Abstract
The association of actin filaments with membranes is an important feature in the motility of nonmuscle cells. We investigated the role of membrane particles in the attachment of actin filaments to membranes in those systems in which the attachment site can be identified. Freeze fractures through the end-on attachment site of the acrosomal filament bundles in Mytilus (mussel) and Limulus (horseshoe crab) sperm and the attachment site of the microvillar filament bundles in the brush border of intestinal epithelial cells were examined. There are no particles on the P face of the membrane at these sites in the sperm systems and generally none at these sites in microvilli. In microvilli, the actin filaments are also attached along their lengths to the membrane by bridges. When the isolated brush border is incubated in high concentrations of Mg++ (15 mM), the actin filaments form paracrystals and, as a result, the bridges are in register (330 A period). Under these conditions, alignment of the particles on the P face of the membrane into circumferential bands also occurs. However, these bands are generally separated by 800-900 A, indicating that all the bridges cannot be directly attached to membrane particles. Thus membrane particles are not directly involved in the attachment of actin filaments to membranes.
Full Text
The Full Text of this article is available as a PDF (5.0 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Allison A. C., Davies P., De Petris S. Role of contractile microfilaments in macrophage movement and endocytosis. Nat New Biol. 1971 Aug 4;232(31):153–155. doi: 10.1038/newbio232153a0. [DOI] [PubMed] [Google Scholar]
- Axline S. G., Reaven E. P. Inhibition of phagocytosis and plasma membrane mobility of the cultivated macrophage by cytochalasin B. Role of subplasmalemmal microfilaments. J Cell Biol. 1974 Sep;62(3):647–659. doi: 10.1083/jcb.62.3.647. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Branton D., Bullivant S., Gilula N. B., Karnovsky M. J., Moor H., Mühlethaler K., Northcote D. H., Packer L., Satir B., Satir P. Freeze-etching nomenclature. Science. 1975 Oct 3;190(4209):54–56. doi: 10.1126/science.1166299. [DOI] [PubMed] [Google Scholar]
- Chang C. M., Goldman R. D. The localization of actin-like fibers in cultured neuroblastoma cells as revealed by heavy meromyosin binding. J Cell Biol. 1973 Jun;57(3):867–874. doi: 10.1083/jcb.57.3.867. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chen Y. S., Hubbell W. L. Temperature- and light-dependent structural changes in rhodopsin-lipid membranes. Exp Eye Res. 1973 Dec 24;17(6):517–532. doi: 10.1016/0014-4835(73)90082-1. [DOI] [PubMed] [Google Scholar]
- Comly L. T. Microfilaments in Chaos carolinensis. Membrane association, distribution, and heavy meromyosin binding in the glycerinated cell. J Cell Biol. 1973 Jul;58(1):230–237. doi: 10.1083/jcb.58.1.230. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Goodenough D. A. Bulk isolation of mouse hepatocyte gap junctions. Characterization of the principal protein, connexin. J Cell Biol. 1974 May;61(2):557–563. doi: 10.1083/jcb.61.2.557. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Helenius A., Simons K. Solubilization of membranes by detergents. Biochim Biophys Acta. 1975 Mar 25;415(1):29–79. doi: 10.1016/0304-4157(75)90016-7. [DOI] [PubMed] [Google Scholar]
- Ishikawa H., Bischoff R., Holtzer H. Formation of arrowhead complexes with heavy meromyosin in a variety of cell types. J Cell Biol. 1969 Nov;43(2):312–328. [PMC free article] [PubMed] [Google Scholar]
- Jeon K. W., Jeon M. S. Cytoplasmic filaments and cellular wound healing in Amoeba proteus. J Cell Biol. 1975 Oct;67(1):243–249. doi: 10.1083/jcb.67.1.243. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Longo F. J., Dornfeld E. J. The fine structure of spermatid differentiation in the mussel, Mytilus edulis. J Ultrastruct Res. 1967 Oct 31;20(5):462–480. doi: 10.1016/s0022-5320(67)80113-8. [DOI] [PubMed] [Google Scholar]
- Mooseker M. S., Tilney L. G. Organization of an actin filament-membrane complex. Filament polarity and membrane attachment in the microvilli of intestinal epithelial cells. J Cell Biol. 1975 Dec;67(3):725–743. doi: 10.1083/jcb.67.3.725. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mukherjee T. M., Staehelin L. A. The fine-structural organization of the brush border of intestinal epithelial cells. J Cell Sci. 1971 May;8(3):573–599. doi: 10.1242/jcs.8.3.573. [DOI] [PubMed] [Google Scholar]
- NIIJIMA L., DAN J. THE ACROSOME REACTION IN MYTILUS EDULIS. I. FINE STRUCTURE OF THE INTACT ACROSOME. J Cell Biol. 1965 May;25:243–248. doi: 10.1083/jcb.25.2.243. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Palevitz B. A., Hepler P. K. Identification of actin in situ at the ectoplasm-endoplasm interface of Nitella. Microfilament-chloroplast association. J Cell Biol. 1975 Apr;65(1):29–38. doi: 10.1083/jcb.65.1.29. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Perdue J. F. The distribution, ultrastructure, and chemistry of microfilaments in cultured chick embryo fibroblasts. J Cell Biol. 1973 Aug;58(2):265–283. doi: 10.1083/jcb.58.2.265. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Perry M. M., John H. A., Thomas N. S. Actin-like filaments in the cleavage furrow of newt egg. Exp Cell Res. 1971 Mar;65(1):249–253. doi: 10.1016/s0014-4827(71)80075-7. [DOI] [PubMed] [Google Scholar]
- Pollard T. D., Korn E. D. Electron microscopic identification of actin associated with isolated amoeba plasma membranes. J Biol Chem. 1973 Jan 25;248(2):448–450. [PubMed] [Google Scholar]
- Pollard T. D., Weihing R. R. Actin and myosin and cell movement. CRC Crit Rev Biochem. 1974 Jan;2(1):1–65. doi: 10.3109/10409237409105443. [DOI] [PubMed] [Google Scholar]
- Schroeder T. E. Actin in dividing cells: contractile ring filaments bind heavy meromyosin. Proc Natl Acad Sci U S A. 1973 Jun;70(6):1688–1692. doi: 10.1073/pnas.70.6.1688. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schroeder T. E. Dynamics of the contractile ring. Soc Gen Physiol Ser. 1975;30:305–334. [PubMed] [Google Scholar]
- Segrest J. P., Gulik-Krzywicki T., Sardet C. Association of the membrane-penetrating polypeptide segment of the human erythrocyte MN-glycoprotein with phospholipid bilayers. I. Formation of freeze-etch intramembranous particles. Proc Natl Acad Sci U S A. 1974 Aug;71(8):3294–3298. doi: 10.1073/pnas.71.8.3294. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Spooner B. S., Ash J. F., Wrenn J. T., Frater R. B., Wessells N. K. Heavy meromyosin binding to microfilaments involved in cell and morphogenetic movements. Tissue Cell. 1973;5(1):37–46. doi: 10.1016/s0040-8166(73)80004-7. [DOI] [PubMed] [Google Scholar]
- Tilney L. G. Actin filaments in the acrosomal reaction of Limulus sperm. Motion generated by alterations in the packing of the filaments. J Cell Biol. 1975 Feb;64(2):289–310. doi: 10.1083/jcb.64.2.289. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tilney L. G., Hatano S., Ishikawa H., Mooseker M. S. The polymerization of actin: its role in the generation of the acrosomal process of certain echinoderm sperm. J Cell Biol. 1973 Oct;59(1):109–126. doi: 10.1083/jcb.59.1.109. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tilney L. G., Mooseker M. Actin in the brush-border of epithelial cells of the chicken intestine. Proc Natl Acad Sci U S A. 1971 Oct;68(10):2611–2615. doi: 10.1073/pnas.68.10.2611. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tilney L. G. The role of actin in nonmuscle cell motility. Soc Gen Physiol Ser. 1975;30:339–388. [PubMed] [Google Scholar]
- Tomita M., Marchesi V. T. Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin. Proc Natl Acad Sci U S A. 1975 Aug;72(8):2964–2968. doi: 10.1073/pnas.72.8.2964. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zucker-Franklin D., Grusky G. The actin and myosin filaments of human and bovine blood platelets. J Clin Invest. 1972 Feb;51(2):419–430. doi: 10.1172/JCI106828. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zucker-Franklin D. The submembranous fibrils of human blood platelets. J Cell Biol. 1970 Oct;47(1):293–299. doi: 10.1083/jcb.47.1.293. [DOI] [PMC free article] [PubMed] [Google Scholar]