Abstract
The interaction of actin with a synthetic peptide which corresponds to one of the repeated tubulin-binding sites present in tau and MAP-2 (microtubule-associated protein 2) proteins has been analysed. The analysis, which uses affinity chromatography of G-actin on a column containing the synthetic peptide, and the co-sedimentation and co-localization of F-actin and the peptide (as determined by immunoelectron microscopy), indicates that the part of the amino acid sequence of tau involved in the binding of tubulin is also involved in actin binding.
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- Arakawa T., Frieden C. Interaction of microtubule-associated proteins with actin filaments. Studies using the fluorescence-photobleaching recovery technique. J Biol Chem. 1984 Oct 10;259(19):11730–11734. [PubMed] [Google Scholar]
- Asai D. J., Thompson W. C., Wilson L., Dresden C. F., Schulman H., Purich D. L. Microtubule-associated proteins (MAPs): a monoclonal antibody to MAP 1 decorates microtubules in vitro but stains stress fibers and not microtubules in vivo. Proc Natl Acad Sci U S A. 1985 Mar;82(5):1434–1438. doi: 10.1073/pnas.82.5.1434. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bernhardt R., Matus A. Initial phase of dendrite growth: evidence for the involvement of high molecular weight microtubule-associated proteins (HMWP) before the appearance of tubulin. J Cell Biol. 1982 Feb;92(2):589–593. doi: 10.1083/jcb.92.2.589. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bulinski J. C., Gundersen G. G. Preparation of antibodies reactive with specific regions of cytoskeletal proteins. Methods Enzymol. 1986;134:453–460. doi: 10.1016/0076-6879(86)34110-7. [DOI] [PubMed] [Google Scholar]
- Collins J. H., Elzinga M. The primary structure of actin from rabbit skeletal muscle. Completion and analysis of the amino acid sequence. J Biol Chem. 1975 Aug 10;250(15):5915–5920. [PubMed] [Google Scholar]
- Danowski B. A. Fibroblast contractility and actin organization are stimulated by microtubule inhibitors. J Cell Sci. 1989 Jun;93(Pt 2):255–266. doi: 10.1242/jcs.93.2.255. [DOI] [PubMed] [Google Scholar]
- Galloway P. G., Perry G., Kosik K. S., Gambetti P. Hirano bodies contain tau protein. Brain Res. 1987 Feb 17;403(2):337–340. doi: 10.1016/0006-8993(87)90071-0. [DOI] [PubMed] [Google Scholar]
- Goedert M., Spillantini M. G., Potier M. C., Ulrich J., Crowther R. A. Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain. EMBO J. 1989 Feb;8(2):393–399. doi: 10.1002/j.1460-2075.1989.tb03390.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Goldberg D. J., Harris D. A., Lubit B. W., Schwartz J. H. Analysis of the mechanism of fast axonal transport by intracellular injection of potentially inhibitory macromolecules: evidence for a possible role of actin filaments. Proc Natl Acad Sci U S A. 1980 Dec;77(12):7448–7452. doi: 10.1073/pnas.77.12.7448. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Griffith L. M., Pollard T. D. Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins. J Cell Biol. 1978 Sep;78(3):958–965. doi: 10.1083/jcb.78.3.958. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Griffith L. M., Pollard T. D. The interaction of actin filaments with microtubules and microtubule-associated proteins. J Biol Chem. 1982 Aug 10;257(15):9143–9151. [PubMed] [Google Scholar]
- Hashimoto F., Horigome T., Kanbayashi M., Yoshida K., Sugano H. An improved method for separation of low-molecular-weight polypeptides by electrophoresis in sodium dodecyl sulfate-polyacrylamide gel. Anal Biochem. 1983 Feb 15;129(1):192–199. doi: 10.1016/0003-2697(83)90068-4. [DOI] [PubMed] [Google Scholar]
- Herzog W., Weber K. Fractionation of brain microtubule-associated proteins. Isolation of two different proteins which stimulate tubulin polymerization in vitro. Eur J Biochem. 1978 Dec 1;92(1):1–8. doi: 10.1111/j.1432-1033.1978.tb12716.x. [DOI] [PubMed] [Google Scholar]
- Isenberg G., Schubert P., Kreutzberg G. W. Experimental approach to test the role of actin in axonal transport. Brain Res. 1980 Aug 4;194(2):588–593. doi: 10.1016/0006-8993(80)91247-0. [DOI] [PubMed] [Google Scholar]
- Krauhs E., Little M., Kempf T., Hofer-Warbinek R., Ade W., Ponstingl H. Complete amino acid sequence of beta-tubulin from porcine brain. Proc Natl Acad Sci U S A. 1981 Jul;78(7):4156–4160. doi: 10.1073/pnas.78.7.4156. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lee G., Cowan N., Kirschner M. The primary structure and heterogeneity of tau protein from mouse brain. Science. 1988 Jan 15;239(4837):285–288. doi: 10.1126/science.3122323. [DOI] [PubMed] [Google Scholar]
- Lee G., Neve R. L., Kosik K. S. The microtubule binding domain of tau protein. Neuron. 1989 Jun;2(6):1615–1624. doi: 10.1016/0896-6273(89)90050-0. [DOI] [PubMed] [Google Scholar]
- Lewis S. A., Wang D. H., Cowan N. J. Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein. Science. 1988 Nov 11;242(4880):936–939. doi: 10.1126/science.3142041. [DOI] [PubMed] [Google Scholar]
- Montejo de Garcini E., Díez J. C., Avila J. Quantitation and characterization of tau factor in porcine tissues. Biochim Biophys Acta. 1986 May 2;881(3):456–461. doi: 10.1016/0304-4165(86)90039-5. [DOI] [PubMed] [Google Scholar]
- Nishida E., Kuwaki T., Sakai H. Phosphorylation of microtubule-associated proteins (MAPs) and pH of the medium control interaction between MAPs and actin filaments. J Biochem. 1981 Aug;90(2):575–578. doi: 10.1093/oxfordjournals.jbchem.a133510. [DOI] [PubMed] [Google Scholar]
- Peterson C., Kress Y., Vallee R., Goldman J. E. High molecular weight microtubule-associated proteins bind to actin lattices (Hirano bodies). Acta Neuropathol. 1988;77(2):168–174. doi: 10.1007/BF00687427. [DOI] [PubMed] [Google Scholar]
- Pollard T. D., Selden S. C., Maupin P. Interaction of actin filaments with microtubules. J Cell Biol. 1984 Jul;99(1 Pt 2):33s–37s. doi: 10.1083/jcb.99.1.33s. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Satir P. Cytoplasmic matrix: old and new questions. J Cell Biol. 1984 Jul;99(1 Pt 2):235s–238s. doi: 10.1083/jcb.99.1.235s. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sattilaro R. F., Dentler W. L., LeCluyse E. L. Microtubule-associated proteins (MAPs) and the organization of actin filaments in vitro. J Cell Biol. 1981 Aug;90(2):467–473. doi: 10.1083/jcb.90.2.467. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sattilaro R. F. Interaction of microtubule-associated protein 2 with actin filaments. Biochemistry. 1986 Apr 22;25(8):2003–2009. doi: 10.1021/bi00356a025. [DOI] [PubMed] [Google Scholar]
- Selden S. C., Pollard T. D. Phosphorylation of microtubule-associated proteins regulates their interaction with actin filaments. J Biol Chem. 1983 Jun 10;258(11):7064–7071. [PubMed] [Google Scholar]
- Serrano L., Avila J., Maccioni R. B. Controlled proteolysis of tubulin by subtilisin: localization of the site for MAP2 interaction. Biochemistry. 1984 Sep 25;23(20):4675–4681. doi: 10.1021/bi00315a024. [DOI] [PubMed] [Google Scholar]
- Serrano L., Montejo de Garcini E., Hernández M. A., Avila J. Localization of the tubulin binding site for tau protein. Eur J Biochem. 1985 Dec 16;153(3):595–600. doi: 10.1111/j.1432-1033.1985.tb09342.x. [DOI] [PubMed] [Google Scholar]
- Serrano L., de la Torre J., Maccioni R. B., Avila J. Involvement of the carboxyl-terminal domain of tubulin in the regulation of its assembly. Proc Natl Acad Sci U S A. 1984 Oct;81(19):5989–5993. doi: 10.1073/pnas.81.19.5989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shelanski M. L., Gaskin F., Cantor C. R. Microtubule assembly in the absence of added nucleotides. Proc Natl Acad Sci U S A. 1973 Mar;70(3):765–768. doi: 10.1073/pnas.70.3.765. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Spudich J. A., Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem. 1971 Aug 10;246(15):4866–4871. [PubMed] [Google Scholar]
- Tellam R. L., Morton D. J., Clarke F. M. A common theme in the amino acid sequences of actin and many actin-binding proteins? Trends Biochem Sci. 1989 Apr;14(4):130–133. doi: 10.1016/0968-0004(89)90142-4. [DOI] [PubMed] [Google Scholar]
- Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Vandekerckhove J. Structural principles of actin-binding proteins. Curr Opin Cell Biol. 1989 Feb;1(1):15–22. doi: 10.1016/s0955-0674(89)80031-6. [DOI] [PubMed] [Google Scholar]
- Vandekerckhove J., Weber K. Actin amino-acid sequences. Comparison of actins from calf thymus, bovine brain, and SV40-transformed mouse 3T3 cells with rabbit skeletal muscle actin. Eur J Biochem. 1978 Oct 16;90(3):451–462. doi: 10.1111/j.1432-1033.1978.tb12624.x. [DOI] [PubMed] [Google Scholar]
- Wang D., Villasante A., Lewis S. A., Cowan N. J. The mammalian beta-tubulin repertoire: hematopoietic expression of a novel, heterologous beta-tubulin isotype. J Cell Biol. 1986 Nov;103(5):1903–1910. doi: 10.1083/jcb.103.5.1903. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weingarten M. D., Lockwood A. H., Hwo S. Y., Kirschner M. W. A protein factor essential for microtubule assembly. Proc Natl Acad Sci U S A. 1975 May;72(5):1858–1862. doi: 10.1073/pnas.72.5.1858. [DOI] [PMC free article] [PubMed] [Google Scholar]