DOI: 10.1091/mbc.11.5.1727. Role of Actin and Myo2p in Polarized Secretion and Growth of<i>Saccharomyces cerevisiae</i>

Role of Actin and Myo2p in Polarized Secretion and Growth ofSaccharomyces cerevisiae

10.1091/mbc.11.5.1727

Crossref journal-article

American Society for Cell Biology (ASCB)

Molecular Biology of the Cell (1076)

Abstract

We examined the role of the actin cytoskeleton in secretion inSaccharomyces cerevisiae with the use of several quantitative assays, including time-lapse video microscopy of cell surface growth in individual living cells. In latrunculin, which depolymerizes filamentous actin, cell surface growth was completely depolarized but still occurred, albeit at a reduced level. Thus, filamentous actin is necessary for polarized secretion but not for secretion per se. Consistent with this conclusion, latrunculin caused vesicles to accumulate at random positions throughout the cell. Cortical actin patches cluster at locations that correlate with sites of polarized secretion. However, we found that actin patch polarization is not necessary for polarized secretion because a mutant,bee1Δ(las17Δ), which completely lacks actin patch polarization, displayed polarized growth. In contrast, a mutant lacking actin cables, tpm1-2 tpm2Δ, had a severe defect in polarized growth. The yeast class V myosin Myo2p is hypothesized to mediate polarized secretion. A mutation in the motor domain of Myo2p,myo2-66, caused growth to be depolarized but with only a partial decrease in the level of overall growth. This effect is similar to that of latrunculin, suggesting that Myo2p interacts with filamentous actin. However, inhibition of Myo2p function by expression of its tail domain completely abolished growth.

Bibliography

Karpova, T. S., Reck-Peterson, S. L., Elkind, N. B., Mooseker, M. S., Novick, P. J., & Cooper, J. A. (2000). Role of Actin and Myo2p in Polarized Secretion and Growth ofSaccharomyces cerevisiae. Molecular Biology of the Cell, 11(5), 1727â1737.

Authors 6

Tatiana S. Karpova (first)
Samara L. Reck-Peterson (additional)
N. Barry Elkind (additional)
Mark S. Mooseker (additional)
Peter J. Novick (additional)
John A. Cooper (additional)

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Dates

Type	When
Created	12 years, 2 months ago (July 2, 2013, 7:51 p.m.)
Deposited	3 years, 6 months ago (Feb. 26, 2022, 9:41 p.m.)
Indexed	1 year, 1 month ago (Aug. 3, 2024, 4:16 p.m.)
Issued	25 years, 4 months ago (May 1, 2000)
Published	25 years, 4 months ago (May 1, 2000)
Published Print	25 years, 4 months ago (May 1, 2000)

Funders 0

None

BibTeX

@article{Karpova_2000, title={Role of Actin and Myo2p in Polarized Secretion and Growth ofSaccharomyces cerevisiae}, volume={11}, ISSN={1939-4586}, url={http://dx.doi.org/10.1091/mbc.11.5.1727}, DOI={10.1091/mbc.11.5.1727}, number={5}, journal={Molecular Biology of the Cell}, publisher={American Society for Cell Biology (ASCB)}, author={Karpova, Tatiana S. and Reck-Peterson, Samara L. and Elkind, N. Barry and Mooseker, Mark S. and Novick, Peter J. and Cooper, John A.}, editor={Schekman, Randy W.}, year={2000}, month=may, pages={1727–1737} }

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  "abstract": "<jats:p>We examined the role of the actin cytoskeleton in secretion inSaccharomyces cerevisiae with the use of several quantitative assays, including time-lapse video microscopy of cell surface growth in individual living cells. In latrunculin, which depolymerizes filamentous actin, cell surface growth was completely depolarized but still occurred, albeit at a reduced level. Thus, filamentous actin is necessary for polarized secretion but not for secretion per se. Consistent with this conclusion, latrunculin caused vesicles to accumulate at random positions throughout the cell. Cortical actin patches cluster at locations that correlate with sites of polarized secretion. However, we found that actin patch polarization is not necessary for polarized secretion because a mutant,bee1\u0394(las17\u0394), which completely lacks actin patch polarization, displayed polarized growth. In contrast, a mutant lacking actin cables, tpm1-2 tpm2\u0394, had a severe defect in polarized growth. The yeast class V myosin Myo2p is hypothesized to mediate polarized secretion. A mutation in the motor domain of Myo2p,myo2-66, caused growth to be depolarized but with only a partial decrease in the level of overall growth. This effect is similar to that of latrunculin, suggesting that Myo2p interacts with filamentous actin. However, inhibition of Myo2p function by expression of its tail domain completely abolished growth.</jats:p>",
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