A DBL-homologous region of the yeast   gene product is important for Ca2+-modulated bud assembly

Miyamoto, Shigehiko; Ohya, Yoshikazu; Sano, Yoshifumi; Sakaguchi, Shuichi; Iida, Hidetoshi; Anraku, Yasuhiro

doi:10.1016/0006-291x(91)91233-3

Cited by 34 publications

(19 citation statements)

References 10 publications

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“…In an early study of mating in 19 cdc mutants (56), two temperature-sensitive alleles of CDC24 were shown to exhibit the greatest deficiency in diploid formation at 35ЊC (Ͻ0.01% of that at the permissive temperature) when mixed with a wild-type ␣ tester strain. The CDC24 gene product has a complex role during bud formation and growth (63) and is a putative calcium-regulated protein (46). Most of the steps of the pheromone response pathway have been defined genetically by null alleles of so-called sterile (STE) genes that block mating.…”

Section: Discussionmentioning

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

183

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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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Section: Discussionmentioning

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

183

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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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“…Although no GEF activity of Cdc24p upon Rholp was detected in vitro (Zheng et al 1994b), it is possible that such activity occurs in vivo or that one of the other Rho proteins is a Cdc24p target. In addition, the domains of Cdc24p implicated in its GEF activity (amino acids 281-518 [Hart et al 1991;Miyamoto et al 1991;Zheng et al 1994b]) and in its interactions with Bemlp (amino acids 780-854 [Peterson et al 1994]) and Rsrlp (amino acids 473-854 [H.-O. Park and I. Herskowitz, pers.…”

Section: Polarity-establishment and Polarity-maintenance Functions: Amentioning

confidence: 99%

Establishment of Cell Polarity in Yeast

Pringle¹,

Bi²,

A.³

et al. 1995

Cold Spring Harbor Symposia on Quantitative Biology

167

169

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A DBL-homologous region of the yeast gene product is important for Ca2+-modulated bud assembly

Cited by 34 publications

References 10 publications

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

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

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

Establishment of Cell Polarity in Yeast

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