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Microcompartmentation of cell wall integrity sensors in Saccharomyces cerevisiae

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https://osnadocs.ub.uni-osnabrueck.de/handle/urn:nbn:de:gbv:700-2016080514803
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dc.contributor.advisorProf. Dr. Jürgen J. Heinisch
dc.creatorKock, Christian
dc.date.accessioned2016-08-05T09:27:13Z
dc.date.available2016-08-05T09:27:13Z
dc.date.issued2016-08-05T09:27:13Z
dc.identifier.urihttps://osnadocs.ub.uni-osnabrueck.de/handle/urn:nbn:de:gbv:700-2016080514803-
dc.description.abstractThe ability to adapt to changing environments is a key feature of living cells which is usually mediated by signal transduction pathways. One of these pathways in Saccharomyces cerevisiae maintains the proper cell wall composition under cell wall remodeling and stress conditions which ensures cell shape and integrity. The pathway is hence commonly referred to as cell wall integrity (CWI) pathway. Five plasma membrane sensors detect surface stress and activate a conserved MAPK cascade through Rom2, Rho1 and Pkc1. Downstream of the cascade, Slt2 activates the transcription factors Rlm1 and SBF. These regulate the expression of genes which are involved in cell wall synthesis and cell cycle control, respectively. The sensors can be grouped into two protein families with Wsc1, Wsc2 and Wsc3 on the one hand and Mid2 and Mtl1 on the other hand. They all contain a highly mannosylated extracellular serine/threonine-rich region (STR), a single transmembrane domain and a cytoplasmic tail. Whereas Wsc-family sensors carry an additional cysteine-rich domain (CRD) headgroup, Mid2 and Mtl1 are N-glycosylated at an asparagine (Kock et al., 2015). A strain deleted in all five sensor genes is not viable and WSC1, WSC2 and MID2 are the main sensor genes to mediate the stress response. Wsc1 and Mid2 show non-overlapping spot-like and network-like localization patterns in the plasma membrane, respectively, whose formation is not governed by their transmembrane domains. Colocalization studies with marker proteins of the known yeast plasma membrane domains “membrane compartment occupied by Can1” (MCC), “membrane compartment occupied by Pma1” (MCP) and the “membrane compartment of the TOR2 complex” (MCT) revealed that Wsc1 forms a distinct plasma membrane domain which is here introduced as “membrane compartment occupied by Wsc1“ (MCW). This microcompartment depends on the cysteine-rich domain (CRD) as sensors mutated in this headgroup accumulate in the vacuole. Blocking endocytosis either by an end3 deletion or by mutation of the NPFDD endocytosis signal in the cytoplasmic tail of Wsc1 restores its signaling function but displays an altered pattern of membrane distribution, changing from spot-like in wild-type to network-like in the mutants. This indicated that clustering may protect the sensor from endocytosis. In addition, Wsc1 has amyloid-like properties suggesting a role in clustering. Accordingly, protein aggregation (clustering) is lost in a mutant of a predicted amyloid motif within the CRD, which also impairs Wsc1 signaling.eng
dc.rightsNamensnennung 3.0 Unported-
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/-
dc.subjectHefeger
dc.subjectyeasteng
dc.subjectSaccharomyces cerevisiaeger
dc.subjectSaccharomyces cerevisiaeeng
dc.subjectZellwandger
dc.subjectcell walleng
dc.subjectZellwandintegritätger
dc.subjectcell wall integrityeng
dc.subjectSensorger
dc.subjectsensoreng
dc.subjectZellrezeptorger
dc.subjectcell receptoreng
dc.subjectMembranproteinger
dc.subjectmembrane proteineng
dc.subjectPlasmamembranger
dc.subjectplasma membraneeng
dc.subjectMembrandomänenger
dc.subjectmembrane domainseng
dc.subjectMAP-Kinaseger
dc.subjectMAP-kinaseeng
dc.subjectWsc1ger
dc.subjectWsc1eng
dc.subjectAmyloidger
dc.subjectamyloideng
dc.subjectMikroskopieger
dc.subjectmicroscopyeng
dc.subject.ddc570 - Biowissenschaften; Biologie
dc.titleMicrocompartmentation of cell wall integrity sensors in Saccharomyces cerevisiaeeng
dc.title.alternativeMikrokompartimentierung von Zellwandintegritätssensoren in Saccharomyces cerevisiaeger
dc.typeDissertation oder Habilitation [doctoralThesis]-
thesis.locationOsnabrück-
thesis.institutionUniversität-
thesis.typeDissertation [thesis.doctoral]-
thesis.date2016-06-16-
dc.contributor.refereeProf. Dr. Achim Paululat
dc.subject.bk42.20 - Genetik
dc.subject.bk42.15 - Zellbiologie
dc.subject.bk42.13 - Molekularbiologie
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