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dc.contributor.advisorSawin, Kenen
dc.contributor.advisorGoryachev, Andrewen
dc.contributor.authorMutavchiev, Delyan Rumenoven
dc.date.accessioned2018-03-27T12:12:39Z
dc.date.available2018-03-27T12:12:39Z
dc.date.issued2017-07-07
dc.identifier.urihttp://hdl.handle.net/1842/29006
dc.description.abstractCell polarisation is a key biological process crucial for the functioning of essentially all cells. Regulation of cell polarity is achieved through various processes determined by both internal and external factors. An example of the latter is that cell polarity can be disrupted or lost as a consequence of a variety of external stresses. When facing such stresses, cells adapt to unfavourable conditions by activating a range of molecular signalling pathways, collectively termed ‘stress response’. Despite the connections between external stress and cell polarity, whether stress-response signalling regulates cell polarisation and what the molecular basis for such regulation remains an open question. The fission yeast Schizosaccharomyces pombe presents an excellent biological platform to study the complexity of cell polarity regulation on a systematic level. This study is aimed at understanding the functional relationship between stress-response signalling and maintenance of cell polarity in this model organism. The findings presented in this thesis set the basis for establishing a functional link between the activation of the S.pombe stress-response pathway and the activity of the master regulator of cell polarity- the Rho GTPase Cdc42. Here, I describe experiments that identify an active involvement of the stress-response mitogen-activated kinase (MAPK) Sty1 in the dispersal of active Cdc42 from the sites of growth. This new role for Sty1 occurs independently from its involvement in transcription regulation and other previously identified signalling pathways involving Sty1. Furthermore, I also find that Sty1’s involvement in Cdc42 regulation has direct implications for fission yeast physiology as it is essential for the maintenance of cellular quiescence upon nitrogen starvation. This thesis also focuses on identifying the targets of Sty1 orchestrating the active Cdc42 disruption. Here, I describe a candidate-based approach, where I investigate the role of proteins from the Cdc42 regulatory network during Sty1 activation. Additionally, I present a global phospho-proteomics approach to identify novel targets of Sty1 and offer preliminary findings which might explain Sty1’s involvement in Cdc42 regulation.en
dc.contributor.sponsorWellcome Trusten
dc.language.isoen
dc.publisherThe University of Edinburghen
dc.relation.hasversionMutavchiev, D.R., Leda, M., Sawin, K.E, Remodeling of the fission yeast Cdc42 cell polarity module via the Sty1 p38 stress-activated protein kinase pathway. (Current Biology, 2016)en
dc.subjectcell polarityen
dc.subjectstress responseen
dc.subjectfission yeasten
dc.subjectSty1en
dc.subjectstress-response proteinen
dc.subjectCdc42en
dc.titleRegulation of fission yeast cell polarity by stress-response pathwaysen
dc.typeThesis or Dissertationen
dc.type.qualificationlevelDoctoralen
dc.type.qualificationnamePhD Doctor of Philosophyen
dc.rights.embargodate2100-12-31
dcterms.accessRightsRestricted Accessen


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