Propulsion of organelles isolated from Acanthamoeba along actin filaments by myosin-I - PubMed (original) (raw)
. 1986 Aug;322(6081):754-6.
doi: 10.1038/322754a0.
- PMID: 3748157
- DOI: 10.1038/322754a0
Propulsion of organelles isolated from Acanthamoeba along actin filaments by myosin-I
R J Adams et al. Nature. 1986 Aug.
Abstract
Eukaryotic cells are dependent on their ability to translocate membraneous elements about the cytoplasm. In many cells long translocations of organelles are associated with microtubules. In other cases, such as the rapid cytoplasmic streaming in some algae, organelles appear to be propelled along actin filaments. It has been assumed, but not proven, that myosin produces these movements. We have tested vesicles from another eukaryotic cell for their ability to move on the exposed actin bundles of Nitella as an indiction that actin-based organelle movements may be a general property of cells. We found that organelles from Acanthamoeba castellanii can move along Nitella actin filaments. Here, we report two different experiments indicating that the single-headed non-polymerizable myosin isozyme myosin-I is responsible for this organelle motility. First, monoclonal antibodies to myosin-I inhibit movement, but antibodies that inhibit double-headed myosin-II do not. Second, approximately 20% of the myosin-I in homogenates co-migrates with motile vesicles during Percoll density-gradient ultracentrifugation. This is the first indication of a role for myosin-I within the cell and supports the suggestion of Albanesi et al. that myosin-I moves vesicles in this way.
Similar articles
- Hydrodynamic models of viscous coupling between motile myosin and endoplasm in characean algae.
Nothnagel EA, Webb WW. Nothnagel EA, et al. J Cell Biol. 1982 Aug;94(2):444-54. doi: 10.1083/jcb.94.2.444. J Cell Biol. 1982. PMID: 7202011 Free PMC article. - The elongation and contraction of actin bundles are induced by double-headed myosins in a motor concentration-dependent manner.
Tanaka-Takiguchi Y, Kakei T, Tanimura A, Takagi A, Honda M, Hotani H, Takiguchi K. Tanaka-Takiguchi Y, et al. J Mol Biol. 2004 Aug 6;341(2):467-76. doi: 10.1016/j.jmb.2004.06.019. J Mol Biol. 2004. PMID: 15276837 - Microinjection into Acanthamoeba castellanii of monoclonal antibodies to myosin-II slows but does not stop cell locomotion.
Sinard JH, Pollard TD. Sinard JH, et al. Cell Motil Cytoskeleton. 1989;12(1):42-52. doi: 10.1002/cm.970120106. Cell Motil Cytoskeleton. 1989. PMID: 2523248 - Myosin VI: a structural role in actin organization important for protein and organelle localization and trafficking.
Frank DJ, Noguchi T, Miller KG. Frank DJ, et al. Curr Opin Cell Biol. 2004 Apr;16(2):189-94. doi: 10.1016/j.ceb.2004.02.001. Curr Opin Cell Biol. 2004. PMID: 15196563 Review.
Cited by
- Yeast actin-binding proteins: evidence for a role in morphogenesis.
Drubin DG, Miller KG, Botstein D. Drubin DG, et al. J Cell Biol. 1988 Dec;107(6 Pt 2):2551-61. doi: 10.1083/jcb.107.6.2551. J Cell Biol. 1988. PMID: 3060468 Free PMC article. - Dictyostelium discoideum contains a gene encoding a myosin I heavy chain.
Jung G, Saxe CL 3rd, Kimmel AR, Hammer JA 3rd. Jung G, et al. Proc Natl Acad Sci U S A. 1989 Aug;86(16):6186-90. doi: 10.1073/pnas.86.16.6186. Proc Natl Acad Sci U S A. 1989. PMID: 2762320 Free PMC article. - Multiple actin-based motor genes in Dictyostelium.
Titus MA, Warrick HM, Spudich JA. Titus MA, et al. Cell Regul. 1989 Nov;1(1):55-63. doi: 10.1091/mbc.1.1.55. Cell Regul. 1989. PMID: 2519618 Free PMC article. - The yeast type II myosin heavy chain: analysis of its predicted polypeptide sequence.
Sweeney FP, Pocklington MJ, Orr E. Sweeney FP, et al. J Muscle Res Cell Motil. 1991 Feb;12(1):61-8. doi: 10.1007/BF01781175. J Muscle Res Cell Motil. 1991. PMID: 2050812 - Identification of actin filaments in the rhabdomeral microvilli of Drosophila photoreceptors.
Arikawa K, Hicks JL, Williams DS. Arikawa K, et al. J Cell Biol. 1990 Jun;110(6):1993-8. doi: 10.1083/jcb.110.6.1993. J Cell Biol. 1990. PMID: 2112548 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources