Characterization of the essential role of Ynl152/Inn1 in cell division in Saccharomyces cerevisiae

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dc.contributor.advisorProf. Dr. Jürgen J. Heinisch
dc.creatorJendretzki, Arne
dc.description.abstractThe essential open reading frame YNL152w (now called INN1) of Saccharomyces cerevisiae was previously identified in a screen for negative regulators of cell integrity signaling. Subsequent studies and data from genome-wide functional analyses suggested, that the encoded protein plays a role in cell division. This was further addressed in the thesis presented here. Functional Inn1-GFP fusions were shown to co-localize with the contractile actomyosin ring component Myo1 during cytokinesis. Mutants depleted for Inn1 failed to form a primary septum, but did not affect the dynamics of the cytokinetic actin ring (CAR). This has been attributed to the inability to couple plasma membrane ingression (hence Inn1) to CAR constriction, a phenomenon also found by Sanchez-Diaz et al. (2008). Further investigations focused on the question of how Inn1 is recruited to the bud neck and identified the cytokinetic regulators Hof1 and Cyk3, which act in concert for this purpose. Each of them contains a SH3 domain, which interacts with the proline-rich carboxy-terminal part of Inn1. Localization studies and genetic analyses indicate that Inn1 acts downstream of Hof1 and Cyk3. Either the simultaneous repression of HOF1 and CYK3 gene expression or the deletion of their SH3 domains was lethal, with a concomitant failure to localize Inn1-GFP to the division site. Overproduction of either, Hof1 or Cyk3 perturbed the dynamics of Inn1-GFP distribution, which followed that of the overproduced proteins. This atypical CAR-independent localization of Inn1 supports a presumed role of Hof1 and Cyk3 in an alternative cytokinesis pathway to form a primary septum. Since INN1 is also a multicopy suppressor of a myo1 deletion, this further supports the notion that Inn1 may be required for plasma membrane ingression, also in CAR-independent cytokinesis. Preliminary data suggest, that the protein Vrp1 is responsible for the required removal of Inn1 from the bud neck after completion of cytokinesis. The essential amino-terminal C2 domain of Inn1 may mediate plasma membrane ingression by interaction with the membrane lipid phosphatidic acid, observed in biochemical studies. Alternatively, the C2 domain has been suggested to modulate chitin synthesis in the primary septum by modulating Chs2 activity (Nishihama et al., 2009).eng
dc.subject.ddc570 - Biowissenschaften; Biologie
dc.subject.ddc570 - Biowissenschaften; Biologie
dc.titleCharacterization of the essential role of Ynl152/Inn1 in cell division in Saccharomyces cerevisiaeeng
dc.typeDissertation oder Habilitation [doctoralThesis]-
thesis.typeDissertation [thesis.doctoral]-
dc.contributor.refereeapl. Prof. Dr. Hans Merzendorfer
Appears in Collections:FB05 - E-Dissertationen

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