Directed motility of phagosomes inTetrahymena thermophila requires actin and Myo1p, a novel unconventional myosin
Abstract
The phagosome cycle was investigated in Tetrahymena thermophila, which had internalized fluorescent latex beads. Confocal microscopy of cells from a GFP-actin strain revealed actin filaments that extended 3-5 mum from the periphery of fluorescent phagosomes. In GFP-actin cells and in wild-type cells, motility of fluorescent phagosomes was directed from the oral cavity to the posterior end of the cell. Although 60% of fluorescent phagosomes in the MYO1-knockout strain were motile, movement of phagosomes was not directed toward the posterior end of the cell and was random. Forty percent of fluorescent phagosomes in knockout cells were non-motile in contrast to only 20% non-motile phagosomes in wild-type cells. The increased incidence of non-motile phagosomes in the knockout strain could reflect absence of Myo1p as a motor. Another myosin or other molecular motors could power random movement of phagosomes in the MYO1-knockout strain. In latrunculin-treated GFP-actin cells, movement of fluorescent phagosomes was random. Average velocity of random movement of fluorescent phagosomes in the knockout strain and in latrunculin-treated cells was statistically the same as the average velocity (2.0 +/- 1.9 microm/min) of phagosomes in GFP-actin cells. These findings are an indication that dynamic actin and Myo1p are required for directed motility of phagosomes.
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In Tetrahymena thermophilia, Myo-1 is required for directed motility of latex-bead phagosomes.
“In Tetrahymena thermophilia, a myosin, Myo-1, is required for the directed motility of latex-bead phagosomes (Hosein et al., 2005).”
From Microtubule motors transport phagosomes in the RPE, and lack of KLC1 leads to AMD-like pathogenesis (2015) · cites this paper as Hosein et al., 2005
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Microtubule motors transport phagosomes in the RPE, and lack of KLC1 leads to AMD-like pathogenesis
Jiang, M., Esteve-Rudd, J., Lopes, V. S., Diemer, T., Lillo, C., Rump, A., & Williams, D. S. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201410112 · Cited by 85 · see citing works
- Authors
- Hosein, R. E., Williams, S. A., & Gavin, R. H.
- Affiliations
- Brooklyn College (US)
- Corresponding author
- Gavin, R. H.
- Venue
- Cell Motility and the Cytoskeleton
- Publisher
- Wiley
- Published
- 2005
- Volume
- 61
- Issue
- 1
- Pages
- 49-60
- ISSN
- 0886-1544 (ISSN-L)
- 1097-0169
- OpenAlex
- W2072087299
- Cited by
- 21
- References
- 56
- Citations by year
- 2025: 1 · 2022: 2 · 2016: 1 · 2015: 2 · 2014: 1 · 2013: 1 · 2012: 1
- FWCI
- 1.08
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cell Motility and the Cytoskeleton (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- Tetrahymena thermophila, unconventional myosins, F-actin, latrunculin, ciliate feeding, molecular motors
- MeSH terms
- Actins, Animals, Antineoplastic Agents, Microspheres, Phagosomes, Recombinant Fusion Proteins, Thiazoles, Nocodazole, Protozoan Proteins, Cell Polarity, Tetrahymena thermophila, Microscopy, Confocal, Myosin Heavy Chains, Bridged Bicyclo Compounds, Heterocyclic, Animals, Genetically Modified, Thiazolidines
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