The cell wall sensor Wsc1p is involved in reorganization of actin cytoskeleton in response to hypo-osmotic shock in Saccharomyces cerevisiae.
The cell wall is essential to preserve osmotic integrity of yeast cells. Some phenotypic traits of cell wall mutants suggest that, as a result of a weakening of the cell wall, hypo-osmotic stress-like conditions are created. Consequent expansion of the cell wall and stretching of the plasma membrane trigger a complex response to prevent cell lysis. In this work we examined two conditions that generate a cell wall and membrane stress: one is represented by the cell wall mutant gas1Delta and the other by a hypo-osmotic shock. We examined the actin cytoskeleton and the role of the cell wall sensors Wsc1p and Mid2p in these stress conditions. In the gas1 null mutant cells, which lack a beta(1,3)-glucanosyltransferase activity required for cell wall assembly, a constitutive marked depolarization of actin cytoskeleton was found. In a hypo-osmotic shock wild-type cells showed a transient depolarization of actin cytoskeleton. The percentage of depolarized cells was maximal at 30 min after the shift and then progressively decreased until cells reached a new steady-state condition. The maximal response was proportional to the magnitude of the difference in the external osmolarity before and after the shift within a given range of osmolarities. Loss of Wsc1p specifically delayed the repolarization of the actin cytoskeleton, whereas Wsc1p and Mid2p were essential for the maintenance of cell integrity in gas1Delta cells. The control of actin cytoskeleton is an important element in the context of the compensatory response to cell wall weakening. Wsc1p appears to be an important regulator of the actin network rearrangements in conditions of cell wall expansion and membrane stretching.
Dipartimento di Scienze Biomolecolari e Biotecnologie, Università degli Studi di Milano, Via Celoria 26, 20133 Milano, Italy.
Tania
T
Gualtieri
Enrico
E
Ragni
Luca
L
Mizzi
Umberto
U
Fascio
Laura
L
Popolo
D000199:Actins / Q000502:physiology*; D001557:Benzenesulfonates / Q000494:pharmacology; D002110:Caffeine / Q000494:pharmacology; D002135:Calcium-Binding Proteins / Q000502:physiology; D016764:Cell Polarity / Q000502:physiology; D002470:Cell Survival / Q000502:physiology; D002686:Chitin / Q000032:analysis; D003599:Cytoskeleton / Q000502:physiology*; D005936:Glucans / Q000032:analysis; D047908:Intracellular Signaling Peptides and Proteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000502:physiology*; D018613:Microscopy, Confocal; D016254:Mutagenesis, Insertional; D009997:Osmotic Pressure; D012441:Saccharomyces cerevisiae / Q000502:physiology*; D029701:Saccharomyces cerevisiae Proteins / Q000502:physiology*; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology
D000199:Actins; D001557:Benzenesulfonates; D002135:Calcium-Binding Proteins; D005936:Glucans; D047908:Intracellular Signaling Peptides and Proteins; C091625:MID2 protein, S cerevisiae; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; C119383:SLG1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D002686:Chitin; D012967:Sodium Dodecyl Sulfate; D002110:Caffeine; C007061:C.I. Fluorescent Brightening Agent 28