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Journal articles on the topic 'Binding actif'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

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1

Arias, Paloma, Miguel A. Fernández-Moreno, and Francisco Malpartida. "Characterization of the Pathway-Specific Positive Transcriptional Regulator for Actinorhodin Biosynthesis inStreptomyces coelicolor A3(2) as a DNA-Binding Protein." Journal of Bacteriology 181, no. 22 (1999): 6958–68. http://dx.doi.org/10.1128/jb.181.22.6958-6968.1999.

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ABSTRACT The ActII-ORF4 protein has been characterized as a DNA-binding protein that positively regulates the transcription of the actinorhodin biosynthetic genes. The target regions for the ActII-ORF4 protein were located within the act cluster. These regions, at high copy number, generate a nonproducer strain by in vivo titration of the regulator. The mutant phenotype could be made to revert with extra copies of the wild-type actII-ORF4 gene but not with theactII-ORF4-177 mutant. His-tagged recombinant wild-type ActII-ORF4 and mutant ActII-ORF4-177 proteins were purified fromEscherichia coli

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2

Pollard, Thomas D. "Actin and Actin-Binding Proteins." Cold Spring Harbor Perspectives in Biology 8, no. 8 (2016): a018226. http://dx.doi.org/10.1101/cshperspect.a018226.

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3

Ampe, Christophe, and Joël Vandekerckhove. "Actin-actin binding protein interfaces." Seminars in Cell Biology 5, no. 3 (1994): 175–82. http://dx.doi.org/10.1006/scel.1994.1022.

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4

Kozuka, Jun, Yoshiharu Ishii, and Toshio Yanagida. "2P130 Dynamic cooperative binding of myosin V on actin filament(Molecular motors,Poster Presentations)." Seibutsu Butsuri 47, supplement (2007): S145. http://dx.doi.org/10.2142/biophys.47.s145_3.

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5

Gross, Stephane R. "Actin binding proteins." Cell Adhesion & Migration 7, no. 2 (2013): 199–213. http://dx.doi.org/10.4161/cam.23176.

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6

Winder, S. J. "Actin-binding proteins." Journal of Cell Science 118, no. 4 (2005): 651–54. http://dx.doi.org/10.1242/jcs.01670.

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7

Vandekerckhove, J. "Actin-binding proteins." Current Opinion in Cell Biology 2, no. 1 (1990): 41–50. http://dx.doi.org/10.1016/s0955-0674(05)80029-8.

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8

Hartwig, John H., and David J. Kwiatkowski. "Actin-binding proteins." Current Opinion in Cell Biology 3, no. 1 (1991): 87–97. http://dx.doi.org/10.1016/0955-0674(91)90170-4.

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9

Winder, S. J., L. Hemmings, S. K. Maciver, et al. "Utrophin actin binding domain: analysis of actin binding and cellular targeting." Journal of Cell Science 108, no. 1 (1995): 63–71. http://dx.doi.org/10.1242/jcs.108.1.63.

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Utrophin, or dystrophin-related protein, is an autosomal homologue of dystrophin. The protein is apparently ubiquitously expressed and in muscle tissues the expression is developmentally regulated. Since utrophin has a similar domain structure to dystrophin it has been suggested that it could substitute for dystrophin in dystrophic muscle. Like dystrophin, utrophin has been shown to be associated with a membrane-bound glycoprotein complex. Here we demonstrate that expressed regions of the predicted actin binding domain in the NH2 terminus of utrophin are able to bind to F-actin in vitro, but d

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10

Drubin, David G. "Actin and actin-binding proteins in yeast." Cell Motility and the Cytoskeleton 15, no. 1 (1990): 7–11. http://dx.doi.org/10.1002/cm.970150103.

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11

McGough, Amy. "F-actin-binding proteins." Current Opinion in Structural Biology 8, no. 2 (1998): 166–76. http://dx.doi.org/10.1016/s0959-440x(98)80034-1.

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12

Stossel, T. P., C. Chaponnier, R. M. Ezzell, et al. "Nonmuscle Actin-Binding Proteins." Annual Review of Cell Biology 1, no. 1 (1985): 353–402. http://dx.doi.org/10.1146/annurev.cb.01.110185.002033.

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13

Sun, Hui-Qiao, Katarzyna Kwiatkowska, and Helen L. Yin. "Actin monomer binding proteins." Current Opinion in Cell Biology 7, no. 1 (1995): 102–10. http://dx.doi.org/10.1016/0955-0674(95)80051-4.

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14

Castellani, Loriana, Bruce W. Elliott, Donald A. Winkelmann, Peter Vibert, and Carolyn Cohen. "Myosin binding to actin." Journal of Molecular Biology 196, no. 4 (1987): 955–60. http://dx.doi.org/10.1016/0022-2836(87)90420-7.

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15

Nakagawa, H., A. G. Terasaki, K. Ohashi, and S. Miyamoto. "3P207 Distributions of actin filament binding proteins are unrelated to the retrograde flow in filopodia and lamellipodia." Seibutsu Butsuri 45, supplement (2005): S255. http://dx.doi.org/10.2142/biophys.45.s255_3.

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16

Aakhus, Anne M., J. Michael Wilkinson, and Nils O. Solum. "Glycoprotein Ib- and actin-binding regions in human platelet actin-binding protein." Biochemical Society Transactions 19, no. 4 (1991): 1133–34. http://dx.doi.org/10.1042/bst0191133.

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17

Hosokawa, Naoki, Masahiro Kuragano, Atsuki Yoshino, Keitaro Shibata, Taro Q. P. Uyeda, and Kiyotaka Tokuraku. "Unidirectional cooperative binding of fimbrin actin-binding domain 2 to actin filament." Biochemical and Biophysical Research Communications 552 (May 2021): 59–65. http://dx.doi.org/10.1016/j.bbrc.2021.02.139.

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18

Belmont, L. D., G. M. Patterson, and D. G. Drubin. "New actin mutants allow further characterization of the nucleotide binding cleft and drug binding sites." Journal of Cell Science 112, no. 9 (1999): 1325–36. http://dx.doi.org/10.1242/jcs.112.9.1325.

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We have generated 9 site-specific mutations in Saccharomyces cerevisiae actin. These mutants display a variety of phenotypes when expressed in vivo, including slow actin filament turnover, slow fluid-phase endocytosis, and defects in actin organization. Actin mutation D157E confers resistance to the actin-sequestering drug, latrunculin A. Latrunculin A inhibits nucleotide exchange on wild-type yeast actin but not on D157E actin, suggesting that this residue is part of the latrunculin A binding site. We have refined our earlier map of the phalloidin binding site on actin, demonstrating a requir

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19

MORRIS, Glenn E., Nguyen thi MAN, Nguyen thi Ngoc HUYEN, Alexander PEREBOEV, John KENDRICK-JONES, and Steven J. WINDER. "Disruption of the utrophin–actin interaction by monoclonal antibodies and prediction of an actin-binding surface of utrophin." Biochemical Journal 337, no. 1 (1998): 119–23. http://dx.doi.org/10.1042/bj3370119.

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Monoclonal antibody (mAb) binding sites in the N-terminal actin-binding domain of utrophin have been identified using phage-displayed peptide libraries, and the mAbs have been used to probe functional regions of utrophin involved in actin binding. mAbs were characterized for their ability to interact with the utrophin actin-binding domain and to affect actin binding to utrophin in sedimentation assays. One of these antibodies was able to inhibit utrophin–F-actin binding and was shown to recognize a predicted helical region at residues 13–22 of utrophin, close to a previously predicted actin-bi

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20

Bathe, M., M. Claessens, E. Frey, and A. Bausch. "Actin-binding proteins sensitively mediate actin bundle stiffness." Journal of Biomechanics 39 (January 2006): S240. http://dx.doi.org/10.1016/s0021-9290(06)83904-7.

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21

Carvalho, M. "Actin and actin-binding proteins in proliferative vitreoretinopathy." Vision Research 35, no. 1 (1995): S85. http://dx.doi.org/10.1016/0042-6989(95)98343-8.

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22

McCurdy, David W., David R. Kovar, and Christopher J. Staiger. "Actin and actin-binding proteins in higher plants." Protoplasma 215, no. 1-4 (2001): 89–104. http://dx.doi.org/10.1007/bf01280306.

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23

BALLWEBER, Edda, Ewald HANNAPPEL, Thomas HUFF та Hans Georg MANNHERZ. "Mapping the binding site of thymosin β4 on actin by competition with G-actin binding proteins indicates negative co-operativity between binding sites located on opposite subdomains of actin". Biochemical Journal 327, № 3 (1997): 787–93. http://dx.doi.org/10.1042/bj3270787.

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The β-thymosins are small monomeric (G-)actin-binding proteins of 5 kDa that are supposed to act intracellularly as actin-sequestering factors stabilizing the cytoplasmic monomeric pool of actin. The binding region of thymosin β4 was determined by analysing the binding of thymosin β4 to actin complexed with DNase I, gelsolin or gelsolin segment 1. Binding was analysed by determining the increase in the critical concentration of actin polymerization by native gel electrophoresis or chemical cross-linking. The formation of a ternary complex including thymosin β4 should indicate that the actin-bi

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24

Kristó, Ildikó, Izabella Bajusz, Csaba Bajusz, Péter Borkúti, and Péter Vilmos. "Actin, actin-binding proteins, and actin-related proteins in the nucleus." Histochemistry and Cell Biology 145, no. 4 (2016): 373–88. http://dx.doi.org/10.1007/s00418-015-1400-9.

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25

Litjens, Sandy H. M., Jan Koster, Ingrid Kuikman, Sandra van Wilpe, José M. de Pereda та Arnoud Sonnenberg. "Specificity of Binding of the Plectin Actin-binding Domain to β4 Integrin". Molecular Biology of the Cell 14, № 10 (2003): 4039–50. http://dx.doi.org/10.1091/mbc.e03-05-0268.

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Plectin is a major component of the cytoskeleton and links the intermediate filament system to hemidesmosomes by binding to the integrin β4 subunit. Previously, a binding site for β4 was mapped on the actin-binding domain (ABD) of plectin and binding of β4 and F-actin to plectin was shown to be mutually exclusive. Here we show that only the ABDs of plectin and dystonin bind to β4, whereas those of other actin-binding proteins do not. Mutations of the ABD of plectin-1C show that Q131, R138, and N149 are critical for tight binding of the ABD to β4. These residues form a small cavity, occupied by

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26

Sidhu, Navneet, and John F. Dawson. "A crosslinked and ribosylated actin trimer does not interact productively with myosin." Biochemistry and Cell Biology 97, no. 2 (2019): 140–47. http://dx.doi.org/10.1139/bcb-2018-0082.

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A purified F-actin-derived actin trimer that interacts with end-binding proteins did not activate or bind the side-binding protein myosin under rigor conditions. Remodeling of the actin trimer by the binding of gelsolin did not rescue myosin binding, nor did the use of different means of inhibiting the polymerization of the trimer. Our results demonstrate that ADP-ribosylation on all actin subunits of an F-actin-derived trimer inhibits myosin binding and that the binding of DNase-I to the pointed end subunits of a crosslinked trimer also remodels the myosin binding site. Taken together, this w

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27

Yan, L.-J., N. Niida, T. Honda, N. Yoshinaga, S. Hatsukaiwa, and Y. Okamoto. "Porcine aorta actin binding protein." Seibutsu Butsuri 41, supplement (2001): S205. http://dx.doi.org/10.2142/biophys.41.s205_3.

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28

Cheng, C. Yan, and Dolores D. Mruk. "Actin binding proteins and spermiogenesis." Spermatogenesis 1, no. 2 (2011): 99–104. http://dx.doi.org/10.4161/spmg.1.2.16913.

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29

Raae, Arnt J., Sonia Bañuelos, Jari Ylänne, et al. "Actin binding of a minispectrin." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1646, no. 1-2 (2003): 67–76. http://dx.doi.org/10.1016/s1570-9639(02)00551-4.

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30

Renley, Brian A., Inna N. Rybakova, Kurt J. Amann, and James M. Ervasti. "Dystrophin binding to nonmuscle actin." Cell Motility and the Cytoskeleton 41, no. 3 (1998): 264–70. http://dx.doi.org/10.1002/(sici)1097-0169(1998)41:3<264::aid-cm7>3.0.co;2-z.

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31

Isenberg, G. "Actin binding proteins — lipid interactions." Journal of Muscle Research and Cell Motility 12, no. 2 (1991): 136–44. http://dx.doi.org/10.1007/bf01774032.

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32

Aakhus, Anne M., J. Michael Wilkinson, and Nils Olav Solum. "Binding of Human Platelet Glycoprotein lb and Actin to Fragments of Actin-Binding Protein." Thrombosis and Haemostasis 67, no. 02 (1992): 252–57. http://dx.doi.org/10.1055/s-0038-1648421.

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SummaryActin-binding protein (ABP) is degraded into fragments of 190 and 90 kDa by calpain. A monoclonal antibody (MAb TI10) against the 90 kDa fragment of ABP coprecipitated with the glycoprotein lb (GP lb) peak observed on crossed immunoelectrophoresis of Triton X-100 extracts of platelets prepared without calpain inhibitors. MAb PM6/317 against the 190 kDa fragment was not coprecipitated with the GP lb peak under such conditions. The 90 kDa fragment was adsorbed on protein A agarose from extracts that had been preincubated with antibodies to GP lb. This supports the idea that the GP Ib-ABP

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33

Fontao, Lionel, Dirk Geerts, Ingrid Kuikman, Jan Koster, Duco Kramer, and Arnoud Sonnenberg. "The interaction of plectin with actin: evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin." Journal of Cell Science 114, no. 11 (2001): 2065–76. http://dx.doi.org/10.1242/jcs.114.11.2065.

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Plectin is a major component of the cytoskeleton and is expressed in a wide variety of cell types. It plays an important role in the integrity of the cytoskeleton by cross-linking the three filamentous networks and stabilizing cell-matrix and cell-cell contacts. Sequence analysis showed that plectin contains a highly conserved actin-binding domain, consisting of a pair of calponin-like subdomains. Using yeast two-hybrid assays in combination with in vitro binding experiments, we demonstrate that the actin-binding domain of plectin is fully functional and preferentially binds to polymeric actin

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34

Bryan, J. "Gelsolin has three actin-binding sites." Journal of Cell Biology 106, no. 5 (1988): 1553–62. http://dx.doi.org/10.1083/jcb.106.5.1553.

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Gelsolin, a Ca2+-modulated actin filament-capping and -severing protein, complexes with two actin monomers. Studies designed to localize binding sites on proteolytic fragments identify three distinct actin-binding peptides. 14NT, a 14-kD fragment that contains the NH2 terminal, will depolymerize F-actin. This peptide forms a 1:1 complex with G-actin which blocks the exchange of etheno-ATP from bound actin. The estimated association and dissociation rates for this complex are 0.3 microM-1 s-1 and 1.35 x 10(-6) s-1 which gives a maximum calculated Kd = 4.5 x 10(-12) M. 26NT, the adjacent peptide

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35

Izdebska, Magdalena, Wioletta Zielińska, Marta Hałas-Wiśniewska, and Alina Grzanka. "Involvement of Actin and Actin-Binding Proteins in Carcinogenesis." Cells 9, no. 10 (2020): 2245. http://dx.doi.org/10.3390/cells9102245.

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The actin cytoskeleton plays a crucial role in many cellular processes while its reorganization is important in maintaining cell homeostasis. However, in the case of cancer cells, actin and ABPs (actin-binding proteins) are involved in all stages of carcinogenesis. Literature has reported that ABPs such as SATB1 (special AT-rich binding protein 1), WASP (Wiskott-Aldrich syndrome protein), nesprin, and villin take part in the initial step of carcinogenesis by regulating oncogene expression. Additionally, changes in actin localization promote cell proliferation by inhibiting apoptosis (SATB1). I

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36

Banigan, Edward J., Kun-Chun Lee, and Andrea J. Liu. "Control of actin-based motility through localized actin binding." Physical Biology 10, no. 6 (2013): 066004. http://dx.doi.org/10.1088/1478-3975/10/6/066004.

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37

Ballweber, Edda, Marco Galla, Klaus Aktories, Sharon Yeoh, Alan G. Weeds, and Hans Georg Mannherz. "Interaction of ADP-ribosylated actin with actin binding proteins." FEBS Letters 508, no. 1 (2001): 131–35. http://dx.doi.org/10.1016/s0014-5793(01)03040-x.

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38

Hurst, Verena, Kenji Shimada, and Susan M. Gasser. "Nuclear Actin and Actin-Binding Proteins in DNA Repair." Trends in Cell Biology 29, no. 6 (2019): 462–76. http://dx.doi.org/10.1016/j.tcb.2019.02.010.

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39

Mannherz, H. G. "Crystallization of actin in complex with actin-binding proteins." Journal of Biological Chemistry 267, no. 17 (1992): 11661–64. http://dx.doi.org/10.1016/s0021-9258(19)49743-3.

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40

Claessens, Mireille M. A. E., Mark Bathe, Erwin Frey, and Andreas R. Bausch. "Actin-binding proteins sensitively mediate F-actin bundle stiffness." Nature Materials 5, no. 9 (2006): 748–53. http://dx.doi.org/10.1038/nmat1718.

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41

Carvalho, M., D. Proença, A. Carmo, E. Silva, and R. Proença. "2122 Actin and actin-binding proteins in proliferative vitreoretinopathy." Vision Research 35 (October 1995): S85. http://dx.doi.org/10.1016/0042-6989(95)90134-5.

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42

Liu, G., J. Tang, B. T. Edmonds, J. Murray, S. Levin, and J. Condeelis. "F-actin sequesters elongation factor 1alpha from interaction with aminoacyl-tRNA in a pH-dependent reaction." Journal of Cell Biology 135, no. 4 (1996): 953–63. http://dx.doi.org/10.1083/jcb.135.4.953.

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The machinery of eukaryotic protein synthesis is found in association with the actin cytoskeleton. A major component of this translational apparatus, which is involved in the shuttling of aa-tRNA, is the actin-binding protein elongation factor 1alpha (EF-1alpha). To investigate the consequences for translation of the interaction of EF-1alpha with F-actin, we have studied the effect of F-actin on the ability of EF-1alpha to bind to aa-tRNA. We demonstrate that binding of EF-1alpha:GTP to aa-tRNA is not pH sensitive with a constant binding affinity of approximately 0.2 microM over the physiologi

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43

Hansen, Scott D., Adam V. Kwiatkowski, Chung-Yueh Ouyang та ін. "αE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors". Molecular Biology of the Cell 24, № 23 (2013): 3710–20. http://dx.doi.org/10.1091/mbc.e13-07-0388.

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The actin-binding protein αE-catenin may contribute to transitions between cell migration and cell–cell adhesion that depend on remodeling the actin cytoskeleton, but the underlying mechanisms are unknown. We show that the αE-catenin actin-binding domain (ABD) binds cooperatively to individual actin filaments and that binding is accompanied by a conformational change in the actin protomer that affects filament structure. αE-catenin ABD binding limits barbed-end growth, especially in actin filament bundles. αE-catenin ABD inhibits actin filament branching by the Arp2/3 complex and severing by c

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44

Nakamura, Fumihiko, Teresia M. Osborn, Christopher A. Hartemink, John H. Hartwig, and Thomas P. Stossel. "Structural basis of filamin A functions." Journal of Cell Biology 179, no. 5 (2007): 1011–25. http://dx.doi.org/10.1083/jcb.200707073.

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Filamin A (FLNa) can effect orthogonal branching of F-actin and bind many cellular constituents. FLNa dimeric subunits have N-terminal spectrin family F-actin binding domains (ABDs) and an elongated flexible segment of 24 immunoglobulin (Ig) repeats. We generated a library of FLNa fragments to examine their F-actin binding to define the structural properties of FLNa that enable its various functions. We find that Ig repeats 9–15 contain an F-actin–binding domain necessary for high avidity F-actin binding. Ig repeats 16–24, where most FLNa-binding partners interact, do not bind F-actin, and thu

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45

Chan, Keefe T., David W. Roadcap, Nicholas Holoweckyj, and James E. Bear. "Coronin 1C harbours a second actin-binding site that confers co-operative binding to F-actin." Biochemical Journal 444, no. 1 (2012): 89–96. http://dx.doi.org/10.1042/bj20120209.

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Dynamic rearrangement of actin filament networks is critical for cell motility, phagocytosis and endocytosis. Coronins facilitate these processes, in part, by their ability to bind F-actin (filamentous actin). We previously identified a conserved surface-exposed arginine (Arg30) in the β-propeller of Coronin 1B required for F-actin binding in vitro and in vivo. However, whether this finding translates to other coronins has not been well defined. Using quantitative actin-binding assays, we show that mutating the equivalent residue abolishes F-actin binding in Coronin 1A, but not Coronin 1C. By

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46

Yin, H. L., K. Iida, and P. A. Janmey. "Identification of a polyphosphoinositide-modulated domain in gelsolin which binds to the sides of actin filaments." Journal of Cell Biology 106, no. 3 (1988): 805–12. http://dx.doi.org/10.1083/jcb.106.3.805.

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Gelsolin is a Ca2+- and polyphosphoinositide-modulated actin-binding protein which severs actin filaments, nucleates actin assembly, and caps the "barbed" end of actin filaments. Proteolytic cleavage analysis of human plasma gelsolin has shown that the NH2-terminal half of the molecule severs actin filaments almost as effectively as native gelsolin in a Ca2+-insensitive but polyphosphoinositide-inhibited manner. Further proteolysis of the NH2-terminal half generates two unique fragments (CT14N and CT28N), which have minimal severing activity. Under physiological salt conditions, CT14N binds mo

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47

Turunen, O., T. Wahlström, and A. Vaheri. "Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family." Journal of Cell Biology 126, no. 6 (1994): 1445–53. http://dx.doi.org/10.1083/jcb.126.6.1445.

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Ezrin, previously also known as cytovillin, p81, and 80K, is a cytoplasmic protein enriched in microvilli and other cell surface structures. Ezrin is postulated to have a membrane-cytoskeleton linker role. Recent findings have also revealed that the NH2-terminal domain of ezrin is associated with the plasma membrane and the COOH-terminal domain with the cytoskeleton (Algrain, M., O. Turunen, A. Vaheri, D. Louvard, and M. Arpin. 1993. J. Cell Biol. 120: 129-139). Using bacterially expressed fragments of ezrin we now demonstrate that ezrin has an actin-binding capability. We used glutathione-S-t

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48

Liu, Gang, Wayne M. Grant, Daniel Persky, Vaughan M. Latham, Robert H. Singer та John Condeelis. "Interactions of Elongation Factor 1α with F-Actin and β-Actin mRNA: Implications for Anchoring mRNA in Cell Protrusions". Molecular Biology of the Cell 13, № 2 (2002): 579–92. http://dx.doi.org/10.1091/mbc.01-03-0140.

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The targeting of mRNA and local protein synthesis is important for the generation and maintenance of cell polarity. As part of the translational machinery as well as an actin/microtubule-binding protein, elongation factor 1α (EF1α) is a candidate linker between the protein translation apparatus and the cytoskeleton. We demonstrate in this work that EF1α colocalizes with β-actin mRNA and F-actin in protrusions of chicken embryo fibroblasts and binds directly to F-actin and β-actin mRNA simultaneously in vitro in actin cosedimentation and enzyme-linked immunosorbent assays. To investigate the ro

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49

Tranter, M. P., S. P. Sugrue, and M. A. Schwartz. "Binding of actin to liver cell membranes: the state of membrane-bound actin." Journal of Cell Biology 112, no. 5 (1991): 891–901. http://dx.doi.org/10.1083/jcb.112.5.891.

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Previous work has shown that actin binds specifically and saturably to liver membranes stripped of endogenous actin (Tranter, M. P., S. P. Sugrue, and M. A. Schwartz. 1989. J. Cell Biol. 109:2833-2840). Scatchard plots of equilibrium binding data were linear, indicating that binding is not cooperative, as would be expected for F- or G-actin. To determine the state of membrane-bound actin, we have analyzed the binding of F- and G-actin to liver cell membranes. G-actin in low salt depolymerization buffer and EF-actin, a derivative that polymerizes very poorly in solution, bind to liver cell memb

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50

Schwartz, M. A., and E. J. Luna. "How actin binds and assembles onto plasma membranes from Dictyostelium discoideum." Journal of Cell Biology 107, no. 1 (1988): 201–9. http://dx.doi.org/10.1083/jcb.107.1.201.

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We have shown previously (Schwartz, M. A., and E. J. Luna. 1986. J. Cell Biol. 102: 2067-2075) that actin binds with positive cooperativity to plasma membranes from Dictyostelium discoideum. Actin is polymerized at the membrane surface even at concentrations well below the critical concentration for polymerization in solution. Low salt buffer that blocks actin polymerization in solution also prevents actin binding to membranes. To further explore the relationship between actin polymerization and binding to membranes, we prepared four chemically modified actins that appear to be incapable of po

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