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Verfasst von:Maier, Peter [VerfasserIn]   i
 Finkbeiner, Martin G. [VerfasserIn]   i
 Taxis, Christof [VerfasserIn]   i
 Knop, Michael [VerfasserIn]   i
Titel:Cytokinesis in yeast meiosis depends on the regulated removal of Ssp1p from the prospore membrane
Verf.angabe:Peter Maier, Nicole Rathfelder, Martin G. Finkbeiner, Christof Taxis, Massimiliano Mazza, Sophie Le Panse, Rosine Haguenauer‐Tsapis and Michael Knop
Umfang:10 S.
Fussnoten:Gesehen am 16.08.2017
Titel Quelle:Enthalten in: European Molecular Biology Organization: The EMBO journal
Jahr Quelle:2007
Band/Heft Quelle:26(2007), 7, S. 1843-1852
ISSN Quelle:1460-2075
Abstract:Intracellular budding is a developmentally regulated type of cell division common to many fungi and protists. In Saccaromyces cerevisiae, intracellular budding requires the de novo assembly of membranes, the prospore membranes (PSMs) and occurs during spore formation in meiosis. Ssp1p is a sporulation‐specific protein that has previously been shown to localize to secretory vesicles and to recruit the leading edge protein coat (LEP coat) proteins to the opening of the PSM. Here, we show that Ssp1p is a multidomain protein with distinct domains important for PI(4,5)P2 binding, binding to secretory vesicles and inhibition of vesicle fusion, interaction with LEP coat components and that it is subject to sumoylation and degradation. We found non‐essential roles for Ssp1p on the level of vesicle transport and an essential function of Ssp1p to regulate the opening of the PSM. Together, our results indicate that Ssp1p has a domain architecture that resembles to some extent the septin class of proteins, and that the regulated removal of Ssp1p from the PSM is the major step underlying cytokinesis in yeast sporulation.
DOI:doi:10.1038/sj.emboj.7601621
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Kostenfrei: Verlag: http://dx.doi.org/10.1038/sj.emboj.7601621
 Kostenfrei: Verlag: http://embojnl.embopress.org/content/26/7/1843
 DOI: https://doi.org/10.1038/sj.emboj.7601621
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1562463063
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