Abstract
N-1-Naphthylphthalamic acid (NPA) binding activity is released into the supernatant when plasma membranes are subjected to high-salt treatment, indicating that this activity is peripherally associated with the membrane. Extraction of plasma membrane vesicles with Triton X-100 resulted in retention of NPA binding activity in the detergent-insoluble cytoskeletal pellet. Treatment of this pellet with KI released NPA binding activity, actin, and alpha-tubulin. Dialysis to remove KI led to the repolymerization of cytoskeletal elements and movement of NPA binding activity into an insoluble cytoskeletal pellet. NPA binding activity partitioned into the detergent-insoluble cytoskeletal pellet obtained from both zucchini and maize membranes and was released from these pellets by KI treatment. Treatment of a cytoskeletal pellet with cytochalasin B doubled NPA binding activity in the resulting supernatant. Together, these experiments indicate that NPA binding activity is peripherally associated with the plasma membrane and interacts with the cytoskeleton in vitro.
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- Bloch R. J. Actin at receptor-rich domains of isolated acetylcholine receptor clusters. J Cell Biol. 1986 Apr;102(4):1447–1458. doi: 10.1083/jcb.102.4.1447. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bonder E. M., Mooseker M. S. Cytochalasin B slows but does not prevent monomer addition at the barbed end of the actin filament. J Cell Biol. 1986 Jan;102(1):282–288. doi: 10.1083/jcb.102.1.282. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brown S. S., Spudich J. A. Cytochalasin inhibits the rate of elongation of actin filament fragments. J Cell Biol. 1979 Dec;83(3):657–662. doi: 10.1083/jcb.83.3.657. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brunn S. A., Muday G. K., Haworth P. Auxin transport and the interaction of phytotropins: probing the properties of a phytotropin binding protein. Plant Physiol. 1992 Jan;98(1):101–107. doi: 10.1104/pp.98.1.101. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bruns R. F., Lawson-Wendling K., Pugsley T. A. A rapid filtration assay for soluble receptors using polyethylenimine-treated filters. Anal Biochem. 1983 Jul 1;132(1):74–81. doi: 10.1016/0003-2697(83)90427-x. [DOI] [PubMed] [Google Scholar]
- Burnette W. N. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate--polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem. 1981 Apr;112(2):195–203. doi: 10.1016/0003-2697(81)90281-5. [DOI] [PubMed] [Google Scholar]
- Cooper J. A. Effects of cytochalasin and phalloidin on actin. J Cell Biol. 1987 Oct;105(4):1473–1478. doi: 10.1083/jcb.105.4.1473. [DOI] [PMC free article] [PubMed] [Google Scholar]
- FitzGibbon T., Reese B. E. Position of growth cones within the retinal nerve fibre layer of fetal ferrets. J Comp Neurol. 1992 Sep 8;323(2):153–166. doi: 10.1002/cne.903230203. [DOI] [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]
- Jacobs M., Gilbert S. F. Basal localization of the presumptive auxin transport carrier in pea stem cells. Science. 1983 Jun 17;220(4603):1297–1300. doi: 10.1126/science.220.4603.1297. [DOI] [PubMed] [Google Scholar]
- Jacobs M., Rubery P. H. Naturally occurring auxin transport regulators. Science. 1988 Jul 15;241(4863):346–349. doi: 10.1126/science.241.4863.346. [DOI] [PubMed] [Google Scholar]
- Lacy B. E., Underhill C. B. The hyaluronate receptor is associated with actin filaments. J Cell Biol. 1987 Sep;105(3):1395–1404. doi: 10.1083/jcb.105.3.1395. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Mescher M. F., Jose M. J., Balk S. P. Actin-containing matrix associated with the plasma membrane of murine tumour and lymphoid cells. Nature. 1981 Jan 15;289(5794):139–144. doi: 10.1038/289139a0. [DOI] [PubMed] [Google Scholar]
- Muday G. K., Brunn S. A., Haworth P., Subramanian M. Evidence for a Single Naphthylphthalamic Acid Binding Site on the Zucchini Plasma Membrane. Plant Physiol. 1993 Oct;103(2):449–456. doi: 10.1104/pp.103.2.449. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Munson P. J., Rodbard D. Ligand: a versatile computerized approach for characterization of ligand-binding systems. Anal Biochem. 1980 Sep 1;107(1):220–239. doi: 10.1016/0003-2697(80)90515-1. [DOI] [PubMed] [Google Scholar]
- Nick P., Bergfeld R., Schafer E., Schopfer P. Unilateral reorientation of microtubules at the outer epidermal wall during photo- and gravitropic curvature of maize coleoptiles and sunflower hypocotyls. Planta. 1990 May;181(2):162–168. doi: 10.1007/BF02411533. [DOI] [PubMed] [Google Scholar]
- Ozols J. Amino acid analysis. Methods Enzymol. 1990;182:587–601. doi: 10.1016/0076-6879(90)82046-5. [DOI] [PubMed] [Google Scholar]
- Pollard T. D. Actin. Curr Opin Cell Biol. 1990 Feb;2(1):33–40. doi: 10.1016/s0955-0674(05)80028-6. [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]
- Rubery P. H. Phytotropins: receptors and endogenous ligands. Symp Soc Exp Biol. 1990;44:119–146. [PubMed] [Google Scholar]
- Schmit A. C., Lambert A. M. Plant actin filament and microtubule interactions during anaphase--telophase transition: effects of antagonist drugs. Biol Cell. 1988;64(3):309–319. doi: 10.1016/0248-4900(88)90005-6. [DOI] [PubMed] [Google Scholar]
- Smith P. K., Krohn R. I., Hermanson G. T., Mallia A. K., Gartner F. H., Provenzano M. D., Fujimoto E. K., Goeke N. M., Olson B. J., Klenk D. C. Measurement of protein using bicinchoninic acid. Anal Biochem. 1985 Oct;150(1):76–85. doi: 10.1016/0003-2697(85)90442-7. [DOI] [PubMed] [Google Scholar]
- Sussman M. R., Gardner G. Solubilization of the receptor for N-1-naphthylphthalamic Acid. Plant Physiol. 1980 Dec;66(6):1074–1078. doi: 10.1104/pp.66.6.1074. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tan Z., Boss W. F. Association of Phosphatidylinositol Kinase, Phosphatidylinositol Monophosphate Kinase, and Diacylglycerol Kinase with the Cytoskeleton and F-Actin Fractions of Carrot (Daucus carota L.) Cells Grown in Suspension Culture : Response to Cell Wall-Degrading Enzymes. Plant Physiol. 1992 Dec;100(4):2116–2120. doi: 10.1104/pp.100.4.2116. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Vaughan M. A., Vaughn K. C. Effects of microfilament disrupters on microfilament distribution and morphology in maize root cells. Histochemistry. 1987;87(2):129–137. doi: 10.1007/BF00533397. [DOI] [PubMed] [Google Scholar]
- Ward J. M., Reinders A., Hsu H. T., Sze H. Dissociation and Reassembly of the Vacuolar H-ATPase Complex from Oat Roots. Plant Physiol. 1992 May;99(1):161–169. doi: 10.1104/pp.99.1.161. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weber K., Rathke P. C., Osborn M., Franke W. W. Distribution of actin and tubulin in cells and in glycerinated cell models after treatment with cytochalasin B (CB). Exp Cell Res. 1976 Oct 15;102(2):285–297. doi: 10.1016/0014-4827(76)90044-6. [DOI] [PubMed] [Google Scholar]
- Xu P., Lloyd C. W., Staiger C. J., Drobak B. K. Association of Phosphatidylinositol 4-Kinase with the Plant Cytoskeleton. Plant Cell. 1992 Aug;4(8):941–951. doi: 10.1105/tpc.4.8.941. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yoshihara C. M., Hall Z. W. Increased expression of the 43-kD protein disrupts acetylcholine receptor clustering in myotubes. J Cell Biol. 1993 Jul;122(1):169–179. doi: 10.1083/jcb.122.1.169. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zettl R., Feldwisch J., Boland W., Schell J., Palme K. 5'-Azido-[3,6-3H2]-1-napthylphthalamic acid, a photoactivatable probe for naphthylphthalamic acid receptor proteins from higher plants: identification of a 23-kDa protein from maize coleoptile plasma membranes. Proc Natl Acad Sci U S A. 1992 Jan 15;89(2):480–484. doi: 10.1073/pnas.89.2.480. [DOI] [PMC free article] [PubMed] [Google Scholar]