Author:
Wloka Carsten,Nishihama Ryuichi,Onishi Masayuki,Oh Younghoon,Hanna Julia,Pringle John R.,Krauß Michael,Bi Erfei
Abstract
AbstractSeptins are essential for cytokinesis inSaccharomyces cerevisiae, but their precise roles remain elusive. Currently, it is thought that before cytokinesis, the hourglass-shaped septin structure at the mother-bud neck acts as a scaffold for assembly of the actomyosin ring (AMR) and other cytokinesis factors. At the onset of cytokinesis, the septin hourglass splits to form a double ring that sandwiches the AMR and may function as diffusion barriers to restrict diffusible cytokinesis factors to the division site. Here, we show that in cells lacking the septin Cdc10 or the septin-associated protein Bud4, the septins form a ring-like structure at the mother-bud neck that fails to re-arrange into a double ring early in cytokinesis. Strikingly, AMR assembly and constriction, the localization of membrane-trafficking and extracellular-matrix-remodeling factors, cytokinesis, and cell-wall-septum formation all occur efficiently incdc10Δandbud4Δmutants. Thus, diffusion barriers formed by the septin double ring do not appear to be critical forS. cerevisiaecytokinesis. However, an AMR mutation and a septin mutation have synergistic effects on cytokinesis and the localization of cytokinesis proteins, suggesting that tethering to the AMR and a septin diffusion barrier may function redundantly to localize proteins to the division site.
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
Cited by
77 articles.
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