Roles of secretion and the cytoskeleton in cell adhesion and polarity establishment in Pelvetia compressa zygotes.
During the establishment of polarity, fucoid algal zygotes adhere to the substratum and select a growth axis according to environmental cues. Since little is known about the early events leading to axis selection, we investigated the chronology of cell adhesion, adhesive deposition, and axis selection induced by light (photopolarization). The requirements for secretion and the cytoskeleton in these processes and in the process of changing the orientation of an axis in response to new environmental cues (axis realignment) were also tested. Adhesive deposition occurred in two distinct stages: it was deposited uniformally on young zygotes (uniform primary adhesive) and later was deposited asymmetrically (polar secondary adhesive). Uniform primary adhesive deposition, cell adhesion, and photopolarization occurred simultaneously, and shortly thereafter, polar secondary adhesive deposition occurred at the future growth site. Uniform primary adhesive deposition and cell adhesion required secretion, but were independent of filamentous-actin (F-actin) and microtubule function. Photopolarization of young zygotes and polar secondary adhesive deposition required secretion but not microtubules. F-actin served to localize secondary adhesive deposition at the rhizoid pole; its function in polarization was more complex. F-actin was required for axis selection; however, its role in realignment of an axis depended on the light regime. The differing requirements for F-actin during development indicates that the axis is not static, but changes with time. These findings indicate that previous and future work on "axis formation" must be interpreted in the context of the developmental stage of the zygote.
Hable
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Department of Biology, University of Utah, Salt Lake City 84112-0840, USA. hable@biology.utah.edu
Kropf
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D000199:Actins / Q000502:physiology; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D012634:Bodily Secretions / Q000502:physiology*; D020126:Brefeldin A; D019086:Bridged Bicyclo Compounds, Heterocyclic / Q000494:pharmacology; D002448:Cell Adhesion / Q000502:physiology*; D003517:Cyclopentanes / Q000494:pharmacology; D015638:Cytochalasin D / Q000494:pharmacology; D003599:Cytoskeleton / Q000502:physiology*; D004136:Dinitrobenzenes / Q000494:pharmacology; D056890:Eukaryota / Q000502:physiology*; D008027:Light; D018942:Macrolides; D018613:Microscopy, Confocal; D008985:Monensin / Q000494:pharmacology; D013424:Sulfanilamides; D013844:Thiazoles / Q000494:pharmacology; D053778:Thiazolidines; D015053:Zygote / Q000166:cytology / Q000254:growth & development*
D000199:Actins; D000900:Anti-Bacterial Agents; D019086:Bridged Bicyclo Compounds, Heterocyclic; D003517:Cyclopentanes; D004136:Dinitrobenzenes; D018942:Macrolides; D013424:Sulfanilamides; D013844:Thiazoles; D053778:Thiazolidines; D020126:Brefeldin A; D015638:Cytochalasin D; C012465:oryzalin; D008985:Monensin; C037068:latrunculin B