, T. S., and Schnapp, B. J. (1996). Plus-end motors override minus-end motors during transport of squid axon vesicles on microtubules. J. Cell Biol 135, 383-397.
177. Nachmias, V. T., Golla, R., Casella, J. F., and Barron-Casella, E. (1996). CapZ, a calcium insensitive capping protein in resting and activated platelets. FEBS Lett. 378, 258-262.
178. Nakaoka, T., Kojima, N., Ogita, T., and Tsuji, S. (1995). Characterization of the phosphatidyl-serine-binding region of rat MARCKS (myristolated, alanine-rich protein kinase C substrate). J. Biol. Chem. 270, 12147-12151.
179. Naumann, C, Dietrich, C, Lu, J. R., Thomas, R. K., Rennie, A. R., Penfold, J., and Bayerl, T. M. (1994). Structure of mixed monolayers of DPPC and polyethylene glycol monododecyl ether at the air-water interface determined by neutron reflection and film balance techniques. Langmuir 10, 1919-1925.
180. Naumann, C, Dietrich, C., Behrisch, A., Bayerl, T. M., Schleicher, M., Bucknall, D., and Sackmann, E. (1996). Hisactophilin-mediated binding of actin
181. Niggli, V., and Burger, M. M. (1987). Interaction of the cytoskeleton with the plasma membrane. J. Metnbr. Biol. 100, 97-121.
182. Niggli, V., and Gimona, M. (1993). Evidence for a ternary interaction between alpha-actinin, (meta) vinculin and acidic phospholipid bilayers. Enr. J. Biocliem. 213, 1009-1015.
183. Niggli, V., Dimitrov, D. P., Brunner, J., and Burger, M. M. (1986). Interaction of the cytoskeletal component vinculin with bilayer structures analyzed with a photoactivatable phospholipid. J. Biol. Chem. 261, 6912-6918.
184. Niggli, V., Sommer, L., Brunner, J., and Burger, M. M. (1990). Interaction in situ of the cytoskeletal protein vinculin in bilayers studied by introducing a photoactivatable fatty acid into living chicken embryo fibroblasts. Eur. J. Biocliem. 187, 111-117.
185. Niggli, V., Kaufmann, S., Goldmann, W. H., Weber, T., and Isenberg, G. (1994). Identification of functional domains in the cytoskeletal protein talin. Eur. J. Biocliem. 224, 951-957.
186. Niggli, V., Andreoli, C, Roy, C., and Mangeat, P. (1995). Identification of a phosphatidylinositol-4,5-biphosphate-binding domain in the N-terminal region of ezrin. FEBS Lett. 376, 172-176.
187. Okimasu, E., Nobori, K., Kobayashi, S., Suzaki, E.,Terada, S., and Utsumi, K. (1987). Inhibitory effect of cholesterol on interaction between cytoplasmic actin and liposomes, and restorative effect of high osmotic pressure. Cell Struct. Funct. 12, 187-195.
188. Onoda, K., and Yin, H. L. (1993). gCap39 is phosphorylated. J. Biol. Chem. 268,4106-4112.
189. Otey, C. A., Pavalko, F. M., and Burridge, K. (1990). An interaction between alpha-actinin and β1 integrin subunit in vitro. J. Cell Biol. 111, 721-729.
190. Pantaloni, D., and Carlier, M.-F. (1993). How profilin promotes actin filament assembly in the presence of thymosin β4. Cell (Cambridge, Mass.) 75, 1007-1014.
191. 2+-binding domain. Eur. J. Biocliem. 210, 801-809.
192. Paschal, B. M., Mikami, A., Pfister, K. K., and Vallee, R. B. (1992). Homology of the 74-kDa cytoplasmic dynein subunit with a flagellar dynein polypeptide suggests an intracellular targeting function. J. Cell Biol. 118, 1133-1143.
193. Pavalko, F. M., Otey, C. A., Simon, K. O., and Burridge, K. (1991). Alpha-actinin: A direct link between actin and integrins. Biochem. Soc. Trans. 19, 1065-1069.
194. Penfold, J., and Thomas, R. K. (1989). The application of the specular reflection of neutrons to the study of surfaces and interfaces. Sci. Eng. Res. Counc. RAL 57,1-72.
195. Perides, G., Scherbarth, A., Kühn, S., and Traub, P. (1986a). An electron microscopic study of the interaction in vitro of vimentin intermediate filaments with vesicles prepared from Ehrlich ascites tumor cell lipids. Eur. J. Cell Biol 41, 313-325.
196. Perides, G., Scherbarth, A., and Traub, P. (1986b). Influence of phospholipids on the formation and stability of vimentin-type intermediate filaments. Eur. J. Cell Biol. 42, 268-280.
197. Perides, G., Harter, C., and Traub, P. (1987). Electrostatic and hydrophobic interactions of the intermediate filament protein vimentin and its amino terminus with lipid bilayers. J. Biol. Chem. 262, 13742-13749.
198. Plager, D. A., and Nelsestuen, G. L. (1994). Direct enthalpy measurements of the calcium-dependent interaction of annexins V and VI with phospholipid vesicles. Biochemistry 33, 13239-13249.
199. Pollard, T. D., Almo, S., Quirk, S., Vinson, V., and Lattman, E. E. (1994). Structure of actin-binding proteins: Insights about function at atomic resolution. Annu. Rev. Cell Biol. 10, 207-249.
200. Raetz, C. R. H. (1990). Biochemistry of endotoxins. Annu. Rev. Biochem. 59, 129-170.
201. Raghunathan, V., Mowery, P., Rozycki, M., Lindberg, U., and Schutt, C. (1992). Structural changes in profilin accompany its binding to phosphatidylinositol 4,5-bisphosphate. FEBS Lett. 297, 46-50.
202. Rees, D. I. G., Ades, S. E., Singer, S. J., and Hynes, R. O. (1990). Sequence and domain structure of talin. Nature (London) 247, 685-689.
203. Regula, C. S., Sager, P. R., and Berlin, R. D. (1986). Membrane tubulin. Ann. N. Y. Acad. Sei. 466, 832-842.
204. Resh, M. D. (1994). Myristoylation and palmitoylation of Src family members: The fats of the matter. Cell (Cambridge, Mass.) 76, 411-413.
205. Rilling, H. C, Breunger, E., Epstein, W. W., and Grain, P. F. (1990). Prenylated proteins: The structure of the isoprenoid group. Science 247, 318-320.
206. Ruddies, R., Goldmann, W. H., Isenberg, G., and Sackmann, E. (1993). The voscoelasticity of entangled actin networks: The influence of defects and modulation by talin and vinculin. Eur. Biophys. J. 22, 309-322.
207. Sackmann, E. (1995). Biological membranes- architecture and function. Hand. Pliys. Biol. Syst. 1, 4-63.
208. Salim, K., Bottomley, M. J., Querfurth, E., Zvelebil, M. J., Gout, I. Scaife, R., Margolis, R. L., Gigg, R., Smith, C. I. E., Driscoll, P. C, Waterfield, M. D., and Panatayou, G. (1996). Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase. EMBO J. 15, 6241-6250.
209. Sarria, A. J., Panini, S. R., and Evans, R. M. (1992). A functional role for vimentin intermediate filaments in the metabolism of lipoprotein-derived cholesterol in human SW-13 cells. J. Biol. Chem. 267, 19455-19463.
210. Schafer, D. A., Jennings, P. B., and Cooper, J. A. (1996). Dynamics of capping protein and actin assembly in vitro: Uncapping barbed ends by phosphoinositides. J. Cell Biol. 135, 169-179.
211. Scheel, J., Ziegelbauer, K., Kupke, T., Humbel, B. M., Noegel, A. A., Gerisch, G., and Schleicher, M. (1989). Hiasactophilin, a histidine rich actin binding protein from Dictyostelium discoideum. J. Biol. Chem. 264, 24533-24539.
212. Schleicher, M., Gerisch, G., and Isenberg, G. (1984). New actin binding proteins from Dictyostelium discoideum. EMBO J. 3, 2095-2100.
213. Schleicher, M., Noegel, A. A., Schwarz, T., Wallraff, E., Brink, M., Faix, J., Gerisch, G., and Isenberg, G. (1988). A Dictyostelium mutant with severe defects in alpha-actinin: Its characterization using cDNA probes and monoclonal antibodies. J. Cell Sei. 90, 59-71.
214. Schmidt, M. F. G. (1989). Fatty acylation of proteins. Biochim. Biopliys. Acta 988, 411-426.
215. Schwienbacher, C., Jockusch, B. M., and Rüdiger, M. (1996). Intramolecular interactions regulate serine/threonine phosphorylation of vinculin. FEBS Lett. 384, 71-74.
216. Shariff, A., and Luna, E. J. (1992). Diacylglycerol-stimulated formation of actin nucleation sites at plasma membranes. Science 256, 245-247.
217. Shoeman, R. L., and Traub, P. (1995). The proteins of intermediate filament systems. In "The Cytoskeleton: Structure and Assembly" (J. E. Hesketh and I. F. Pryme, eds.), Vol. 1, pp. 205-256. JAI Press, Greenwich, CT and London.
218. Shpetner, H. S., Herskovits, J. S., and Vallee, R. B. (1996). A binding site for SH3 domains targets dynamin to coated pits. J. Biol. Chem. 271, 13-16.
219. Sikorski, A. F., and Kuczek, M. (1985). Labeling of erythrocyte spectrin in situ with phenylisothiocyanate. Biochim. Biophys. Acta 820, 147-153.
220. Small, J. V., Isenberg, G., and Celis, J. E. (1978). Polarity of actin at the leading edge of cultured cells. Nature 272, 638-639.
221. Smith, D. P., Kilbourn, M. R., McDowell, J. H., and Hargrave, P. (1981). Topography of rhodopsin in retinal rod outer segment disk membranes. Photochemical labeling with 1-azidopyrene. Biochemistry 20, 2417-2424.
222. Sohn, R. H., Chen, J., Koblan, K. S., Bray, P. F., and Goldschmidt-Clermont, P. J. (1995). Localization of a binding site for phosphatidylinositol 4,5-bisphosphate on human profilin. J. Biol. Chem. 270, 2114-21120.
223. Staufenbiel, M. (1987). Ankyrin-bound fatty acid turns over rapidly at the erythrocyte plasma membrane. Mol. Cell. Biol. 7, 2981-2984.
224. Stephens, R. E. (1981). Chemical differences distinguish ciliary membrane and axonemal tubulins. Biochemistry 20, 4716-4723.
225. Stephens, R. E. (1985). Evidence for a tubulin-containing lipid-protein structural complex in ciliary membranes. J. Cell Biol. 100, 1082-1089.
226. Stephens, R. E. (1986). Membrane tubulin. Biol Cell. 57, 95-110.
227. Stephens, R. E., Oleszko-Szuts, S., and Good, M. J. (1987). Evidence that tubulin forms an integral membrane skeleton in molluscan gill cilia. J. Cell Sei. 88, 527-535.
228. Stochaj, U., Flocke, K., Mathes, W., and Mannherz, H. G. (1989). 5'-nucleotidase of chicken gizzard and human pancreatic adenocarcinoma cells are anchored to the plasma membrane via a phosphatidylinositol-glycan. Biochem. J. 262, 33-40.
229. St. Onge, D., and Gicquaud, C. (1989). Evidence of direct interaction between actin and membrane lipids. Biochem. Cell Biol. 67, 297-300.
230. Stossel, T. P. (1989). From signal to pseudopod. J. Biol. Chem. 264, 18261-18264.
231. Surridge, C. D., and Burns, R. G. (1992). Phosphatidylinositol inhibits microtubule assembly by binding to microtubule-associated protein 2 at a single, specific, high-affinity site. Biochemistry 31, 6140-6144.
232. Surridge, C. D., and Burns, R. G. (1994). The difference in the binding of phosphatidylinositol distinguishes MAP2 from MAP2C and tau. Biochemistry 33, 8051-8057.
233. ++-simulated binding of myosin I to phosphatidylserine concerted with calmodulin dissociation. J. Biol. Chem. 267, 3445-3454.
234. Swierczynski, S. L., and Blackshear, P. J. (1996). Myristoylation-dependent and electrostatic interactions exert independent effects on the membrane association of the myristoylated alanine-rich protein kinase C substrate protein in intact cells. J. Biol. Chem. 271, 23424-23430.
235. Takeshita, K., and MacDonald, R. I., and MacDonald, R. C. (1993). Band 4.1 enhances spectrin binding to phosphatidylserine vesicles. Biochem. Biophys. Res. Commun. 191, 165-171.
236. Taniguchi, H., and Manenti, S. (1993). Interaction of myristoylated alanine-rich protein kinase C substrate (MARCKS) with membrane phospholipids. J. Biol. Chem. 268, 9960-9963.
237. Tempel, M., Goldmann, W. H., and Isenberg, G. (1994a). Computer analyses suggest interactions of non-muscle filamin with lipid membranes. FEES Lett. 350, 169-172.
238. Tempel, M., Goldmann, W. H., Dietrich, C, Niggli, V., Weber, T., Sackmann, E., and Isenberg, G. (1994b). Insertion of filamin into lipid membranes examined by calorimetry, the film balance technique and lipid photolabeling. Biochemistry 33, 12565-12572.
239. Tempel, M., Goldmann, W. H., Isenberg, G., and Sackmann, E. (1995). Interaction of the 47-kDa talin fragment and the 32-kDa vinculin fragment with acidic phospholipids: A computer analysis. Biophys. J. 69, 228-241.
240. Tempel, M., Isenberg, G., and Sackmann, E. (1996). Temperature-induced sol-gel transition and microgel formation in alpha-actinin crosslinked actin networks: A Theological study. Phys. Rev. 54, 1802-1810.
241. Traub, P., Perides, G., Scherbarth, A., and Traub, U. (1985). Tenacious binding of lipids to vimentin during its isolation and purification from Ehrlich ascites tumor cells. FEBS Lett. 193, 217-221.
242. Traub, P., Perides, G., Schimmel, H., and Scherbath, A. (1986). Interaction in vitro of nonepithelial intermediate filament proteins with total cellular lipids, individual phospholipids, and a phospholipid mixture. J. Biol. Cliem. 261, 10558-10568.
243. Traub, P., Perides, G., Kuhn, S., and Scherbarth, A. (1987). Efficient interaction of nonpolar lipids with intermediate filaments of the vimentin type. Eur. J. Cell Biol. 43, 55-64.
244. Travé, G., Quignard, J.-F., Lionne, C, Widada, J. S., and Liautard, J. -P. (1994). Interdependence of phospholipid specificity and calcium binding in annexin I as shown by site-directed mutagenesis. Biochim. Biophys Acta 1205, 215-222.
245. Tuma, P. L., and Collins, C. A. (1995). Dynamin forms polymeric complexes in the presence of lipid vesicles. J. Biol. Chcm. 270, 26707-26714.
246. Tuma, P. L., Stachniak, M. C., and Collins, C. A. (1993). Activation of dynamin GTPase by acidic phospholipids and endogenous rat brain vesicles. J. Biol. Cliem. 268, 17240-17246.
247. Vallee, R. B. (1993). Molecular analysis of the microtubule motor dynein. Proc. Natl. Acad. Sei. U.S.A. 90, 8769-8772.
248. Vallee, R. B., and Sheetz, M. P. (1996). Targeting of motor proteins. Science 271,1539-1544.
249. Vallee, R. B., and Shpetner, H. S. (1993). Dynamin in synaptic dynamics. Nature (London) 365, 107-108.
250. Vandekerckhove, J. (1990). Actin-binding proteins. Curr. Opin. Cell Biol. 2, 41-50.
251. Vergères, G., Manenti, S., Weber, T., and Sttirzinger, C. (1995). The myristoyl moiety of myristoylated Alanin-rich C kinase substrate (MARCKS) and MARCKS-related protein is embedded in the membrane. J. Biol. Cliem. 270, 19879-19887.
252. Vorotnikov, A. V., and Gusev, N. B. (1990). Interaction of smooth muscle caldesmon with phospholipids. FEBS Lett. 277, 134-136.
253. Vorotnikov, A. V., Bogatcheva, N. V., and Gusev, N. B. (1992). Caldesmon-phospholipid interaction. Biochem. J. 284, 911-916.
254. Wallraff, E., Schleicher, M., Modersitzki, M., Rieger, D., Isenberg, G., and Gerisch, G. (1986). Selection of Dictyostelium mutants defective in cytoskeletal proteins: Use of an antibody that binds to the ends of alpha-actinin rods. EM BO J. 5, 61-65.
255. Wang, D.-S., and Shaw, G. (1995). The association of the C-terminal region of βIIIspectrin to brain membranes is mediated by a PH domain, does not require membrane proteins and coincides with a inositol-1,4,5-triphosphate binding site. Biochem. Biophys. Res. commun. 217, 608-615.
256. Wang, D.-S., Miller, R., Shaw, R., and Shaw, G. (1996). The pleckstrin homology domain of human βIII spectrin is targeted to the plasma membrane in vivo. Biochem. Biophys. Res. Commun. 225, 420-426.
257. Wang, W., and Creutz, C. E. (1994). Role of the amino-terminal domain in regulating interactions of annexin I with membranes: Effects of amino-terminal truncation and mutagenesis of the phosphorylation sites. Biochemistry 33, 275-282.
258. Weeds, A. G., and MacIver, S. K. (1993). F-actin capping proteins. Curr. Opin. Cell Biol. 5, 63-69.
259. Weekes, J., Barry, S. T., and Critchley, D. R. (1996). Acidic phospholipids inhibit the intramolecular association between the N- and C-terminal regions of vinculin, exposing actin-binding and protein kinase C phosphorylation sites. Biochem. J. 314, 827-832.
260. Wuesthube, L. J., and Luna, E. J. (1989). F-actin binds to the cytoplasmic surface of ponticulin, a 17 kDa integral glycoprotein from Dictyostelium discoideutn plasma membranes. J. Cell Biol. 105,1741-1751.
261. Yamauchi, P. S., and Purich, D. L. (1987). Modulation of microtubule assembly and stability by phosphatidylinositol action on microtubule-associated protein-2. J. Biol. Cliem. 262, 3369-3375.
262. Yamauchi, P. S., and Purich, D. (1993). Microtubule-associated protein interactions with actin flaments: Evidence for differential behaviour of neuronal MAP-2 and Tau in the presence of phosphatidyl-inositol. Biochem. Biophys. Res. Commun. 190, 710-715.
263. Yin, H. L., lida, K., and Janmey, P. A. (1988). Identification of a polyphosphoinositide-modulated domain in gelsolin which binds to the sides of actin filaments. J. Cell Biol. 106, 805-812.
264. Yonezawa, N., Nishida, E., lida, K., Yahara, I., and Sakai, H. (1990). Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides. J. Biol. Chem. 265, 8382-8386.
265. Yonezawa, N., Homma, Y., Yahara, I., Sakai, H., and Nishida, E. (1991). A short sequence repsonsible for both phosphoinositide binding and actin binding activities of cofilin. J. Biol. Chem. 266, 17218-17221.
266. Yu, F. X., Johnston, P. A., Südhof, T. C, and Yin, H. (1990). gCap39, a calcium ion and poyphosphoinositide-regulated actin capping protein. Science 250, 1413-1415.
267. Yu, F. X., Sun, H.-Q., Janmey, P. A., and Yin, H. L. (1992). Identification of a polyphosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin. J. Biol. Chem. 267, 14616-14621.
268. Zhang, Z., Tanaka, Y., Nonaka, S., Aizawa, H., Kawasaki, H., Nakata, T., and Hirokawa, N. (1993). The primary structure of rat brain (cytoplasmic) dynein heavy chain, a cytoplasmic motor enzyme. Proc. Natl. Acad. Sei. U.S.A. 90, 7928-7932.
269. Zheng, J., Cahill, S. M., Lemmon, M. A., Fushman, D., Schlessinger, J., and Cowburn, D. (1996). Identification of the binding site for acidic phospholipids on the PH domain of dynamin: Implications for stimulation of GTPase activity. J. Mol. Biol. 255, 14-21.
270. Zot, H. G. (1995). Phospholipid-membrane-associated brush border myosin-I activity. Cell Motil. Cytoskel. 30, 26-37.
271. Zot, H. G., Doberstein, S. K., and Pollard, T. D. (1992). Myosin-I moves actin filaments on a phospholipid substrate: Implications for membrane targeting. J. Cell Biol. 116, 367-376.