Nucleotide sequence of the CLS4 (CDC24) gene of Saccharomyces cerevisiae

Miyamoto, Shigehiko; Ohya, Yoshikazu; Ohsumi, Yoshinori; Anraku, Yasuhiro

doi:10.1016/0378-1119(87)90354-4

Cited by 84 publications

(39 citation statements)

References 25 publications

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“…The cdc24-4 mutation was found to be suppressed by overproduction of CDC42 (Bender and Pringle, 1989), but Cdc24p is not a member of the small GTPase family and its primary structure does not contain the Cys-AliAli-Leu sequence that is a substrate for GGTase I (Miyamoto et al, 1987(Miyamoto et al, , 1991. We have begun to isolate spontaneous mutations that allow the integrated copies of RHOI (L209M) and CDC42 (L191M) to suppress the GGTase I deletion.…”

Section: Discussionmentioning

confidence: 99%

Suppression of yeast geranylgeranyl transferase I defect by alternative prenylation of two target GTPases, Rho1p and Cdc42p.

Ohya

Qadota

Anraku

et al. 1993

MBoC

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Geranylgeranyl transferase I (GGTase I), which modifies proteins containing the sequence Cys-Ali-Ali-Leu (Ali: aliphatic) at their C-termini, is indispensable for growth in the budding yeast Saccharomyces cerevisiae. We report here that GGTase I is no longer essential when Rho1p and Cdc42p are simultaneously overproduced. The lethality of a GGTase I deletion is most efficiently suppressed by provision of both Rho1p and Cdc42p with altered C-terminal sequences (Cys-Ali-Ali-Met) corresponding to the C-termini of substrates of farnesyl transferase (FTase). Under these circumstances, the FTase, normally not essential for growth of yeast, becomes essential.

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Section: Discussionmentioning

confidence: 99%

Suppression of yeast geranylgeranyl transferase I defect by alternative prenylation of two target GTPases, Rho1p and Cdc42p.

Ohya

Qadota

Anraku

et al. 1993

MBoC

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“…A localized elevation in intracellular Ca2" levels could cause organization of the cytoskeleton in the proper place by activating polarity-establishment gene products. Sequence analysis and the isolation of calcium-sensitive alleles suggest that Cdc24 protein may bind calcium (Ohya et al, 1986;Miyamoto et al, 1987). A yeast phospholipase C has recently been identified (Payne and Fitzgerald-Hayes, 1993), but mutants in the phospholipase C gene were not reported to display any defects in mating or shmooing.…”

Section: Chemotaxismentioning

confidence: 99%

Cell polarization directed by extracellular cues in yeast.

Chênevert

1994

MBoC

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Many cell types are able to generate cellular asymmetry, or polarize, in response to chemical gradients in the environment. The question of how external signals influence cell polarity requires an understanding of how a chemoattractant signaling pathway leads to organization of the cytoskeleton. Studies of polarizing yeast cells and other chemotactic cells indicate that similar molecules and pathways may be involved in these diverse systems. This review will focus on cell polarization in response to extracellular signals during yeast mating. First, the phenomenon of cell polarization during yeast mating will be described. Then the extensive work on cell polarization during yeast budding will be reviewed, and a model for mating cell polarity will be presented. Finally, eucaryotic chemotaxis will be briefly summarized, and the similarities to polarization during yeast mating will be discussed.

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“…Viability of the cotransformants in the absence of histidine indicates a positive interaction, although ␤-galactoside activity is much lower than with other promoters (36); under these conditions, no false-positive colonies were observed under His Ϫ selection. Plasmid pGBT::Cdc24, which contained the complete coding sequence of CDC24 (CLS4 [45]), using the corrected initiation site (46), rescued both growth and pheromone response defects in the cdc24-4 ts strain, indicating the fusion protein to be functional (Fig. 5).…”

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confidence: 99%

Pheromone Signalling in Saccharomyces cerevisiae Requires the Small GTP-Binding Protein Cdc42p and Its Activator CDC24

Zhao

Leung

Manser

et al. 1995

Molecular and Cellular Biology

190

184

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Pheromone signalling in Saccharomyces cerevisiae is mediated by the STE4-STE18 G-protein ␤␥ subunits. A possible target for the subunits is Ste20p, whose structural homolog, the serine/threonine kinase PAK, is activated by GTP-binding p21s Cdc42 and Rac1. The putative Cdc42p-binding domain of Ste20p, expressed as a fusion protein, binds human and yeast GTP-binding Cdc42p. Cdc42p is required for ␣-factor-induced activation of FUS1. cdc24 ts strains defective for Cdc42p GDP/GTP exchange show no pheromone induction at restrictive temperatures but are partially rescued by overexpression of Cdc42p, which is potentiated by Cdc42p 12V mutants. Epistatic analysis indicates that CDC24 and CDC42 lie between STE4 and STE20 in the pathway. The two-hybrid system revealed that Ste4p interacts with Cdc24p. We propose that Cdc42p plays a pivotal role both in polarization of the cytoskeleton and in pheromone signalling.In eukaryotic cells, many growth and differentiation signals are channelled through protein phosphorylation cascades that involve the mitogen-activated protein (MAP) kinase family. The similarity of MAP kinase cascades in multicellular organisms to those in the yeast Saccharomyces cerevisiae is a subject of great interest (7,17,42,50). One of the best studied of these cascades at the genetic level is the pheromone-dependent pathway in S. cerevisiae, which links occupation of pheromone receptors by a-or ␣-factor to a variety of events that lead to mating (for reviews, see references 3, 27, and 41). The pheromone-induced transcriptional activation of mating-specific genes requires a kinase cascade that includes the protein kinases encoded by STE20, STE11, STE7, KSS1, and FUS3. Activation of the pathway is initiated by the heterotrimeric G-protein ␤␥ subunits encoded by STE4 and STE18 (71, 72); the STE20 gene product is a kinase which may lie at the top of the kinase cascade and has been implicated as a target of the STE4-encoded ␤ subunit (32). In mammalian cells, the activation of MAP kinase by various proto-oncogenic tyrosine kinases requires small GTP-binding proteins (p21s) of the Ras family; more recently, heterotrimeric G-protein signalling to MAP kinase has been shown to be mediated by ␤␥ subunits via Ras (13). While the mating pathway in Schizosaccharomyces pombe parallels this pathway in requiring ras1 (73), there has been no evidence for the involvement of a p21 in the S. cerevisiae pheromone-induced kinase cascade.We have described a number of proteins that appear to be the target of the Rho subfamily of p21s (39,40). One of these proteins was purified and shown to be a serine/threonine kinase that is directly activated by GTP-binding Cdc42 (GTPCdc42p) and GTP-Rac1. This brain-enriched kinase, designated PAK (40), is related to Ste20p both in the kinase domain and in a separate region identified as the p21-binding domain. These findings suggested that Cdc42p, a p21 first identified as a gene product required for polarized budding (29), participates in the mating response (Rac has not been found in S. cere...

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Nucleotide sequence of the CLS4 (CDC24) gene of Saccharomyces cerevisiae

Cited by 84 publications

References 25 publications

Suppression of yeast geranylgeranyl transferase I defect by alternative prenylation of two target GTPases, Rho1p and Cdc42p.

Suppression of yeast geranylgeranyl transferase I defect by alternative prenylation of two target GTPases, Rho1p and Cdc42p.

Cell polarization directed by extracellular cues in yeast.

Pheromone Signalling in Saccharomyces cerevisiae Requires the Small GTP-Binding Protein Cdc42p and Its Activator CDC24

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