Role of actin and Myo2p in polarized secretion and growth of Saccharomyces cerevisiae.

Karpova, T S; Reck-Peterson, S L; Elkind, N B; Mooseker, M S; Novick, P J; Cooper, J A

Karpova, T S; Reck-Peterson, S L; Elkind, N B; Mooseker, M S; Novick, P J; Cooper, J A.

Afiliación

Karpova TS; Department of Cell Biology and Physiology, Washington University, St. Louis, Missouri 63110, USA.

Mol Biol Cell ; 11(5): 1727-37, 2000 May.

Article en En | MEDLINE | ID: mdl-10793147

RESUMEN

We examined the role of the actin cytoskeleton in secretion in Saccharomyces 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, bee1Delta(las17Delta), which completely lacks actin patch polarization, displayed polarized growth. In contrast, a mutant lacking actin cables, tpm1-2 tpm2Delta, 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.

Asunto(s)

Actinas/metabolismo; Proteínas Portadoras/metabolismo; Proteínas Fúngicas/metabolismo; Cadenas Pesadas de Miosina; Miosina Tipo II; Miosina Tipo V; Proteínas de Saccharomyces cerevisiae; Saccharomyces cerevisiae/fisiología; Proteínas de Schizosaccharomyces pombe; Citoesqueleto de Actina/efectos de los fármacos; Citoesqueleto de Actina/metabolismo; Citoesqueleto de Actina/ultraestructura; Actinas/efectos de los fármacos; Actinas/genética; Compuestos Bicíclicos Heterocíclicos con Puentes/farmacología; Proteínas Portadoras/genética; División Celular; Polaridad Celular; Proteínas Fúngicas/genética; Proteínas Fluorescentes Verdes; Proteínas Luminiscentes/genética; Proteínas Luminiscentes/metabolismo; Microscopía por Video/métodos; Mutación; Proteínas Recombinantes/genética; Proteínas Recombinantes/metabolismo; Saccharomyces cerevisiae/efectos de los fármacos; Saccharomyces cerevisiae/ultraestructura; Tiazoles/farmacología; Tiazolidinas

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Proteínas Fúngicas / Proteínas Portadoras / Actinas / Cadenas Pesadas de Miosina / Miosina Tipo II / Miosina Tipo V / Proteínas de Saccharomyces cerevisiae / Proteínas de Schizosaccharomyces pombe Idioma: En Revista: Mol Biol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2000 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

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