The protein kinase Kic1 affects 1,6-β-glucan levels in the cell wall of Saccharomyces cerevisiae

Vink, Erik P. de; Vossen, Jack H.; Ende, H. van den; Brekelmans, S.S.C.; Nobel, Hans de; Klis, Frans M.

doi:10.1099/00221287-148-12-4035

Cited by 16 publications

(21 citation statements)

References 54 publications

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“…In fact, some cell wall-related mutants that display a constitutive high level of Slt2 phosphorylation, such as gas1, ecm33, itc1, or rot2, have been shown to be hypersensitive to Calcofluor White, a compound that interferes with cell wall assembly in a similar way to Congo Red (4,38). In agreement with a role for MSG5 in modulating cell wall-related cellular signaling, this gene has recently been isolated as a multicopy suppressor of the Calcofluor White sensitivity of cells overexpressing KIC1, a gene encoding a protein kinase involved in cell wall integrity (39).…”

Section: Discussionmentioning

confidence: 97%

Reciprocal Regulation between Slt2 MAPK and Isoforms of Msg5 Dual-specificity Protein Phosphatase Modulates the Yeast Cell Integrity Pathway

Flández

Cosano

Nombela

et al. 2004

Journal of Biological Chemistry

101

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Dual-specificity protein phosphatases (DSPs) are involved in the negative regulation of mitogen-activated protein kinases (MAPKs) by dephosphorylating both threonine-and tyrosine-conserved residues located at the activation loop. Here we show that Msg5 DSP activity is essential for maintaining a low level of signaling through the cell integrity pathway in Saccharomyces cerevisiae. Consistent with a role of this phosphatase on cell wall physiology, cells lacking Msg5 displayed an increased sensitivity to the cell wall-interfering compound Congo Red. We have observed that the N-terminal non-catalytic region of this phosphatase was responsible for binding to the kinase domain of Slt2, the MAPK that operates in this pathway. In vivo and in vitro experiments revealed that both proteins act on each other. Msg5 bound and dephosphorylated activated Slt2. Reciprocally, Slt2 phosphorylated Msg5 as a consequence of the activation of the cell integrity pathway. In addition, alternative use of translation initiation sites at MSG5 resulted in two protein forms that are functional on Slt2 and became equally phosphorylated following activation of this MAPK. Under activating conditions, a decrease in the affinity between Msg5 and Slt2 was observed, leading us to suggest that the mechanism by which Slt2 controls the action of Msg5 was via the modulation of protein-protein interactions. Our results indicate the existence of posttranscriptional mechanisms of regulation of DSPs in yeast and provide new insights into the negative control of the cell integrity pathway.

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Section: Discussionmentioning

confidence: 97%

Reciprocal Regulation between Slt2 MAPK and Isoforms of Msg5 Dual-specificity Protein Phosphatase Modulates the Yeast Cell Integrity Pathway

Flández

Cosano

Nombela

et al. 2004

Journal of Biological Chemistry

101

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“…The kic1 gene is essential and its mutants show morphological defects and cell-wall alterations. The defects include thicker cell walls, cell lysis, F-actin changes at the bud neck and growth in unseparated chains or clusters, which indicate a separation defect (Sullivan et al, 1998;Vink et al, 2002). Several other genes have been identified that might contribute to the same regulatory pathway as Nak1/Orb3 because their deletion phenotypes are very similar to that of nak1/orb3.…”

Section: Discussionmentioning

confidence: 98%

Ste20/GCK kinase Nak1/Orb3 polarizes the actin cytoskeleton in fission yeast during the cell cycle

Leonhard

Nurse

2005

Journal of Cell Science

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Polar growth is a crucial process during cell morphogenesis. The microtubule and actin cytoskeletons, and vesicular transport are tightly regulated to direct cellular growth and to generate specific cell forms. We demonstrate here that the Ste20-related protein kinase Nak1/Orb3 is required in fission yeast to polarize the actin cytoskeleton at the tips of the cells and for cell separation, and so is involved in controlling both cell shape and late stages of cytokinesis. The localization of the Nak1/Orb3 kinase to the cell tips, a medial ring and the spindle-pole bodies changes during the cell cycle, and the accumulation of F-actin at the cell tips is dependent on Nak1/Orb3 kinase. The phosphorylation of Nak1/Orb3 is periodic during the cell cycle and could be part of a mechanism that relocalizes a constitutively active kinase from the cell tips to the middle of the cell, thereby coordinating reorganization of the actin cytoskeleton and regulation of cell separation with cell-cycle progression.

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“…The resistance has been attributed to changes in the mannoprotein layer (Vink et al, 2002), with a specific function for some of the cell-wall proteins (Van Der Vaart et al, 1995). In mutant scw4scw10, zymolyase resistance is not lost after deletion of CHS3.…”

Section: Discussionmentioning

confidence: 99%

Scw10p, a cell-wall glucanase/transglucosidase important for cell-wall stability in Saccharomyces cerevisiae

et al. 2004

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Glycosyl hydrolases and transferases are crucial for the formation of a rigid but at the same time plastic cell wall in yeasts and fungi. The Saccharomyces cerevisiae glucan hydrolase family 17 (GH17) contains the soluble cell-wall proteins Scw4p, Scw10p, Scw11p and Bgl2p. For Bgl2p, endoglucanase/glucanosyltransferase activity has been demonstrated, and Scw11p has been shown to be involved in cell separation. Here, Scw4p and Scw10p, which show 63 % amino acid identity, were characterized. scw4 and scw10 single mutants were sensitive towards cell-wall destabilizing agents, suggesting a role in cell-wall assembly or maintenance. Simultaneous deletion of SCW4 and SCW10 showed a synergistic effect, and activated the cell-wall compensatory mechanism in a PKC1-dependent manner. Both the amount of cell-wall chitin and the amount of mannoproteins attached to chitin were increased in mutant scw4scw10. Deletion of CHS3 proved the critical role of chitin in scw4scw10. However, the mannoprotein Sed1p and the glucan synthase Fks2p were also crucial for cell-wall stability in mutant scw4scw10. The exchange of two conserved glutamate residues localized in the putative catalytic domain of GH17 family members strongly suggests that Scw10p acts as a 1,3-b-glucanase or as a 1,3-b-glucanosyltransferase. In addition, the synthetic interactions between Bgl2p and Scw10p which support a functional cooperation in cell-wall assembly were analysed. The data suggest that Scw4p and Scw10p act as glucanases or transglucosidases in concert with other cell-wall proteins to assure cell-wall integrity.

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The protein kinase Kic1 affects 1,6-β-glucan levels in the cell wall of Saccharomyces cerevisiae

Cited by 16 publications

References 54 publications

Reciprocal Regulation between Slt2 MAPK and Isoforms of Msg5 Dual-specificity Protein Phosphatase Modulates the Yeast Cell Integrity Pathway

Reciprocal Regulation between Slt2 MAPK and Isoforms of Msg5 Dual-specificity Protein Phosphatase Modulates the Yeast Cell Integrity Pathway

Ste20/GCK kinase Nak1/Orb3 polarizes the actin cytoskeleton in fission yeast during the cell cycle

Scw10p, a cell-wall glucanase/transglucosidase important for cell-wall stability in Saccharomyces cerevisiae

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