Wsc1 and Mid2 Are Cell Surface Sensors for Cell Wall Integrity Signaling That Act through Rom2, a Guanine Nucleotide Exchange Factor for Rho1

REFERENCES

• Buchsbaum, R., J.-B. Telliez, S. Goonesekera, and L. A. Feig. 1996. The N-terminal pleckstrin, coiled-coil, and IQ domains of the exchange factor Ras-GRF act cooperatively to facilitate activation by calcium. Mol. Cell. Biol. 16:4888–4896.
   PubMed Web of Science ®Google Scholar
• Buehrer, B. M., and B. Errede. 1997. Coordination of the mating and cell integrity mitogen-activated protein kinase pathways in Saccharomyces cerevisiae. Mol. Cell. Biol. 17:6517–6525.
   PubMed Web of Science ®Google Scholar
• Chen, R. E., T. Michaeli, L. Van Aelst, and R. Ballester. 2000. A role for the noncatalytic N terminus in the function of Cdc25, a Saccharomyces cerevisiae Ras-guanine nucleotide exchange factor. Genetics 154:1473–1484.
   PubMedGoogle Scholar
• Cid, V. J., A. Durán, F. del Rey, M. P. Snyder, C. Nombela, and M. Sánchez. 1995. Molecular basis of cell integrity and morphogenesis in Saccharomyces cerevisiae. Microbiol. Rev. 59:345–386.
   PubMedGoogle Scholar
• Costigan, C., S. Gehrung, and M. Snyder. 1992. A synthetic lethal screen identifies SLK1, a novel protein kinase homolog implicated in yeast cell morphogenesis and cell growth. Mol. Cell. Biol. 12:1162–1178.
   PubMedGoogle Scholar
• Davenport, K. R., M. Sohaskey, Y. Kamada, and D. E. Levin. 1995. A second osmosensing signal transduction pathway in yeast. J. Biol. Chem. 270:30157–30161.
   PubMedGoogle Scholar
• Douglas, C. M., F. Foor, J. A. Marrinan, N. Morin, J. B. Nielsen, A. M. Dahl, P. Mazur, W. Baginsky, W. Li, M. El-Sherbeini, J. A. Clemas, S. M. Mandala, B. R. Frommer, and M. B. Kurtz. 1994. The Saccharomyces cerevisiae FKS1 (ETG1) gene encodes an integral membrane protein which is a subunit of 1,3-β-D-glucan synthase. Proc. Natl. Acad. Sci. USA 91:12907–12911.
   PubMed Web of Science ®Google Scholar
• Drgonova, J., T. Drgon, K. Tanaka, R. Kollar, G.-C. Chen, R. A. Ford, C. S. M. Chan, Y. Takai, and E. Cabib. 1996. Rho1p, a yeast protein at the interface between cell polarization and morphogenesis. Science 272:277–279.
   PubMed Web of Science ®Google Scholar
• Errede, B., R. M. Cade, B. M. Yashar, Y. Kamada, D. E. Levin, K. Irie, and K. Matsomoto. 1995. Dynamics and organization of MAP kinase signal pathways. Mol. Reprod. Dev. 42:477–485.
   PubMed Web of Science ®Google Scholar
• Girrbach, V., T. Zeller, M. Priesmeier, and S. Strahl-Bolsinger. 2000. Structure-function analysis of the dolichyl phosphate-mannose: protein O-mannosyltransferase ScPmt1p. J. Biol. Chem. 275:19288–19296.
   PubMedGoogle Scholar
• Gray, J. V., J. P. Ogas, Y. Kamada, M. Stone, D. E. Levin, and I. Herskowitz. 1997. A role for the Pkc1 MAP kinase pathway of Saccharomyces cerevisiae in bud emergence and identification of a putative upstream regulator. EMBO J. 16:4924–4937.
   PubMed Web of Science ®Google Scholar
• Hill, J. E., A. M. Muers, T. J. Koerner, and A. Tzagoloff. 1986. Yeast/E. coli shuttle vectors with multiple unique restriction sites. Yeast 2:163–167.
   PubMed Web of Science ®Google Scholar
• Ho, S.-N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51–59.
   PubMed Web of Science ®Google Scholar
• Iida, H., H. Nakamura, T. Ono, M. S. Okumura, and Y. Anraku. 1994. MID1, a novel Saccharomyces cerevisiae gene encoding a plasma membrane protein, is required for Ca2+ influx and mating. Mol. Cell. Biol. 14:8259–8271.
   PubMed Web of Science ®Google Scholar
• Inoue, S. B., N. Takewaki, T. Takasuka, T. Mio, M. Adachi, Y. Fujii, C. Miyamoto, M. Arisawa, Y. Furuichi, and T. Watanabe. 1995. Characterization and gene cloning of 1,3-β-D-glucan synthase from Saccharomyces cerevisiae. Eur. J. Biochem. 231:845–854.
   PubMedGoogle Scholar
• Irie, K., M. Takase, K. S. Lee, D. E. Levin, H. Araki, K. Matsumoto, and Y. Oshima. 1993. MKK1 and MKK2, which encode Saccharomyces cerevisiae mitogen-activated protein kinase-kinase homologs, function in the pathway mediated by protein kinase C. Mol. Cell. Biol. 13:3076–3083.
   PubMed Web of Science ®Google Scholar
• Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163–168.
   PubMed Web of Science ®Google Scholar
• Jacoby, J. J., S. M. Nilius, and J. J. Heinisch. 1998. A screen for upstream components of the yeast protein kinase C signal transduction pathway identifies the product of the SLG1 gene. Mol. Gen. Genet. 258:148–155.
   PubMedGoogle Scholar
• Jentoft, N.. 1990. Why are proteins O-glycosylated?. Trends Biochem. Sci. 15:291–294.
   PubMed Web of Science ®Google Scholar
• Jung, U. S., and D. E. Levin. 1999. Genome-wide analysis of gene expression regulated by the yeast cell wall integrity signaling pathway. Mol. Microbiol. 34:1049–1057.
   PubMed Web of Science ®Google Scholar
• Kamada, Y., U. S. Jung, J. Piotrowski, and D. E. Levin. 1995. The protein kinase C-activated MAP kinase pathway of Saccharomyces cerevisiae mediates a novel aspect of the heat shock response. Genes Dev. 9:1559–1571.
   PubMed Web of Science ®Google Scholar
• Kamada, Y., H. Qadota, C. P. Python, Y. Anraku, Y. Ohya, and D. E. Levin. 1996. Activation of yeast protein kinase C by Rho1 GTPase. J. Biol. Chem. 271:9193–9195.
   PubMed Web of Science ®Google Scholar
• Ketela, T., R. Green, and H. Bussey. 1999. Saccharomyces cerevisiae Mid2p is a potential cell wall stress sensor and upstream activator of the PKC1-MPK1 cell integrity pathway. J. Bacteriol. 181:3330–3340.
   PubMed Web of Science ®Google Scholar
• Kim, Y. J., L. Francisco, G. C. Chen, E. Marcotte, and C. S. M. Chan. 1994. Control of cellular morphogenesis by the Ipl2/Bem2 GTP-activating protein: possible role of protein phosphorylation. J. Cell Biol. 127:1381–1394.
   PubMedGoogle Scholar
• Klis, F. M.. 1994. Review: cell wall assembly in yeast. Yeast 10:851–869.
   PubMed Web of Science ®Google Scholar
• Lee, K. S., K. Irie, Y. Gotoh, Y. Watanabe, H. Araki, E. Nishida, K. Matsumoto, and D. E. Levin. 1993. A yeast mitogen-activated protein kinase homolog (Mpk1) mediates signalling by protein kinase C. Mol. Cell. Biol. 13:3067–3075.
   PubMed Web of Science ®Google Scholar
• Lee, K. S., and D. E. Levin. 1992. Dominant mutations in a gene encoding a putative protein kinase (BCK1) bypass the requirement for a Saccharomyces cerevisiae protein kinase C homolog. Mol. Cell. Biol. 12:172–182.
   PubMed Web of Science ®Google Scholar
• Levin, D. E., and E. Bartlett-Heubusch. 1992. Mutants in the S. cerevisiae PKC1 gene display a cell cycle-specific osmotic stability defect. J. Cell Biol. 116:1221–1229.
   PubMed Web of Science ®Google Scholar
• Levin, D. E., B. Bowers, C. Chen, Y. Kamada, and M. Watanabe. 1994. Dissecting the protein kinase C/MAP kinase signaling pathway of Saccharomyces cerevisiae. Cell. Mol. Biol. Res. 40:229–239.
   PubMedGoogle Scholar
• Levin, D. E., and B. Errede. 1995. The proliferation of MAP kinase signaling pathways in yeast. Curr. Opin. Cell Biol. 7:197–202.
   PubMed Web of Science ®Google Scholar
• Levin, D. E., F. O. Fields, R. Kunisawa, J. M. Bishop, and J. Thorner. 1990. A candidate protein kinase C gene PKC1, is required for the S. cerevisiae cell cycle. Cell 62:213–224.
   PubMed Web of Science ®Google Scholar
• Lodder, A. L., T. K. Lee, and R. Ballester. 1999. Characterization of the Wsc1 protein, a putative receptor in the stress response of Saccharomyces cerevisiae. Genetics 152:1487–1499.
   PubMed Web of Science ®Google Scholar
• Manning, B. D., R. Padmanabha, and M. Snyder. 1997. The Rho-GEF Rom2p localizes to sites of polarized cell growth and participates in cytoskeletal functions in Saccharomyces cerevisiae. Mol. Biol. Cell 8:1829–1844.
   PubMedGoogle Scholar
• Mazur, P., N. Morin, W. Baginsky, M. El-Sherbeini, J. A. Clemas, J. B. Nielsen, and F. Foor. 1995. Differential expression and function of two homologous subunits of yeast 1,3-β-d-glucan synthase. Mol. Cell. Biol. 15:5671–5681.
   PubMed Web of Science ®Google Scholar
• Nonaka, H., K. Tanaka, H. Hirano, T. Fujiwara, H. Kohno, M. Umikawa, A. Mino, and Y. Takai. 1995. A downstream target of RHO1 small GTP-binding protein is PKC1, a homolog of protein kinase C, which leads to activation of the MAP kinase cascade in Saccharomyces cerevisiae. EMBO J. 14:5931–5938.
   PubMed Web of Science ®Google Scholar
• Ono, T., T. Suzuki, Y. Anraku, and H. Iida. 1994. The MID2 gene encodes a putative integral membrane protein with a Ca(2+)-binding domain and shows mating pheromone-stimulated expression in Saccharomyces cerevisiae. Gene 151:203–208.
   PubMed Web of Science ®Google Scholar
• Ozaki, K., K. Tanaka, H. Imamura, T. Hihara, T. Kamayema, H. Nonaka, H. Hirano, Y. Matsuura, and Y. Takai. 1996. Rom1p and Rom2p are small GDP/GTP exchange proteins (GEPs) for the Rho1p small GTP-binding protein in Saccharomyces cerevisiae. EMBO J. 15:2196–2207.
   PubMed Web of Science ®Google Scholar
• Paravicini, G., M. Cooper, L. Friedli, D. J. Smith, J.-L. Carpentier, L. S. Klig, and M. A. Payton. 1992. The osmotic integrity of the yeast cell requires a functional PKC1 gene product. Mol. Cell. Biol. 12:4896–4905.
   PubMed Web of Science ®Google Scholar
• Peterson, J., Y. Zheng, L. Bender, A. Myers, R. Cerione, and A. Bender. 1994. Interactions between the bud emergence proteins Bem1 and Bem2 and the Rho-type GTPases in yeast. J. Cell Biol. 127:1395–1406.
   PubMedGoogle Scholar
• Qadota, H., C. P. Python, S. B. Inoue, M. Arisawa, Y. Anraku, Y. Zheng, T. Watanabe, D. E. Levin, and Y. Ohya. 1996. Identification of yeast Rho1p GTPase as a regulatory subunit of 1,3-β-glucan synthase. Science 272:279–281.
   PubMed Web of Science ®Google Scholar
• Quilliam, L. A., R. Khosravi-Far, S. Y. Huff, and C. J. Der. 1995. Guanine nucleotide exchange factors: activators of the Ras superfamily of proteins. Bioessays 17:395–404.
   PubMed Web of Science ®Google Scholar
• Rajavel, M., B. Philip, B. M. Buehrer, B. Errede, and D. E. Levin. 1999. Mid2 is a putative sensor for cell integrity signaling in Saccharomyces cerevisiae. Mol. Cell. Biol. 19:3969–3976.
   PubMed Web of Science ®Google Scholar
• Ram, A. F. J., S. S. C. Brekelmans, L. J. W. M. Oehlen, and F. M. Klis. 1995. Identification of two cell cycle regulated genes affecting the β-1,3-glucan content of cell wall in Saccharomyces cerevisiae. FEBS Lett. 358:165–170.
   PubMedGoogle Scholar
• Rose, M. D., F. Winston, and P. Hieter. 1990. Methods in yeast genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y
   Google Scholar
• Schmidt, A., M. Bickle, T. Beck, and M. Hall. 1997. The yeast phosphatidylinositol kinase homolog TOR2 activates RHO1 and RHO2 via the exchange factor ROM2. Cell 88:531–542.
   PubMed Web of Science ®Google Scholar
• Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19–27.
   PubMed Web of Science ®Google Scholar
• Strahl-Bolsinger, S., M. Gentzsch, and W. Tanner. 1999. Protein O-mannosylation. Biochim. Biophys. Acta 1426:297–307.
   PubMed Web of Science ®Google Scholar
• Verna, J., A. Lodder, K. Lee, A. Vagts, and R. Ballester. 1997. A family of genes required for the maintenance of cell wall integrity and for the stress response in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 94:13804–13809.
   PubMed Web of Science ®Google Scholar
• Watanabe, M., C.-Y. Chen, and D. E. Levin. 1994. Saccharomyces cerevisiae PKC1 encodes a protein kinase C (PKC) homolog with a substrate specificity similar to that of mammalian PKC. J. Biol. Chem. 269:16829–16836.
   PubMed Web of Science ®Google Scholar
• Watanabe, Y., G. Takaesu, M. Hagiwara, K. Irie, and K. Matsumoto. 1997. Characterization of a serum response factor-like protein in Saccharomyces cerevisiae, Rlm1, which has transcriptional activity regulated by the Mpk1 (Slt2) mitogen-activated protein kinase pathway. Mol. Cell. Biol. 17:2615–2623.
   PubMedGoogle Scholar
• Zhao, Z.-S., T. Leung, E. Manser, and L. Lim. 1995. Pheromone signaling in Saccharomyces cerevisiae requires the small GTP-binding protein Cdc42p and its activator CDC24. Mol. Cell. Biol. 15:5246–5257.
   PubMedGoogle Scholar