Rvs161p and Sphingolipids Are Required for Actin Repolarization following Salt Stress

Balguerie, Axelle; Bagnat, Michel; Bonneu, Marc; Aigle, Michel; Breton, Annick M.

doi:10.1128/ec.1.6.1021-1031.2002

Cited by 55 publications

(92 citation statements)

References 45 publications

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“…In our studies, the distribution and amounts of Gas1p and Pma1p marker proteins were not altered in sur2D and thus not dependent on C4 hydroxylation of sphingoid bases. Consistent with this result, Balguerie et al [35] found that in intact cells Pma1p tagged with green fluorescent protein is correctly localized at the cell surface in a sur2D mutant, again suggesting that lipid raft delivery of Pma1p is not altered. Nevertheless, preliminary results reveal that a few protein compositional differences occur between the DIGs of sur2D and the isogenic wild-type strain as revealed by two-dimensional differential gel electrophoresis (J. Idkowiak-Baldys, unpublished).…”

Section: Discussionsupporting

confidence: 68%

Sphingolipid C4 hydroxylation influences properties of yeast detergent‐insoluble glycolipid‐enriched membranes

2004

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Sphingoid base C4 hydroxylation is required for syringomycin E action on the yeast plasma membrane. Detergent-insoluble glycolipid-enriched membranes (DIGs) from a yeast strain lacking C4 hydroxylated sphingoid bases (sur2D) are composed of linear membrane fragments instead of vesicular structures observed for wild-type DIGs, though they have similar lipid compositions and amounts of DIG marker proteins. Lightscattering bands collected from sur2D after centrifugation of Triton X-100-treated cell lysates in continuous density gradients have lower buoyant densities than that of the wild-type. The results show that C4 hydroxylation influences the physical and structural properties of DIGs and suggest that syringomycin E interacts with lipid rafts.

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Section: Discussionsupporting

confidence: 68%

Sphingolipid C4 hydroxylation influences properties of yeast detergent‐insoluble glycolipid‐enriched membranes

2004

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“…The plasmid containing a GFP-tagged version of Pma1p was kindly provided by A. Breton (Institut de Biochimie et Genetique Cellulaires, Bordeaux, France) (18). The URA3 marker on this plasmid was switched to LEU2 using the marker swap plasmid pUL9 (19).…”

Section: Methodsmentioning

confidence: 99%

Very Long-chain Fatty Acid-containing Lipids rather than Sphingolipids per se Are Required for Raft Association and Stable Surface Transport of Newly Synthesized Plasma Membrane ATPase in Yeast

Gaigg

Toulmay

Schneiter

2006

Journal of Biological Chemistry

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The proton-pumping H ؉ -ATPase, Pma1p, is an abundant and very long lived polytopic protein of the yeast plasma membrane. Pma1p constitutes a major cargo of the secretory pathway and thus serves as a model to study plasma membrane biogenesis. Pma1p associates with detergent-resistant membrane domains (lipid "rafts") already in the ER, and a lack of raft association correlates with mistargeting of the protein to the vacuole, where it is degraded. We are analyzing the role of specific lipids in membrane domain formation and have previously shown that surface transport of Pma1p is independent of newly synthesized sterols but that sphingolipids with C26 very long chain fatty acid are crucial for raft association and surface transport of Pma1p (Gaigg, B., Timischl, B., Corbino, L., and Schneiter, R. (2005) J. Biol. Chem. 280, 22515-22522). We now describe a more detailed analysis of the function that sphingolipids play in this process. Using a yeast strain in which the essential function of sphingolipids is substituted by glycerophospholipids containing C26 very long chain fatty acids, we find that sphingolipids per se are dispensable for raft association and surface delivery of Pma1p but that the C26 fatty acid is crucial. We thus conclude that the essential function of sphingolipids for membrane domain formation and stable surface delivery of Pma1p is provided by the C26 fatty acid that forms part of the yeast ceramide.

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“…It is postulated that Ssk2p may control the activity of Bni1p and other proteins of the actin cytoskeleton to promote actin repolarization. Rvs161p, organizer of the actin cytoskeleton and component of lipid rafts, has also been shown to play a role in the repolarization of actin following a hyperosmotic shock (7). Finally, Ras2p is necessary for actin repolarization following a mild heat shock (26).…”

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confidence: 99%

“…Stresses include rapid changes in external osmolarity and temperature and insults to the cell wall, to DNA, and to the actin cytoskeleton. Some stresses have pleiotropic effects; for example, hyper-and hypoosmotic stresses cause not only ion imbalance and cell shrinkage or swelling but also a rapid although transient depolarization of the actin cytoskeleton (7,23,26,60). Perturbations of the actin cytoskeleton are known to arrest dividing cells until the damage is repaired (25).…”

mentioning

confidence: 99%

Transcript Profiles of Candida albicans Cortical Actin Patch Mutants Reflect Their Cellular Defects: Contribution of the Hog1p and Mkc1p Signaling Pathways

et al. 2006

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In Candida albicans, Myo5p and Sla2p are required for the polarized localization and function of cortical actin patches, for hyphal formation, and for endocytosis. Deletion of either the MYO5 or the SLA2 gene generated a common transcriptional response that involved changes in the transcript levels of cell wall proteinand membrane protein-encoding genes. However, these profiles were distinct from those observed for a mutant with specific deletions of the actin-organizing domains of Myo5p or for wild-type cells treated with cytochalasin A, both of which also generate defects in the organization of cortical actin patches. The profiles observed for the myo5⌬ and sla2⌬ mutants had similarities to those of wild-type cells subjected to an osmotic shock, and the defects in cortical patch function found with myo5⌬ and sla2⌬ mutants, but not cortical actin patch distribution per se, affected sensitivity to various stresses, including heat and osmotic shocks and cell wall damage. Secondary effects coupled with defective endocytosis, such as lack of polarized lipid rafts and associated protein Rvs167-GFP (where GFP is green fluorescent protein) and lack of polarized wall remodeling protein GFP-Gsc1, were also observed for the myo5⌬ and sla2⌬ mutants. The mitogen-activated protein kinases Hog1p and Mkc1p, which mediate signaling in response to osmotic stress and cell wall damage, do not play a major role in regulating the transcript level changes in the myo5⌬ and sla2⌬ mutants. Hog1p was not hyperphosphorylated in the myo5⌬ and sla2⌬ mutants, and the transcript levels of only a subset of genes affected in the myo5⌬ mutant were dependent upon the presence of Hog1p and Mkc1p. However, it appears that Hog1p and Mkc1p play important roles in the myo5⌬ mutant cells because double deletion of myosin I and either Hog1p or Mkc1p resulted in very-slow-growing cells.

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Rvs161p and Sphingolipids Are Required for Actin Repolarization following Salt Stress

Cited by 55 publications

References 45 publications

Sphingolipid C4 hydroxylation influences properties of yeast detergent‐insoluble glycolipid‐enriched membranes

Sphingolipid C4 hydroxylation influences properties of yeast detergent‐insoluble glycolipid‐enriched membranes

Very Long-chain Fatty Acid-containing Lipids rather than Sphingolipids per se Are Required for Raft Association and Stable Surface Transport of Newly Synthesized Plasma Membrane ATPase in Yeast

Transcript Profiles of Candida albicans Cortical Actin Patch Mutants Reflect Their Cellular Defects: Contribution of the Hog1p and Mkc1p Signaling Pathways

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