Pea2 protein of yeast is localized to sites of polarized growth and is required for efficient mating and bipolar budding.

Valtz, N; Herskowitz, Ira

doi:10.1083/jcb.135.3.725

Cited by 91 publications

(131 citation statements)

References 40 publications

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“…All components of the polarisome localize to the sites of polarized growth. Deletion of each component causes a defect in bipolar bud site selection and a moderate defect in polarized growth at all temperatures, resulting in rounder cells, and cells with any of these components deleted show synthetically lethal interaction with gic1⌬ gic2⌬ cells (30,39,62,63,66,70). These data suggest that the polarisome and Gic1/Gic2 may act in parallel to control polarized growth.…”

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confidence: 74%

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Regulation of Cell Polarity by Interactions of Msb3 and Msb4 with Cdc42 and Polarisome Components

Tcheperegine

Gao

2005

Molecular and Cellular Biology

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In Saccharomyces cerevisiae, polarized growth depends on interactions between the actin cytoskeleton and the secretory machinery. Here we show that the Rab GTPase-activating proteins (GAPs) Msb3 and Msb4 interact directly with Spa2, a scaffold protein of the "polarisome" that also interacts with the formin Bni1. Spa2 is required for the polarized localization of Msb3 and Msb4 at the bud tip. We also show that Msb3 and Msb4 bind specifically to Cdc42-GDP and Rho1-GDP in vitro and that Msb3 and Rho GDP dissociation inhibitor act independently but oppositely on Cdc42. Finally, we show that Msb3 and Msb4 are involved in Bni1-nucleated actin assembly in vivo. These results suggest that Msb3 and Msb4 regulate polarized growth by multiple mechanisms, directly regulating exocytosis through their GAP activity toward Sec4 and potentially coordinating the functions of Cdc42, Rho1, and Bni1 in the polarisome through their binding to these GTPases. A functional equivalent of the polarisome probably exists in other fungi and mammals.Cell polarity is essential for the development and differentiation of most unicellular and multicellular organisms. Core mechanisms underlying cell polarity appear conserved from yeasts to humans at both the conceptual and the molecular level (46). In the budding yeast Saccharomyces cerevisiae, polarized cell growth is achieved through a multistage process. The cell first selects a cortical site for cell polarization, then marks that site with polarity establishment proteins, and finally polarizes the actin cytoskeleton, including the actin cables and patches, at the marked site. The actin cables then direct secretion to the chosen site to form a bud (53, 54).Cdc42, a conserved Rho GTPase, affects polarized actin organization and secretion in both S. cerevisiae and mammalian cells (2,3,32,36,45,49,50,72). In S. cerevisiae, Cdc42 plays an essential role in polarity establishment (31, 54). Conditional inactivation of Cdc42 with temperature-sensitive mutations in CDC42 or CDC24, which encodes the guanine nucleotide exchange factor (GEF) for Cdc42, results in complete loss of polarized actin organization and secretion (3,64,75).

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confidence: 74%

“…Bud6 is an actin monomer-binding protein that promotes Bni1-stimulated actin assembly in vitro (6,44). The biochemical function of Pea2 is not known (66). All components of the polarisome localize to the sites of polarized growth.…”

mentioning

confidence: 99%

Regulation of Cell Polarity by Interactions of Msb3 and Msb4 with Cdc42 and Polarisome Components

Tcheperegine

Gao

2005

Molecular and Cellular Biology

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“…Similar dependencies between polarisome components are described in budding yeast. ScSpa2 and ScPea2 play an important role for recruitment of ScBni1, ScSpa2 and ScPea2 (Fujiwara et al, 1998;Ozaki-Kuroda et al, 2001;Sheu et al, 1998;Valtz and Herskowitz, 1996), whereas lack of ScBud6 only slightly disturbs ScBni1 localization (Jin and Amberg, 2000;Ozaki-Kuroda et al, 2001). Thus, in both A. gossypii and budding yeast, Bni1, Spa2 and Pea2 seem to form a functional unit.…”

Section: Localization Of Polarisome Components In Deletion Strainsmentioning

confidence: 99%

Growth-speed-correlated localization of exocyst and polarisome components in growth zones of Ashbya gossypii hyphal tips

Köhli

Galati

Boudier

et al. 2008

Journal of Cell Science

109

121

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“…The second class of genes, which includes SPA2, PEA2, and BUD6-BUD9, is required specifically in a/␣ cells. Mutations in any of these genes cause a random budding pattern in a/␣ cells but do not affect the axial budding pattern of a and ␣ cells (Snyder 1989;Valtz and Herskowitz 1996;Zahner et al 1996). These genes are hypothesized to determine the bipolar cortical cues.…”

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confidence: 99%

Localization of Bud2p, a GTPase-activating protein necessary for programming cell polarity in yeast to the presumptive bud site

Park¹,

Sanson²,

Herskowitz³

1999

Genes & Development

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Yeast cells of different cell type exhibit distinct budding patterns that reflect the organization of the actin cytoskeleton. Bud1p (Rsr1p), a Ras-like GTPase, and Bud2p, a GTPase-activating protein for Bud1p, are essential for proper budding pattern. We show that Bud2p is localized at the presumptive bud site in G 1 cells in all cell types and that this localization is independent of Bud1p. Bud2p subsequently localizes to the mother-bud neck after bud emergence; this localization depends on the integrity of the septins. These observations indicate that Bud2p becomes positioned in G 1 cells by recognizing cell type-specific landmarks at the presumptive bud site.

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Pea2 protein of yeast is localized to sites of polarized growth and is required for efficient mating and bipolar budding.

Cited by 91 publications

References 40 publications

Regulation of Cell Polarity by Interactions of Msb3 and Msb4 with Cdc42 and Polarisome Components

Regulation of Cell Polarity by Interactions of Msb3 and Msb4 with Cdc42 and Polarisome Components

Growth-speed-correlated localization of exocyst and polarisome components in growth zones of Ashbya gossypii hyphal tips

Localization of Bud2p, a GTPase-activating protein necessary for programming cell polarity in yeast to the presumptive bud site

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